Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
-
increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. Glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
-
-
?
additional information
?
-
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
autoglucosylation by glycogenin-1
-
-
?
additional information
?
-
human glycogenin during its reaction cycle shows a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This switch includes the ordering of a polypeptide stretch containing Tyr195, and major movement of an approximately 30-residue lid segment covering the active site. The rearranged lid guides the nascent maltosaccharide chain into the active site in either an intra- or intersubunit mode dependent upon chain length and steric factors and positions the donor and acceptor sugar groups for catalysis. Mapping of donor and acceptor subsites in hGYG1, overview
-
-
?
additional information
?
-
-
human glycogenin during its reaction cycle shows a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This switch includes the ordering of a polypeptide stretch containing Tyr195, and major movement of an approximately 30-residue lid segment covering the active site. The rearranged lid guides the nascent maltosaccharide chain into the active site in either an intra- or intersubunit mode dependent upon chain length and steric factors and positions the donor and acceptor sugar groups for catalysis. Mapping of donor and acceptor subsites in hGYG1, overview
-
-
?
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
-
glycogenin-1 catalyzes both the glucose-O-tyrosine linkage and the alpha1,4 glucosidic bonds linking the glucose molecules in the oligosaccharide
-
-
?
additional information
?
-
glycosylated HLPFIYNLSSNTMYTYSPAFK peptide products originating from glycogenin-2, mass spectrometric analysis, overview
-
-
?
additional information
?
-
glycosylated HLPFIYNLSSNTMYTYSPAFK peptide products originating from glycogenin-2, mass spectrometric analysis, overview
-
-
?
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
additional information
?
-
the enzyme performs autoglucosylation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-1
UDP + alpha-D-glucosylglycogenin-1
self-glucosylation of the glycosyltransferase glycogenin-1
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
essential for the formation of glycogen granules, binds a chain of 5-13 glucose molecules at a specific tyrosine residue (Y194) by autoglycosylation
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
UDP-alpha-D-glucose + glycogenin-2
UDP + alpha-D-glucosylglycogenin-2
self-glucosylation of the glycosyltransferase glycogenin-2
-
-
?
UDP-glucose + glycogenin
UDP + glucosylated glycogenin
-
-
-
-
?
UDP-glucose + glycogenin
UDP + glucosylglycogenin
-
increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. Glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
autoglucosylation by glycogenin-1
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
-
-
?
UDP-alpha-D-glucose + glycogenin
UDP + alpha-D-glucosylglycogenin
-
autoglucosylation by glycogenin-1
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,4-alpha-glucan branching enzyme deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Cardiomyopathies
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
Cardiomyopathies
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Cardiomyopathies
Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage.
Diabetes Mellitus
The role of glycogenin in glycogen synthesis and non-insulin dependent diabetes mellitus.
Diabetes Mellitus, Type 2
Mutational analysis of the coding regions of the genes encoding protein kinase B-alpha and -beta, phosphoinositide-dependent protein kinase-1, phosphatase targeting to glycogen, protein phosphatase inhibitor-1, and glycogenin: lessons from a search for genetic variability of the insulin-stimulated glycogen synthesis pathway of skeletal muscle in NIDDM patients.
Glycogen Storage Disease
A new muscle glycogen storage disease associated with glycogenin-1 deficiency.
Glycogen Storage Disease
A newly identified c.1824_1828dupATACG mutation in exon 13 of the GAA gene in infantile-onset glycogen storage disease type II (Pompe disease).
Glycogen Storage Disease
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
Glycogen Storage Disease
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Glycogen Storage Disease
Glycogen and its metabolism: some new developments and old themes.
Glycogen Storage Disease
Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
Glycogen Storage Disease
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
Glycogen Storage Disease
Molecular pathogenesis of a new glycogenosis caused by a glycogenin-1 mutation.
Glycogen Storage Disease
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
Glycogen Storage Disease
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.
Glycogen Storage Disease Type II
A newly identified c.1824_1828dupATACG mutation in exon 13 of the GAA gene in infantile-onset glycogen storage disease type II (Pompe disease).
glycogenin glucosyltransferase deficiency
A new muscle glycogen storage disease associated with glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Cardiomyopathy as presenting sign of glycogenin-1 deficiency-report of three cases and review of the literature.
glycogenin glucosyltransferase deficiency
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
glycogenin glucosyltransferase deficiency
Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage.
glycogenin glucosyltransferase deficiency
Glycogenin-1 deficiency and inactivated priming of glycogen synthesis.
glycogenin glucosyltransferase deficiency
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
glycogenin glucosyltransferase deficiency
Muscle glycogen synthesis and breakdown are both impaired in glycogenin-1 deficiency.
glycogenin glucosyltransferase deficiency
Polyglucosan myopathy and functional characterization of a novel GYG1 mutation.
glycogenin glucosyltransferase deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
HIV Infections
Peripheral blood RNA gene expression in children with pneumococcal meningitis: a prospective case-control study.
Lafora Disease
Glycogen and its metabolism: some new developments and old themes.
Lafora Disease
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Muscle Weakness
Severe asymmetric muscle weakness revealing glycogenin-1 polyglucosan body myopathy.
Muscular Diseases
Functional characterization of GYG1 variants in two patients with myopathy and glycogenin-1 deficiency.
Muscular Diseases
GYG1: A distal myopathy with polyglucosan bodies.
Muscular Diseases
Late-onset polyglucosan body myopathy in five patients with a homozygous mutation in GYG1.
Muscular Diseases
Longitudinal follow-up and muscle MRI pattern of two siblings with polyglucosan body myopathy due to glycogenin-1 mutation.
Muscular Diseases
Muscle pathology and whole-body MRI in a polyglucosan myopathy associated with a novel glycogenin-1 mutation.
Muscular Diseases
Polyglucosan myopathy and functional characterization of a novel GYG1 mutation.
Muscular Diseases
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Muscular Diseases
Severe asymmetric muscle weakness revealing glycogenin-1 polyglucosan body myopathy.
Muscular Dystrophies, Limb-Girdle
Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.
Neoplasms
Metastasis of Uveal Melanoma with Monosomy-3 Is Associated with a Less Glycogenetic Gene Expression Profile and the Dysregulation of Glycogen Storage.
Perinatal Death
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
Respiratory Distress Syndrome
Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.
ring-type e3 ubiquitin transferase deficiency
Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.
Sarcoma, Ewing
Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
unlike mice, humans and other primates have a second variant of glycogenin called glycogenin-2, which is mainly expressed in the liver
evolution
unlike mice, humans and other primates have a second variant of glycogenin called glycogenin-2, which is mainly expressed in the liver
malfunction
the Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive
malfunction
complete lack of glycogenin-1 is usually associated with late onset muscle weakness, indicating that lack of glycogenin-1 has no major impact on muscle energy metabolism. The muscle weakness that appears later in life is associated with muscle fiber degeneration, replacement of muscle tissue by fat and fibrous connective tissue explains the weakness. Several recessive pathogenic mutations have been identified in the glycogenin-1 gene, GYG1. Complete absence of glycogenin-1 protein secondary tobi-allelic truncating mutations in GYG1 causes a rare muscle disease that is characterized by accumulation of glycogen. This glycogen is, in addition to lack of a glycogenin-1 core, abnormal with regard to its ultrastructure. Many glycogen particles show uneven size and irregular shape, and some of the storage material has a fibrillar structure. A more severe heart disease associated with missense GYG1 mutations has been described in several individuals. Muscle glycogen depletion caused by truncating mutations in GYS1, which encodes the ubiquitously expressed glycogen synthase, does not result in a compensatory upregulation of the liver glycogen synthase isoform. In patients with total lack of glycogen due to muscle glycogen synthase deficiency, glycogenin-1 is present in similar quantities as in normal individuals
malfunction
etiology and pathogenesis of a late-onset myopathy associated with glycogenin-1 deficiency, overview. Two siblings heterozygous for two mutations in the glycogenin-1 gene, one 1-base deletion and one missense mutation, are analyzed. They show remarkably different clinical expression of the disease. There is no clear correlation between the genotype and the phenotypic expression even within the same family. Glycogenin-1 deficiency should be considered as a differential diagnosis in middle-aged and elderly individuals with slowly progressive myopathy, and it may present with highly variable distribution of weakness and wasting. Phenotypes, detailed overview
physiological function
glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis
physiological function
glycogen synthesis is initiated by self-glucosylation of the glycosyltransferases glycogenin-1 and -2 that, in the presence of UDP-glucose, form both the first glucose-O-tyrosine linkage, and then stepwise add a series of alpha1,4-linked glucoses to a growing chain of variable length. The self-glucosylation endpoint is the incorporation of 4-8 glucose units on Tyr195 of glycogenin-1
physiological function
glycogenin-1 is a constitutively active enzyme so does not represent a point of regulation
physiological function
glycogenin is a core protein in glycogen particles and functions as a glycosyl transferase with the ability to autoglucosylate
malfunction
-
glycogen depletion in skeletal muscle is a result of a non-functional glycogenin-1 due to a Thr83Met substitution in glycogenin-1
malfunction
analysis of GYG2 deletion phenotype and effects on glucose metabolism and/or glycogen synthesis, GYG2 deletion mutant phenotype overview, liver histopathology and enzyme expression level, overview
malfunction
glycogenin-2 is unable to glucosylate inactive glycogenin-1, at least not an enzymatically inactivated Thr83Met glycogenin-1 mutant, recently identified in a patient with severe glycogen depletion
malfunction
glycogen storage disease (GSD) type XV is a rare disease caused by mutations in the GYG1 gene that codes for the core molecule of muscle glycogen, glycogenin 1. Nonetheless, glycogen is present in muscles of glycogenin 1-deficient patients due to activity of glycogenin 2. Apart from occurrence of polyglucosan (PG) bodies in few fibers, glycogen appears normal in most cells, and the concentration is normal in patients with GSD type XV. Analysis of formation of glycogen and changes in glycogen metabolism in patients with GSD type XV, overview
malfunction
muscle glycogen depletion caused by truncating mutations in GYS1, which encodes the ubiquitously expressed glycogen synthase, does not result in a compensatory upregulation of the liver glycogen synthase isoform
physiological function
-
glycogenin is a self-glycosylating protein primer that initiates glycogen granule formation
physiological function
-
glycogenin-1 initiates the glycogen synthesis in skeletal muscle by the autocatalytic formation of a short oligosaccharide at tyrosine 195
physiological function
glycogen synthesis is initiated by self-glucosylation of the glycosyltransferases glycogenin-1 and -2 that, in the presence of UDP-glucose, form both the first glucose-O-tyrosine linkage, and then stepwise add a series of alpha1,4-linked glucoses to a growing chain of variable length. The self-glucosylation endpoint is only 0-4 glucose units on Tyr228 of glycogenin-2. The glucosylation of glycogenin-2 is enhanced to 2-4 glucose units by the presence of enzymatically active glycogenin-1
physiological function
glycogenin-2 is dispensable for liver glycogen synthesis and glucagon-stimulated glucose release. Glycogenin-2 is not required for liver glycogen synthesis and glucagon-stimulated glucose release
physiological function
enzyme glycogenin 2 compensates for glycogenin 1 in human skeletal muscles of GYG1-deficient mutants. No expression of GYG2 occurs in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
physiological function
glycogenin 1 protein forms the core of glycogen in skeletal and cardiac muscle
physiological function
glycogenin is a core protein in glycogen particles and functions as a glycosyl transferase with the ability to autoglucosylate
additional information
hGYG1 ccurs in two distinct states, the ground state and the active state, the two states are interchangeable during catalysis and involve conformational rearrangements in three regions that influence active site accessibility, overview
additional information
-
hGYG1 ccurs in two distinct states, the ground state and the active state, the two states are interchangeable during catalysis and involve conformational rearrangements in three regions that influence active site accessibility, overview
additional information
the recombinant glycogen synthase-glycogenin-1 complex GYS1:GN1 is functional and exhibits both allosteric and phospho-dependent regulatio, activation of GYS1:GN1 complex by GYS1 dephosphorylationn
additional information
-
the recombinant glycogen synthase-glycogenin-1 complex GYS1:GN1 is functional and exhibits both allosteric and phospho-dependent regulatio, activation of GYS1:GN1 complex by GYS1 dephosphorylationn
additional information
muscle glycogenin contains a single tyrosine, Tyr194, in covalent linkage with the first sugar unit, glucose, beta-phenyl-D-glucopyranoside (beta-PhGlc), confirming that tyrosine is fundamental for glycogen formation. Analysis of the mechanism for the early stages of the biosynthesis of glycogen. This macromolecule structure (PDB ID 3U2U) is constructed via the covalent attachment of glucose units to glycogenin, which remains covalently bonded to Tyr194 in a mature glycogen molecule. Isolation of the Tyr194 side chain in covalent linkage with glucose, of beta-phenyl-D-glucopyranoside, and examined the influence that the substitution of the tyrosine with different interacting reactants has on the preferred interaction sites, preferred interaction site for both alpha- and beta-Glc at body temperature is the 4-OH group of beta-PhGl, overview. The phenolic substituent of tyrosine is ideal, as it provides a rigid structure, acting as a hook for glucose, and the aromatic ring provides a tantalizing interacting environment that most molecules find entropically more favourable. The ability of glycogenin to elongate its glucan chain may reflect structural constraints both in the amino acid and at the catalytic site
additional information
-
aggregation might be an explanation for the incomplete autoglucosylation of wild-type glycogenin-1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D163T
a naturall yoccuring truncating 1-base deletion (c.484delG; p.Asp163Thrfs*5) causes reduced expression of glycogenin-1 protein, the phenotype includes altered morphology, muscle weakness and wasting, overview
G135R
determination of a naturally occuring missense mutation that causes reduced expression of glycogenin-1 protein and abolishes the enzyme's activity and function, phenotype includes altered morphology, muscle weakness and wasting, overview
D163T
naturally occuring mutation c.487del (p.Asp163Thrfs*5) in GYG1 causing glycogen storage disease (GSD) type XV, phenotype, overview
D56H/D160T
naturally occuring mutations c.166G.C (p.Asp56His)/c.472Del (p.Asp160Thr fs*5) in GYG1 causing glycogen storage disease (GSD) type XV, phenotype, overview
T83A
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83C
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83F
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83M
-
naturally occuring mutation, glycogenin-1 with the Thr83Met substitution is unable to form the glucose-O-tyrosine linkage at tyrosine 195 unless co-expressed with the catalytically active Tyr195Phe glycogenin-1. The mutant shows no incorporation of glucose, no autoglycosylation
T83S
-
site-directed mutagenesis, the mutant is catalytically active
T83V
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
T83Y
-
site-directed mutagenesis, the mutant shows no incorporation of glucose, no autoglycosylation
Y195F
-
site-directed mutagenesis, glycogenin-1 with the Thr83Met substitution is unable to form the glucose-O-tyrosine linkage at tyrosine 195 unless co-expressed with the catalytically active Tyr195Phe glycogenin-1
T83M
the Thr83Met mutant is structurally ablated in forming the active state, molecular basis, the mutation is linked with glycogen storage disease XV, GSD type XV. hGYG1T83M is not endogenously glucosylated
T83M
naturally occuring mutation of glycogenin-1, earlier detected in a patient with glycogen depletion in the skeletal muscle, the mutated glycogenin-1 is catalytically inactive and unable to become self-glucosylated or glycosylated by wild-type glycogenin-2, but it can be glucosylated by the catalytically active Y195F glycogenin-1 mutant
additional information
-
non-glucosylated glycogenin-1 constructs, with various amino acid substitutions in position 83 and 195, are expressed in a cell-free expression system and autoglucosylated in vitro
additional information
-
expression analysis of GYG2 in wild-type and GYG1-deficient mutant muscle tissue samples, no expression of GYG2 in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
additional information
expression analysis of GYG2 in wild-type and GYG1-deficient mutant muscle tissue samples, no expression of GYG2 in wild-type skeletal muscle, but glycogenin 2 is detected in the patients, much stronger in the more affected patient 2 than in patient 1
additional information
-
two patients with mutations in the GYG1 gene are investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism, phenotypes, overview
additional information
two patients with mutations in the GYG1 gene are investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism, phenotypes, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Shearer, J.; Wilson, R.J.; Battram, D.S.; Richter, E.A.; Robinson, D.L.; Bakovic, M.; Graham, T.E.
Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle
Am. J. Physiol.
289
E508-514
2005
Homo sapiens
brenda
Barbetti, F.; Rocchi, M.; Bossolasco, R.; et a.
The human skeletal muscle glycogenin gene: cDNA, tissue expression and chromosomal localization
Biochem. Biophys. Res. Commun.
220
72-77
1996
Homo sapiens (P46976), Homo sapiens
brenda
van Maanen, M.H.; Fournier, P.A.; Palmer, T.N.; Abraham, L.J.
Characterization of the human glycogenin-1 gene: identification of a muscle-specific regulatory domain
Gene
234
217-226
1999
Homo sapiens
brenda
Zhai, L.; Mu, J.; Zong, H.; DePaoli-Roach, A.A.; Roach, P.J.
Structure and chromosomal localization of the human glycogenin-2 gene GYG2
Gene
242
229-235
2000
Homo sapiens (P46976), Homo sapiens
brenda
Skurat, A.V.; Dietrich, A.D.; Roach, P.J.
Interaction between glycogenin and glycogen synthase
Arch. Biochem. Biophys.
456
93-97
2006
Homo sapiens
brenda
Wilson, R.J.; Gusba, J.E.; Robinson, D.L.; Graham, T.E.
Glycogenin protein and mRNA expression in response to changing glycogen concentration in exercise and recovery
Am. J. Physiol.
292
E1815-E1822
2007
Homo sapiens (P46976)
brenda
Douillard-Guilloux, G.; Raben, N.; Takikita, S.; Batista, L.; Caillaud, C.; Richard, E.
Modulation of glycogen synthesis by RNA interference: Towards a new therapeutic approach for glycogenosis type II
Hum. Mol. Genet.
17
3876-3886
2008
Homo sapiens
brenda
Nilsson, J.; Halim, A.; Moslemi, A.R.; Pedersen, A.; Nilsson, J.; Larson, G.; Oldfors, A.
Molecular pathogenesis of a new glycogenosis caused by a glycogenin-1 mutation
Biochim. Biophys. Acta
1822
493-499
2012
Homo sapiens
brenda
Chaikuad, A.; Froese, D.; Berridge, G.; Von Delft, F.; Oppermann, U.; Yue, W.
Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis
Proc. Natl. Acad. Sci. USA
108
21028-21033
2011
Homo sapiens (P46976), Homo sapiens
brenda
Nilsson, J.; Halim, A.; Larsson, E.; Moslemi, A.R.; Oldfors, A.; Larson, G.; Nilsson, J.
LC-MS/MS characterization of combined glycogenin-1 and glycogenin-2 enzymatic activities reveals their self-glucosylation preferences
Biochim. Biophys. Acta
1844
398-405
2014
Homo sapiens (O15488), Homo sapiens (P46976)
brenda
Irgens, H.U.; Fjeld, K.; Johansson, B.B.; Ringdal, M.; Immervoll, H.; Leh, S.; Sovik, O.; Johansson, S.; Molven, A.; Njolstad, P.R.
Glycogenin-2 is dispensable for liver glycogen synthesis and glucagon-stimulated glucose release
J. Clin. Endocrinol. Metab.
100
E767-E775
2015
Homo sapiens (O15488), Homo sapiens
brenda
Hunter, R.W.; Zeqiraj, E.; Morrice, N.; Sicheri, F.; Sakamoto, K.
Expression and purification of functional human glycogen synthase-1:glycogenin-1 complex in insect cells
Protein Expr. Purif.
108
23-29
2015
Homo sapiens (P46976), Homo sapiens
brenda
Hedberg-Oldfors, C.; Mensch, A.; Visuttijai, K.; Stoltenburg, G.; Stoevesandt, D.; Kraya, T.; Oldfors, A.; Zierz, S.
Polyglucosan myopathy and functional characterization of a novel GYG1 mutation
Acta Neurol. Scand.
137
308-315
2018
Homo sapiens (P46976)
brenda
Oldfors, A.
Is glycogenin essential for glycogen synthesis?
Cell Metab.
26
12-14
2017
Homo sapiens (O15488), Homo sapiens (P46976), Mus musculus (Q9R062)
brenda
Krag, T.O.; Ruiz-Ruiz, C.; Vissing, J.
Glycogen synthesis in glycogenin 1-deficient patients a role for glycogenin 2 in muscle
J. Clin. Endocrinol. Metab.
102
2690-2700
2017
Homo sapiens, Homo sapiens (O15488)
brenda
Camiruaga, A.; Usabiaga, I.; Insausti, A.; Cocinero, E.; Leon, I.; Fernandez, J.
Understanding the role of tyrosine in glycogenin
Mol. Biosyst.
13
1709-1712
2017
Homo sapiens (P46976)
-
brenda