BRENDA - Enzyme Database
show all sequences of 2.7.3.2

Cellular compartmentation of energy metabolism: creatine kinase microcompartments and recruitment of B-type creatine kinase to specific subcellular sites

Schlattner, U.; Klaus, A.; Ramirez Rios, S.; Guzun, R.; Kay, L.; Tokarska-Schlattner, M.; Amino Acids 48, 1751-1774 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene Ckb, brain cDNA library screening for enzyme interaction partners
Rattus norvegicus
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of an N-terminally trucated isozyme BCK
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoskeleton
recruitment of BCK to submembrane domains, formation of dynamic actin-based protrusions
Mus musculus
5856
-
cytosol
cytosolic brain-type creatine kinase
Mus musculus
5829
-
cytosol
cytosolic brain-type creatine kinase, mainly soluble brain BCK
Rattus norvegicus
5829
-
endoplasmic reticulum
-
Mus musculus
5783
-
endoplasmic reticulum
isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
Rattus norvegicus
5783
-
membrane
; association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions
Mus musculus
16020
-
membrane
association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
Rattus norvegicus
16020
-
mitochondrial inner membrane
-
Mus musculus
5743
-
mitochondrial outer membrane
-
Mus musculus
5741
-
mitochondrion
association with by brain-type creatine kinase; octameric MtCK is situated in the mitochondrial intermembrane space, binding simultaneously to both mitochondrial inner and outer membranes, as well as in the cristae space bound to inner membrane
Mus musculus
5739
-
mitochondrion
-
Rattus norvegicus
5739
-
additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview; the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
Mus musculus
-
-
additional information
as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
Rattus norvegicus
-
-
nucleus
-
Mus musculus
5634
-
plasma membrane
-
Mus musculus
5886
-
synaptic vesicle
association with by brain-type creatine kinase
Mus musculus
8021
-
synaptic vesicle
association with by brain-type creatine kinase, isolated from rat forebrains by separation from nerve-ending particles (synaptosomes). Synaptic vesicle BCK is indeed firmly anchored in the vesicle membrane and not just interacting electrostatically with the lipid headgroups or simply enclosed within the vesicles
Rattus norvegicus
8021
-
synaptosome
-
Rattus norvegicus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required; required
Mus musculus
Mg2+
required
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + creatine
Mus musculus
-
ADP + phosphocreatine
-
-
r
ATP + creatine
Rattus norvegicus
-
ADP + phosphocreatine
-
-
r
ATP + creatine
Mus musculus
the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter
ADP + phosphocreatine
-
-
r
ATP + creatine
Rattus norvegicus Wistar
-
ADP + phosphocreatine
-
-
r
additional information
Mus musculus
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
?
-
-
-
additional information
Rattus norvegicus
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
?
-
-
-
additional information
Rattus norvegicus Wistar
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mus musculus
P30275
U-type creatine kinase; gene Ckmt1
-
Mus musculus
Q04447
B-type creatine kinase; gene Ckb
-
Rattus norvegicus
P07335
B-type creatine kinase; gene Ckb
-
Rattus norvegicus Wistar
P07335
B-type creatine kinase; gene Ckb
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump
Mus musculus
phosphoprotein
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. BCK phosphorylation is a regulatory process for cellular localization that involves a particular physiological signal (energy stress) which is highly specific for a defined protein kinase (AMPK) and a specific BCK site (Ser6), and provides colocalization between BCK and an ATPase
Rattus norvegicus
Purification (Commentary)
Commentary
Organism
native isozyme BCK in synaptic vesicles and membranes of neuronal synaptosomes and mitochondria
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
astrocyte
;
Mus musculus
-
brain
cytosolic brain-type cratine kinase; cytosolic brain-type creatine kinase, the CK energy buffering and shuttle system seems to operate in many brain cells, in particular in the polarized large cells like neurons or hair bundle and photoreceptor cells in the sensory organs
Mus musculus
-
brain
-
Rattus norvegicus
-
fibroblast
-
Mus musculus
-
forebrain
-
Rattus norvegicus
-
additional information
in a given cell type, at least one dimeric cytosolic isoform is always co-expressed with a predominantly octameric mitochondrial isoform (MtCK), generally cytosolic muscle-type CK (MCK) with sarcomeric MtCK (sMtCK), or cytosolic brain-type CK (BCK) with ubiquitous MtCK; in a given cell type, at least one dimeric cytosolic isoform is always co-expressed with a predominantly octameric mitochondrial isoform (MtCK), generally cytosolic muscle-type CK (MCK) with sarcomeric MtCK (sMtCK), or cytosolic brain-type CK (BCK) with ubiquitous MtCK
Mus musculus
-
additional information
no expression of BCK in liver
Rattus norvegicus
-
myotube
in cultured mouse myotubes, BCK localizes near the endings of the cells, interaction with skeletal and cardiac alpha-actin
Mus musculus
-
photoreceptor cell
-
Mus musculus
-
retina
-
Mus musculus
-
stomach
parietal cells of the stomach, BCK is co-localizing with and fueling the gastric H+/K+-ATPase pump at the apical membrane and the membranes of the tubulovesicular system
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + creatine
-
737427
Mus musculus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
-
737427
Rattus norvegicus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter
737427
Mus musculus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
-
737427
Rattus norvegicus Wistar
ADP + phosphocreatine
-
-
-
r
additional information
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
737427
Mus musculus
?
-
-
-
-
additional information
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
737427
Rattus norvegicus
?
-
-
-
-
additional information
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
737427
Rattus norvegicus Wistar
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
cytosolic isozyme
Mus musculus
octamer
mitochondrial isozyme; mitochondrial isozyme
Mus musculus
octamer
mitochondrial isozyme
Rattus norvegicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
11.5
assay at
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
ADP
;
Mus musculus
ADP
-
Rattus norvegicus
ATP
;
Mus musculus
ATP
-
Rattus norvegicus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Ckb, brain cDNA library screening for enzyme interaction partners
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ADP
-
Mus musculus
ADP
-
Rattus norvegicus
ATP
-
Mus musculus
ATP
-
Rattus norvegicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of an N-terminally trucated isozyme BCK
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoskeleton
recruitment of BCK to submembrane domains, formation of dynamic actin-based protrusions
Mus musculus
5856
-
cytosol
cytosolic brain-type creatine kinase
Mus musculus
5829
-
cytosol
cytosolic brain-type creatine kinase, mainly soluble brain BCK
Rattus norvegicus
5829
-
endoplasmic reticulum
-
Mus musculus
5783
-
endoplasmic reticulum
isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
Rattus norvegicus
5783
-
membrane
association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions
Mus musculus
16020
-
membrane
-
Mus musculus
16020
-
membrane
association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
Rattus norvegicus
16020
-
mitochondrial inner membrane
-
Mus musculus
5743
-
mitochondrial outer membrane
-
Mus musculus
5741
-
mitochondrion
association with by brain-type creatine kinase
Mus musculus
5739
-
mitochondrion
octameric MtCK is situated in the mitochondrial intermembrane space, binding simultaneously to both mitochondrial inner and outer membranes, as well as in the cristae space bound to inner membrane
Mus musculus
5739
-
mitochondrion
-
Rattus norvegicus
5739
-
additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview
Mus musculus
-
-
additional information
the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
Mus musculus
-
-
additional information
as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
Rattus norvegicus
-
-
nucleus
-
Mus musculus
5634
-
plasma membrane
-
Mus musculus
5886
-
synaptic vesicle
association with by brain-type creatine kinase
Mus musculus
8021
-
synaptic vesicle
association with by brain-type creatine kinase, isolated from rat forebrains by separation from nerve-ending particles (synaptosomes). Synaptic vesicle BCK is indeed firmly anchored in the vesicle membrane and not just interacting electrostatically with the lipid headgroups or simply enclosed within the vesicles
Rattus norvegicus
8021
-
synaptosome
-
Rattus norvegicus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Mus musculus
Mg2+
required
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + creatine
Mus musculus
-
ADP + phosphocreatine
-
-
r
ATP + creatine
Rattus norvegicus
-
ADP + phosphocreatine
-
-
r
ATP + creatine
Mus musculus
the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter
ADP + phosphocreatine
-
-
r
ATP + creatine
Rattus norvegicus Wistar
-
ADP + phosphocreatine
-
-
r
additional information
Mus musculus
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
?
-
-
-
additional information
Rattus norvegicus
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
?
-
-
-
additional information
Rattus norvegicus Wistar
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump
Mus musculus
phosphoprotein
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. BCK phosphorylation is a regulatory process for cellular localization that involves a particular physiological signal (energy stress) which is highly specific for a defined protein kinase (AMPK) and a specific BCK site (Ser6), and provides colocalization between BCK and an ATPase
Rattus norvegicus
Purification (Commentary) (protein specific)
Commentary
Organism
native isozyme BCK in synaptic vesicles and membranes of neuronal synaptosomes and mitochondria
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
astrocyte
-
Mus musculus
-
brain
cytosolic brain-type creatine kinase, the CK energy buffering and shuttle system seems to operate in many brain cells, in particular in the polarized large cells like neurons or hair bundle and photoreceptor cells in the sensory organs
Mus musculus
-
brain
cytosolic brain-type cratine kinase
Mus musculus
-
brain
-
Rattus norvegicus
-
fibroblast
-
Mus musculus
-
forebrain
-
Rattus norvegicus
-
additional information
in a given cell type, at least one dimeric cytosolic isoform is always co-expressed with a predominantly octameric mitochondrial isoform (MtCK), generally cytosolic muscle-type CK (MCK) with sarcomeric MtCK (sMtCK), or cytosolic brain-type CK (BCK) with ubiquitous MtCK
Mus musculus
-
additional information
no expression of BCK in liver
Rattus norvegicus
-
myotube
in cultured mouse myotubes, BCK localizes near the endings of the cells, interaction with skeletal and cardiac alpha-actin
Mus musculus
-
photoreceptor cell
-
Mus musculus
-
retina
-
Mus musculus
-
stomach
parietal cells of the stomach, BCK is co-localizing with and fueling the gastric H+/K+-ATPase pump at the apical membrane and the membranes of the tubulovesicular system
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + creatine
-
737427
Mus musculus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
-
737427
Rattus norvegicus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter
737427
Mus musculus
ADP + phosphocreatine
-
-
-
r
ATP + creatine
-
737427
Rattus norvegicus Wistar
ADP + phosphocreatine
-
-
-
r
additional information
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
737427
Mus musculus
?
-
-
-
-
additional information
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
737427
Rattus norvegicus
?
-
-
-
-
additional information
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
737427
Rattus norvegicus Wistar
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
cytosolic isozyme
Mus musculus
octamer
mitochondrial isozyme
Mus musculus
octamer
mitochondrial isozyme
Rattus norvegicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
11.5
assay at
Rattus norvegicus
General Information
General Information
Commentary
Organism
malfunction
knockout mice that lack the brain CK isoforms, i.e. BCK and/or ubiquitous MtCK, uMtCK, show defects in spatial memory acquisition and behavior, development of the hippocampus, correct functioning of hair bundle cells in the auditory system, and energy distribution within photoreceptor cells, transgenic models of creatine deficiency, overview; knockout mice that lack the brain CK isoforms, i.e. BCK and/or ubiquitous MtCK, uMtCK, show defects in spatial memory acquisition and behavior, development of the hippocampus, correct functioning of hair bundle cells in the auditory system, and energy distribution within photoreceptor cells, transgenic models of creatine deficiency, overview
Mus musculus
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability; importance of functional coupling between MtCK, ANT and respiration/ATP synthesis provided by the close co-localization of MtCK and ANT in proteolipid complexes. Co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability
Mus musculus
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. spatial organization of the CK/PCr shuttle in brain, in particular the association of BCK to subcellular components as well as to specific, interacting proteins, overview
Rattus norvegicus
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP; phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
Mus musculus
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
Rattus norvegicus
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump. In retina photoreceptor cells, BCK may play an equally important role, but rather in synaptic transmission at the synaptic terminal or for cGMP resynthesis in the rod outer segments. In astrocytes and fibroblasts, BCK in peripheral cellular structures facilitates actin-driven cell spreading and migration; creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. The role of MtCK within the mitochondrial interactosome is to separate energy fluxes from the intracellular energy signals and to amplify these signals due to the intramitochondrial recycling of ADP
Mus musculus
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Recruitment of BCK into the surface layer of a membrane, close to ATPases, and the resulting two-dimensional ATP diffusion along the membrane are sufficient to provide an energetic advantage. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump
Rattus norvegicus
General Information (protein specific)
General Information
Commentary
Organism
malfunction
knockout mice that lack the brain CK isoforms, i.e. BCK and/or ubiquitous MtCK, uMtCK, show defects in spatial memory acquisition and behavior, development of the hippocampus, correct functioning of hair bundle cells in the auditory system, and energy distribution within photoreceptor cells, transgenic models of creatine deficiency, overview
Mus musculus
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability
Mus musculus
metabolism
importance of functional coupling between MtCK, ANT and respiration/ATP synthesis provided by the close co-localization of MtCK and ANT in proteolipid complexes. Co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability
Mus musculus
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. spatial organization of the CK/PCr shuttle in brain, in particular the association of BCK to subcellular components as well as to specific, interacting proteins, overview
Rattus norvegicus
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
Mus musculus
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
Rattus norvegicus
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump. In retina photoreceptor cells, BCK may play an equally important role, but rather in synaptic transmission at the synaptic terminal or for cGMP resynthesis in the rod outer segments. In astrocytes and fibroblasts, BCK in peripheral cellular structures facilitates actin-driven cell spreading and migration
Mus musculus
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. The role of MtCK within the mitochondrial interactosome is to separate energy fluxes from the intracellular energy signals and to amplify these signals due to the intramitochondrial recycling of ADP
Mus musculus
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Recruitment of BCK into the surface layer of a membrane, close to ATPases, and the resulting two-dimensional ATP diffusion along the membrane are sufficient to provide an energetic advantage. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump
Rattus norvegicus
Other publictions for EC 2.7.3.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737427
Schlattner
Cellular compartmentation of e ...
Mus musculus, Rattus norvegicus, Rattus norvegicus Wistar
Amino Acids
48
1751-1774
2016
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1
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1
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-
18
2
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7
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4
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2
1
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11
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8
3
1
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1
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4
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1
6
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1
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21
3
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7
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2
1
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14
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8
4
1
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1
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7
11
-
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-
738403
Cai
Effect of Cd2+ on muscle type ...
Pelodiscus sinensis
Int. J. Biol. Macromol.
83
233-241
2016
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-
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1
2
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1
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1
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3
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1
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3
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1
3
2
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1
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1
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1
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1
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-
1
-
1
-
-
-
1
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737719
Londergan
Dynamic asymmetry and the role ...
Oryctolagus cuniculus
Biochemistry
54
83-95
2015
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1
1
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1
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2
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1
1
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1
1
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738079
Niedzwiecka
Purification and stability of ...
Clupea harengus
Comp. Biochem. Physiol. B
185
16-23
2015
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1
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1
1
2
2
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4
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2
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2
2
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2
6
2
2
4
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1
2
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739256
Wu
The activity of carp muscle-sp ...
Cyprinus carpio, Oryctolagus cuniculus
Physiol. Biochem. Zool.
87
507-516
2014
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7
2
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7
2
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2
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1
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739653
Horjus
Creatine kinase inhibits ADP-i ...
Homo sapiens
Sci. Rep.
4
6551
2014
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1
1
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5
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1
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1
1
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721310
Fan
Inactivation of recombinant hu ...
Homo sapiens
Appl. Biochem. Biotechnol.
169
268-280
2013
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1
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1
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2
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1
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1
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1
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1
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737741
Lin
Enhancement of brain-type crea ...
Homo sapiens, Mus musculus, Mus musculus R6/2
Biochim. Biophys. Acta
1832
742-753
2013
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1
1
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1
2
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3
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6
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4
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1
4
4
1
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739050
Boeck
Mitochondrial respiratory chai ...
Mus musculus, Mus musculus CF-1
Mol. Cell. Biochem.
384
129-137
2013
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1
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2
1
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4
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4
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2
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1
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1
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2
2
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739598
Feng
Effects of the Fc-III tag on a ...
Homo sapiens
Protein Sci.
22
1008-1015
2013
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1
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1
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1
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1
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1
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721916
Arnold
High levels of brain-type crea ...
Homo sapiens
Blood Cells Mol. Dis.
48
62-67
2012
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1
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1
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722245
Riviere
Dynamical properties of the lo ...
Oryctolagus cuniculus
FEBS J.
279
2863-2875
2012
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1
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722307
de Andrade
Kinetic studies on the inhibit ...
Rattus norvegicus
Food Chem. Toxicol.
50
3468-3474
2012
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1
35
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4
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1
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1
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1
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24
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24
35
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721259
Jeneson
Similar mitochondrial activati ...
Mus musculus
Am. J. Physiol. Regul. Integr. Comp. Physiol.
300
1316-1325
2011
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1
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722077
Wu
Activity and function of rabbi ...
Oryctolagus cuniculus
Comp. Biochem. Physiol. B
158
189-198
2011
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1
3
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701761
Mu
Kinetics of Zn2+-induced brain ...
Oryctolagus cuniculus
Appl. Biochem. Biotechnol.
160
1309-1320
2010
-
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1
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701768
Lue
Structural analysis and inhibi ...
Homo sapiens
Appl. Biochem. Biotechnol.
160
831-842
2010
-
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1
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1
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1
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703504
Streijger
Complete brain-type creatine k ...
Mus musculus
Epilepsia
51
79-88
2010
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2
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1
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1
1
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721956
Yerlykina
Enzymatic characteristics of c ...
Rattus norvegicus
Bull. Exp. Biol. Med.
149
14-17
2010
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1
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1
1
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722398
Gao
Isoenzyme-specific thermostabi ...
Homo sapiens
Int. J. Biol. Macromol.
47
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2010
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1
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6
1
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2
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2
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2
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1
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5
3
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1
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6
1
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2
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1
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5
3
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-
-
722399
Gao
Dissecting the key residues cr ...
Danio rerio, Homo sapiens
Int. J. Biol. Macromol.
47
366-370
2010
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2
-
18
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38
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2
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6
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2
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1
1
2
19
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2
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18
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38
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2
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2
-
1
1
2
19
-
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-
722684
Yang
Regulation of sodium-calcium e ...
Homo sapiens
J. Biol. Chem.
285
28275-28285
2010
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-
-
-
13
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3
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1
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3
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1
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1
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13
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3
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1
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1
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-
1
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-
-
-
-
-
-
-
-
-
1
1
-
-
-
703836
Tylkova
Architectural and functional r ...
Mus musculus
Gen. Physiol. Biophys.
28
219-224
2009
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-
-
-
-
-
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2
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2
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4
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1
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1
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1
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4
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
704042
Li
COMMD6 from amphioxus Branchio ...
Oryctolagus cuniculus
Int. J. Biochem. Cell Biol.
41
2459-2465
2009
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-
-
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2
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3
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2
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1
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1
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1
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2
-
-
1
-
-
-
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-
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-
-
-
-
704051
Lue
The effects of acrylamide on b ...
Oryctolagus cuniculus
Int. J. Biol. Macromol.
44
128-132
2009
-
-
-
-
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
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-
1
-
-
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-
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-
-
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-
-
-
-
704082
Bourdelas
Dynamic expression pattern of ...
Xenopus laevis
Int. J. Dev. Biol.
53
1075-1079
2009
-
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2
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12
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16
-
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-
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-
-
1
-
-
2
-
-
705501
Tonin
Inhibition of creatine kinase ...
Rattus norvegicus
Metab. Brain Dis.
24
349-360
2009
-
-
-
-
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-
1
-
2
-
-
-
-
5
-
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2
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1
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1
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1
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1
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2
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2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
705502
Pacheco
Brain creatine kinase activity ...
Rattus norvegicus
Metab. Brain Dis.
24
383-394
2009
-
-
-
-
-
-
2
-
-
-
-
-
-
5
-
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5
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1
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1
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1
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2
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5
-
-
1
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
706831
Lepper
Lead inhibits in vitro creatin ...
Rattus norvegicus
Toxicol. In Vitro
24
1045-1051
2009
-
-
-
-
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-
2
-
2
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-
-
3
-
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2
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1
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1
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1
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2
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2
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2
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1
-
-
-
-
-
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-
-
-
-
-
-
-
-
684382
Bennett
Pharmacokinetic and pharmacody ...
Canis lupus familiaris
Am. J. Trop. Med. Hyg.
79
36-41
2008
-
-
-
-
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2
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
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685504
Wennefors
Stereospecificity, substrate, ...
Oryctolagus cuniculus
Bioorg. Chem.
36
169-177
2008
-
-
-
-
-
-
1
3
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-
-
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2
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1
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3
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-
3
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1
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1
1
3
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1
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
685679
Yu
Leptin promotes proliferation ...
Sus scrofa
Biosci. Biotechnol. Biochem.
72
13-21
2008
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-
-
-
-
-
-
-
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2
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1
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-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686183
Ren
Creatine kinase inhibitor iodo ...
Rattus norvegicus
Clin. Exp. Pharmacol. Physiol.
36
141-145
2008
-
-
-
-
-
-
1
-
-
-
-
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2
-
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1
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1
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687261
Xie
Inhibition of acrylamide toxic ...
Mus musculus
J. Agric. Food Chem.
56
6054-6060
2008
-
-
-
-
-
-
1
-
-
-
-
-
-
4
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688203
Gruberg
Troponin-positive, CK-MB-negat ...
Homo sapiens
J. Invasive Cardiol.
20
125-128
2008
-
1
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3
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688324
Bong
Overexpression, purification, ...
Homo sapiens
J. Microbiol. Biotechnol.
18
295-298
2008
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1
1
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-
-
-
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-
-
-
3
-
-
1
-
-
1
-
-
1
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-
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-
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-
1
-
1
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-
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-
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-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688814
Rech
Cysteamine prevents inhibition ...
Rattus norvegicus, Rattus norvegicus Wistar
Metab. Brain Dis.
23
133-145
2008
-
-
-
-
-
-
2
-
-
-
-
-
-
170
-
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-
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-
1
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-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
2
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-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689220
Di-Pietro
Inhibition of brain creatine k ...
Rattus norvegicus, Rattus norvegicus Wistar
Neurosci. Lett.
434
139-143
2008
-
-
-
-
-
-
-
-
-
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-
-
-
169
-
-
-
-
-
6
-
-
2
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
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-
-
-
-
-
-
-
6
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689889
Iwanami
Cytoplasmic and mitochondrial ...
Physeter catodon
Protein J.
27
43-49
2008
-
-
1
-
-
-
-
4
2
-
-
-
-
6
-
-
-
-
-
1
-
-
2
-
-
-
-
4
-
-
-
-
-
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-
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-
1
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-
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4
2
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-
-
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-
-
1
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
697687
Vissing
Effects of concentric and repe ...
Homo sapiens
Eur. J. Appl. Physiol.
103
323-332
2008
1
-
-
-
-
-
-
-
-
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2
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-
1
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-
1
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
702414
Wang
Detection of local polarity an ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
1784
415-422
2008
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
2
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-
1
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-
-
-
-
-
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-
1
-
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-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671058
Ohren
Structural asymmetry and inter ...
Oryctolagus cuniculus
Acta Crystallogr. Sect. D
63
381-389
2007
-
-
-
1
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
1
3
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-
-
-
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-
-
-
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671618
Awama
Despite its high similarity wi ...
Oryctolagus cuniculus
Arch. Biochem. Biophys.
458
158-166
2007
-
-
-
-
1
1
3
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671627
Abnous
Regulation of skeletal muscle ...
Urocitellus richardsonii
Arch. Biochem. Biophys.
467
10-19
2007
-
-
-
-
-
-
-
6
-
-
1
-
-
4
-
1
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671632
Pereira Oliveira
Cystine inhibits creatine kina ...
Sus scrofa
Arch. Med. Res.
38
164-169
2007
-
-
-
-
-
-
1
-
2
-
-
-
-
4
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
1
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-
2
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671679
Assis
Effect of antipsychotics on cr ...
Rattus norvegicus
Basic Clin. Pharmacol. Toxicol.
101
315-319
2007
2
1
-
-
-
-
2
-
-
-
-
-
-
5
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673067
Eliuk
Active site modifications of t ...
Homo sapiens
Chem. Res. Toxicol.
20
1260-1268
2007
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674027
He
Role of the linker between the ...
Oryctolagus cuniculus
Int. J. Biochem. Cell Biol.
39
1816-1827
2007
-
-
-
-
2
-
-
8
-
-
-
-
-
2
-
-
-
-
-
2
4
-
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
8
-
-
-
-
-
-
-
-
-
2
4
-
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
674031
Feng
Effects of the single point ge ...
Homo sapiens
Int. J. Biochem. Cell Biol.
39
392-401
2007
-
-
-
-
1
-
-
4
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-
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1
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-
-
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-
1
3
-
1
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
3
-
1
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
674788
Zhao
The generation of the oxidized ...
Oryctolagus cuniculus
J. Biol. Chem.
282
12022-12029
2007
-
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1
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674947
Zou
Monomeric creatine kinase aggr ...
Oryctolagus cuniculus
J. Biomol. Struct. Dyn.
24
359-367
2007
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675240
Zanette
Modulation of creatine kinase ...
Rattus norvegicus
J. Inorg. Biochem.
101
267-273
2007
2
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675316
Bretonnet
NMR screening applied to the f ...
Oryctolagus cuniculus
J. Med. Chem.
50
1865-1875
2007
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1
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675783
Delwing
Arginine administration reduce ...
Rattus norvegicus
Metab. Brain Dis.
22
13-23
2007
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1
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1
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4
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675955
Buerklen
Brain-type creatine kinase BB- ...
Homo sapiens
Mol. Cell. Biochem.
297
53-64
2007
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1
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675956
Zurmanova
Creatine kinase binds more fir ...
Oryctolagus cuniculus
Mol. Cell. Biochem.
305
55-61
2007
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675957
Lenz
Inhibition of cytosolic and mi ...
Homo sapiens
Mol. Cell. Biochem.
306
153-162
2007
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3
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5
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6
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676173
Shin
Hair bundles are specialized f ...
Gallus gallus, Mus musculus
Neuron
53
371-386
2007
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1
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1
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4
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685344
Zugno
Evidence that the inhibitory e ...
Rattus norvegicus
Biochim. Biophys. Acta
1772
563-569
2007
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1
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686860
Daosukho
Phenylbutyrate, a histone deac ...
Mus musculus
Free Radic. Biol. Med.
42
1818-1825
2007
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-
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3
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1
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687322
Berri
Consequence of muscle hypertro ...
Gallus gallus
J. Anim. Sci.
85
2005-2011
2007
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1
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689192
Illa
Symptomatic dysferlin gene mut ...
Homo sapiens
Neurology
68
1284-1289
2007
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1
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671814
Shi
Sodium barbital is a slow reve ...
Oryctolagus cuniculus
Biochem. Cell Biol.
84
142-147
2006
-
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1
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1
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672065
Wang
Exploring the role of the acti ...
Homo sapiens
Biochemistry
45
11464-11472
2006
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3
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2
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2
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2
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672307
Zhang
Two fused proteins combining S ...
Oryctolagus cuniculus
Biochemistry (Moscow)
71
983-988
2006
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1
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6
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4
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6
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3
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1
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672391
Hoffman
The role of an absolutely cons ...
Chaetopterus variopedatus, Gallus gallus, Tethya aurantium
Biochim. Biophys. Acta
1764
1512-1517
2006
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13
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3
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4
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1
13
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3
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-
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673159
Grzyb
-
Purification and some properti ...
Clupea harengus
Comp. Biochem. Physiol. B
144B
152-158
2006
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4
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1
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1
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2
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4
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2
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1
2
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-
-
-
-
-
-
-
-
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673658
Zhao
Impact of intra-subunit domain ...
Oryctolagus cuniculus
FEBS Lett.
580
3835-3840
2006
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-
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8
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18
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1
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1
9
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1
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3
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8
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18
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1
9
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1
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3
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674039
Matsushima
Comparison of kinetic constant ...
Danio rerio, Dendronephthya gigantea, Hediste diversicolor, Lethenteron camtschaticum, Mus musculus
Int. J. Biol. Macromol.
38
83-88
2006
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16
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22
13
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5
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-
-
16
-
-
-
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-
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-
-
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674083
Wang
Heterogeneity of Escherichia c ...
Homo sapiens
IUBMB Life
58
421-428
2006
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1
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8
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3
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3
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1
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5
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1
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8
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3
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1
-
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674384
Zonouzi
Kinetic properties of extracte ...
Mus musculus
J. Biochem. Mol. Biol.
39
426-431
2006
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2
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3
2
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1
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1
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2
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2
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3
2
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1
-
1
-
-
-
2
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-
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674713
Meyer
Mitochondrial creatine kinase ...
Rattus norvegicus
J. Biol. Chem.
281
37361-37371
2006
3
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2
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2
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1
-
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675415
Du
Mixed macromolecular crowding ...
Oryctolagus cuniculus
J. Mol. Biol.
364
469-482
2006
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1
3
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3
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-
-
-
-
-
-
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-
-
-
-
-
-
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675718
Pancera
Effect of pH on the adsorption ...
Oryctolagus cuniculus
J. Phys. Chem. B
110
2674-2680
2006
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1
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1
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1
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2
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1
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-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
675781
Barschak
Inhibition of the electron tra ...
Homo sapiens
Metab. Brain Dis.
21
11-19
2006
-
1
-
-
-
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1
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-
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3
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-
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3
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1
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1
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3
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661270
Jourden
Transition state stabilization ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
1751
178-183
2005
-
-
1
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11
-
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14
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1
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1
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2
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1
1
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2
-
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2
-
1
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-
14
1
-
-
2
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-
-
-
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1
2
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11
-
-
-
-
14
-
1
-
1
-
-
-
1
-
2
-
-
2
-
1
-
-
14
1
-
-
-
-
-
-
-
-
-
661271
Hoffman
Over-expression, purification ...
Chaetopterus variopedatus
Biochim. Biophys. Acta
1751
184-193
2005
-
-
1
-
-
-
-
-
1
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3
1
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5
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1
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-
-
-
-
2
3
1
-
-
-
-
-
-
2
-
-
-
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1
2
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-
-
-
-
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1
-
3
1
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-
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1
-
-
-
-
2
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
661523
Grzyb
Characterization of creatine k ...
Clupea harengus
Comp. Biochem. Physiol. B
140
629-634
2005
-
-
-
-
-
-
-
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4
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4
1
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3
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1
-
-
2
2
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1
2
-
-
-
-
-
-
-
2
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-
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2
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4
-
4
1
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1
-
2
2
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
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661528
McLeish
Relating structure to mechanis ...
Bos taurus, Gallus gallus, Homo sapiens, Oryctolagus cuniculus, Tetronarce californica
Crit. Rev. Biochem. Mol. Biol.
40
1-20
2005
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1
1
5
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27
21
10
5
4
10
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7
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1
5
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5
1
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26
11
-
-
-
16
2
-
-
10
-
4
-
-
1
1
10
5
-
-
-
27
-
21
10
5
4
10
-
-
-
1
-
5
1
-
26
11
-
-
-
16
2
-
-
4
-
-
-
-
-
-
661095
Novak
Isoleucine 69 and valine 325 f ...
Homo sapiens
Biochemistry
43
13766-13774
2004
-
-
1
-
5
-
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4
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1
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1
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1
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1
-
4
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13
1
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1
2
-
5
-
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4
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1
-
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2
1
-
4
-
1
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13
1
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661220
Belousova
Kinetics of chemical modificat ...
Bos taurus
Biochemistry
69
455-461
2004
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2
1
2
2
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1
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2
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1
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1
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1
1
2
2
-
1
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2
-
-
1
-
1
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-
1
-
-
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-
642420
Miura
Inactivation of creatine kinas ...
Rattus norvegicus
Food Chem. Toxicol.
41
759-765
2003
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4
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642424
Winnard
-
Isolation, characterization an ...
Chaenocephalus aceratus
Comp. Biochem. Physiol. B
134B
651-667
2003
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1
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2
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1
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1
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642425
Borders
Asparagine 285 plays a key rol ...
Oryctolagus cuniculus
Protein Sci.
12
532-537
2003
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3
-
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642426
Grzyb
-
Quantitative determination of ...
Clupea harengus
Comp. Biochem. Physiol. C
134C
207-213
2003
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1
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1
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642435
Gregor
Substrate channelling in a cre ...
Rattus norvegicus
Exp. Physiol.
88
1-6
2003
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1
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660930
Tang
Effects of lactic acid and NaC ...
Oryctolagus cuniculus
Biochem. Cell Biol.
81
1-7
2003
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1
1
1
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1
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660931
Guo
Studies on the stability of cr ...
Oryctolagus cuniculus
Biochem. Cell Biol.
81
9-16
2003
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1
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1
2
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661068
Cox
Generation of an active monome ...
Oryctolagus cuniculus
Biochemistry
42
1863-1871
2003
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1
-
5
-
2
1
1
1
10
1
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2
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1
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1
3
1
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4
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5
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2
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1
1
1
10
1
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1
3
1
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4
-
1
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661901
Pilla
Kinetic studies on the inhibit ...
Rattus norvegicus
Int. J. Dev. Neurosci.
21
145-151
2003
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4
3
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2
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4
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2
6
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4
6
3
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3
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1
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1
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662511
Kanemitsu
Mitochondrial creatine kinase ...
Homo sapiens
J. Chromatogr. B
783
191-197
2003
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1
2
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5
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2
1
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1
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1
-
1
-
1
-
-
1
-
5
-
-
-
-
-
-
662524
Birkedal
Creatine kinase and mitochondr ...
Gadus morhua, Oncorhynchus mykiss, Trachemys scripta elegans
J. Comp. Physiol. B
173
493-499
2003
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4
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8
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6
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5
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3
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662723
Hahn
Aggregation and folding of rec ...
Homo sapiens
J. Protein Chem.
22
563-570
2003
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1
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642433
Bonz
Functional properties and [Ca( ...
Mus musculus
Biochem. Biophys. Res. Commun.
298
163-168
2002
-
1
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1
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-
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642437
Wang
Expression of Torpedo californ ...
Tetronarce californica
Protein Expr. Purif.
26
89-95
2002
-
-
-
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4
3
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-
6
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1
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2
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1
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4
3
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1
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2
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-
1
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-
-
-
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-
-
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642441
Lahiri
The 2.1.ANG. Structure of Torp ...
Tetronarce californica
Biochemistry
41
13861-13867
2002
-
-
-
1
-
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2
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
642429
Ye
Myocardial creatine kinase kin ...
Canis lupus familiaris
Am. J. Physiol.
281
H376-H386
2001
-
1
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2
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-
-
-
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642431
Harder
Isolation and characterization ...
Danio rerio
Biochem. Cell Biol.
79
779-782
2001
-
-
1
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-
-
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2
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1
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-
-
-
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-
-
-
-
-
-
-
-
642438
Lipskaya
Mitochondrial creatine kinase: ...
Bos taurus, Columba livia
Biochemistry
66
1098-1111
2001
-
-
-
-
-
-
-
8
2
-
-
-
-
2
-
-
-
-
-
4
-
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-
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2
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8
2
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-
4
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
642446
Zhu
Relationship between Kinetic a ...
Oryctolagus cuniculus
Biochem. Biophys. Res. Commun.
285
857-862
2001
-
-
-
-
-
-
-
1
-
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-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
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642430
Schlattner
Divergent enzyme kinetics and ...
Homo sapiens
Biol. Chem.
381
1063-1070
2000
-
-
-
-
-
-
-
4
2
-
3
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2
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-
-
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-
2
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-
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-
-
2
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4
2
-
3
-
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-
-
-
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
642436
Kanemitsu
Characterization of two types ...
Homo sapiens
Electrophoresis
21
266-270
2000
-
-
-
-
-
-
-
2
1
-
-
-
-
2
-
-
-
-
-
4
-
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-
1
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-
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-
3
-
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-
-
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-
2
1
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-
-
-
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-
-
4
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
642439
Mourad-Terzian
Creatine kinase isoenzymes spe ...
Homo sapiens
FEBS Lett.
475
22-26
2000
-
-
1
-
2
-
-
-
-
-
-
-
-
2
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-
1
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-
1
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2
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642442
Eder
Crystal structure of human ubi ...
Homo sapiens
Proteins
39
216-225
2000
-
-
-
1
-
-
-
-
1
-
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-
-
3
-
-
-
-
-
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-
1
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642421
Buist
-
Temperature dependence of the ...
Rattus norvegicus
Can. J. Chem.
77
1887-1891
1999
-
-
-
-
-
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-
1
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1
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-
1
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-
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-
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-
1
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-
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642423
Gregor
Creatine kinase reaction in sk ...
Rattus norvegicus
Physiol. Res.
48
27-35
1999
-
-
-
-
-
-
-
-
1
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-
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3
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-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642443
Tang
Crystallization and preliminar ...
Homo sapiens
Acta Crystallogr. Sect. D
55
669-670
1999
-
-
-
1
-
-
-
-
-
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-
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2
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-
-
1
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642444
Eder
Crystal structure of brain-typ ...
Gallus gallus
Protein Sci.
8
2258-2269
1999
-
-
-
1
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-
-
-
-
-
-
-
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-
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-
1
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642427
Ventura-Clapier
Functional coupling of creatin ...
Columba livia, Frog, Gallus gallus, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
Mol. Cell. Biochem.
184
231-247
1998
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6
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6
-
8
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6
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
6
-
-
-
-
-
-
-
-
6
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642428
Yang
Reactivation kinetics of 5,5'- ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
1388
190-198
1998
-
-
-
-
-
-
-
-
-
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-
2
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-
-
1
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-
-
-
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642440
Gellerich
Dextran strongly increases the ...
Rattus norvegicus
Eur. J. Biochem.
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172-180
1998
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-
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642445
Rao
Crystal structure of rabbit mu ...
Oryctolagus cuniculus
FEBS Lett.
439
133-137
1998
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-
-
1
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1
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642422
Walterscheid-Muller
Purification and characterizat ...
Homo sapiens
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1997
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2
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2
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-
2
-
-
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-
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642434
Couthon
High salt concentrations induc ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
1339
277-288
1997
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-
-
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2
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2
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2
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-
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642432
Tombes
Isolation and characterization ...
Strongylocentrotus purpuratus
Methods Cell Biol.
47
467-472
1995
-
-
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-
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2
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1
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2
1
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1
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2
1
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-
642371
Wyss
Mitochondrial creatine kinase: ...
Bos taurus, Columba livia, Gallus gallus, Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus, Strongylocentrotus purpuratus, Sus scrofa
Biochim. Biophys. Acta
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119-166
1992
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8
-
8
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8
24
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8
8
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8
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8
8
-
80
-
-
16
-
-
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-
14
-
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-
-
8
-
-
8
-
-
8
-
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8
24
-
8
8
-
-
-
8
-
80
-
-
16
-
-
-
-
-
14
-
-
8
-
-
-
-
-
-
642372
Schnyder
Crystallization of mitochondri ...
Gallus gallus
J. Biol. Chem.
266
5318-5322
1991
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1
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3
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3
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1
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1
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2
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1
1
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-
-
-
642412
Nakagawa
-
Enzymic properties of fish mus ...
Cyprinus carpio, Pagrus major, Scomber japonicus
Comp. Biochem. Physiol. B
98
349-354
1991
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6
6
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3
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3
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-
3
-
-
3
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-
3
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-
3
-
3
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-
-
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6
-
6
-
3
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3
-
3
-
-
3
-
-
-
3
-
3
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-
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642373
Schnyder
Crystallization and preliminar ...
Gallus gallus
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809-812
1990
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3
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2
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1
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2
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3
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1
2
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642374
Wyss
Mitochondrial creatine kinase ...
Gallus gallus
J. Biol. Chem.
265
15900-15908
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-
-
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1
2
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3
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3
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1
-
-
3
1
-
1
1
2
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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1
2
-
3
-
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1
-
3
1
-
1
1
2
-
1
-
2
-
-
-
-
-
-
-
-
-
642375
Schlegel
Native mitochondrial creatine ...
Gallus gallus
J. Biol. Chem.
263
16942-16953
1988
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-
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3
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2
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3
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1
-
-
2
1
2
1
2
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
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3
-
2
-
-
-
-
1
-
2
1
2
1
2
-
-
-
-
-
-
-
-
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-
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642376
Schnyder
Native mitochondrial creatine ...
Gallus gallus
J. Biol. Chem.
263
16954-16962
1988
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-
-
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1
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2
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3
1
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2
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-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
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-
1
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2
-
3
1
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-
1
-
-
2
-
-
-
-
-
-
-
-
-
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-
-
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642410
Hossle
Distinct tissue specific mitoc ...
Gallus gallus
Biochem. Biophys. Res. Commun.
151
408-416
1988
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-
1
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-
-
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2
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1
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2
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-
-
4
-
-
1
1
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-
-
-
-
-
-
-
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-
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-
1
-
-
-
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-
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-
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2
-
1
-
-
-
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-
-
4
-
-
1
1
-
-
-
-
-
-
-
-
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-
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-
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642413
Robert
Purification and characterizat ...
Xenopus laevis
Biochem. Genet.
26
543-555
1988
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-
-
-
-
-
-
-
2
-
2
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4
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1
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-
-
-
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-
1
-
-
-
-
-
-
-
-
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-
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-
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2
-
2
-
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1
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-
-
-
-
1
-
-
-
-
-
-
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-
-
-
-
-
-
-
642414
Schneider
Kinetic characterization of hu ...
Homo sapiens
Enzyme
39
220-226
1988
-
-
-
-
-
-
-
1
-
-
-
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2
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-
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4
-
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1
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4
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-
-
-
-
-
-
-
-
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-
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642377
Brooks
Homogeneous chicken heart mito ...
Gallus gallus
Anal. Biochem.
164
190-198
1987
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-
-
-
-
-
-
-
2
-
2
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4
-
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1
-
-
2
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
1
-
2
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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642418
Tombes
Enzyme termini of a phosphocre ...
Strongylocentrotus purpuratus
J. Biol. Chem.
262
16011-16019
1987
-
-
-
-
-
-
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1
1
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4
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3
-
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1
-
-
4
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
4
-
-
-
-
1
-
4
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642378
Hershenson
Purification and crystallizati ...
Oryctolagus cuniculus
J. Biol. Chem.
261
3732-3736
1986
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-
-
1
-
-
-
-
-
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-
-
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2
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-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642415
Afolayan
Isolation and properties of cr ...
Eidolon helvum
Comp. Biochem. Physiol. B
85
463-468
1986
-
-
-
-
-
-
1
-
-
3
2
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-
3
-
1
1
-
-
5
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
3
2
-
-
-
1
1
-
5
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642416
Gray
Purification and characterizat ...
Ginglymostoma cirratum
Comp. Biochem. Physiol. B
83
613-620
1986
-
-
-
-
-
-
2
4
-
1
-
-
-
6
-
-
1
-
-
4
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
4
-
1
-
-
-
-
-
1
-
4
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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642379
Barrantes
Isolation and characterization ...
Discopyge tschudii, Torpedo marmorata
J. Biol. Chem.
260
3024-3034
1985
-
-
-
-
-
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4
3
2
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-
3
-
-
2
-
-
3
2
-
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
4
3
2
-
-
-
-
-
2
-
3
2
-
2
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
642380
Vaidya
Purification of five creatine ...
Homo sapiens
Biochim. Biophys. Acta
790
230-237
1984
-
-
-
-
-
-
-
-
-
-
-
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2
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-
1
-
-
5
1
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
1
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
642381
George
Purification and characterizat ...
Canis lupus familiaris
J. Biol. Chem.
259
2667-2674
1984
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-
-
-
-
-
-
-
1
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-
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3
-
-
1
-
-
2
2
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
2
2
-
1
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
642382
Rudge
-
Thermal stability of immobiliz ...
Oryctolagus cuniculus
Biochem. Soc. Trans.
12
311-313
1984
-
1
-
-
-
-
-
-
-
-
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-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642383
Grace
Purification and characterizat ...
Homo sapiens
J. Biol. Chem.
258
15346-15354
1983
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-
-
-
-
-
-
-
3
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1
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-
3
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-
1
-
-
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
-
1
-
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642384
Gilliland
Crystallization and preliminar ...
Bos taurus
J. Mol. Biol.
170
791-793
1983
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-
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1
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1
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2
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-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642385
Blum
Mitochondrial creatine kinase ...
Bos taurus, Gallus gallus, Homo sapiens, Oryctolagus cuniculus, Papio anubis, Rattus norvegicus, Sus scrofa, trout
J. Biochem.
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1247-1257
1983
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1
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-
-
4
9
8
2
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-
9
-
-
1
-
-
9
2
1
8
8
-
-
-
-
9
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
9
8
2
-
-
-
-
1
-
9
2
1
8
8
-
-
-
-
9
-
1
-
-
-
-
-
-
-
642386
Takasawa
Properties of three creatine k ...
Sus scrofa
J. Biochem.
93
389-395
1983
-
-
-
-
-
-
-
-
1
-
-
-
-
2
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-
-
-
-
1
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
642388
Gerhardt
-
Creatine kinase ...
Homo sapiens
Methods Enzym. Anal. ,3rd Ed. (Bergmeyer,H. U. ,ed. )
3
508-510
1983
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1
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15
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2
2
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1
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-
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-
1
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
15
-
-
2
2
-
-
-
-
-
-
1
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642389
Kumar
Purification and characterizat ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
111
156-165
1983
-
-
-
-
-
-
3
1
1
-
1
-
-
2
-
-
1
-
-
2
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642419
Kenyon
Creatine kinase: structure-act ...
Mammalia
Adv. Enzymol. Relat. Areas Mol. Biol.
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367-426
1983
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1
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642390
Olson
Purification and cell-free tra ...
Mus musculus
Biochem. Biophys. Res. Commun.
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1982
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1
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642391
Roberts
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Purification of human and cani ...
Canis lupus familiaris, Homo sapiens
Methods Enzymol.
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1982
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642387
Takasawa
-
Isolation and properties of cr ...
Sus scrofa
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1981
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1
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642392
Takasawa
Crystallization and properties ...
Equus caballus
J. Biochem.
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1981
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642393
Roerts
Purification of mitochondrial ...
Canis lupus familiaris
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2870-2877
1980
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642394
Reddy
Inhibition of creatine kinase ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
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109-113
1979
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642395
Hall
Mitochondrial creatine kinase. ...
Bos taurus
Biochemistry
18
1745-1751
1979
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4
2
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1
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2
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642396
Fisher
Purification of the creatine k ...
Lepomis cyanellus
Anal. Biochem.
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89-95
1979
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642397
Herasymowych
Isolation, purification and ch ...
Bos taurus, Oryctolagus cuniculus
Biochim. Biophys. Acta
534
38-47
1978
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2
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642398
Burgess
Creatine kinase. A new crystal ...
Oryctolagus cuniculus
J. Mol. Biol.
123
691-695
1978
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642399
Reddy
Inhibition of rabbit muscle cr ...
Oryctolagus cuniculus
Biochem. Soc. Trans.
6
553-555
1978
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642400
Saks
The localization of the MM iso ...
Rattus norvegicus
Biochim. Biophys. Acta
465
550-558
1977
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642401
Hall
Purification of mitochondrial ...
Bos taurus
Biochem. Biophys. Res. Commun.
76
950-956
1977
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642402
Madelian
Properties of a structurally a ...
Oryctolagus cuniculus
Arch. Biochem. Biophys.
184
103-110
1977
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1
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642403
Saks
Studies of energy transport in ...
Rattus norvegicus
Eur. J. Biochem.
57
273-290
1975
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642417
Storey
-
Purification and properties of ...
Trachemys scripta
Int. J. Biochem.
6
54-59
1975
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642404
Gercken
Inhibition of creatine kinase ...
Oryctolagus cuniculus
FEBS Lett.
46
87-91
1974
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642405
Witteveen
Kinetic properties of the isoe ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
71
1384-1387
1974
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642406
Schimerlik
Inhibition of creatine kinase ...
Oryctolagus cuniculus
J. Biol. Chem.
248
8418-8423
1973
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642407
Keutel
Studies on adenosine triphosph ...
Bos taurus, Homo sapiens, Oryctolagus cuniculus
Arch. Biochem. Biophys.
150
648-678
1972
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3
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3
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4
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642408
Simonarson
Purification and properties of ...
Scyliorhinus canicula
Biochem. J.
128
1241-1253
1972
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642411
Gosselin-Rrey
Isolation and molecular proper ...
Cyprinus carpio
Biochim. Biophys. Acta
221
241-254
1970
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642447
Moreland
Phosphagen kinases and evoluti ...
echinodermata
Nature
214
458-462
1967
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642409
Kuby
-
ATP-creatine transphosphorylas ...
Mammalia
The Enzymes,2nd. Ed. (Boyer,P. D. ,ed. )
6
515-603
1962
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