3.4.24.17: stromelysin 1
This is an abbreviated version!
For detailed information about stromelysin 1, go to the full flat file.
Word Map on EC 3.4.24.17
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3.4.24.17
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metalloproteinases
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mmp-1
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cartilage
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arthritis
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joint
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osteoarthritis
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rheumatoid
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synovial
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chondrocytes
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necrosis
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timps
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articular
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gelatinase
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tnf
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interleukin-1
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knee
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zymography
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degeneration
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aggrecan
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proteoglycans
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c-reactive
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interstitial
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gelatin
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plasminogen
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proteinases
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cox-2
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synoviocytes
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il-1beta
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fibroblast-like
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cruciate
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intervertebral
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ligament
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matrilysin
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pulposus
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matrix-degrading
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adamts-4
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synovitis
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thrombospondin
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intra-articular
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subchondral
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emmprin
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chondroprotective
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photoaging
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collagenases
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diagnostics
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medicine
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aggrecanase
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prommp-9
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neoepitope
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gelatinolytic
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mt1-mmp
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collagenolytic
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drug development
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analysis
- 3.4.24.17
- metalloproteinases
- mmp-1
- cartilage
- arthritis
- joint
- osteoarthritis
-
rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
-
articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
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c-reactive
-
interstitial
- gelatin
- plasminogen
- proteinases
- cox-2
- synoviocytes
- il-1beta
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fibroblast-like
-
cruciate
-
intervertebral
- ligament
- matrilysin
- pulposus
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matrix-degrading
- adamts-4
- synovitis
- thrombospondin
-
intra-articular
-
subchondral
-
emmprin
-
chondroprotective
-
photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
-
prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
-
collagenolytic
- drug development
- analysis
Reaction
preferential cleavage where P1', P2' and P3' are hydrophobic residues =
Synonyms
Collagen-activating protein, Collagenase activating protein, matrix metalloprotease-3, Matrix metalloproteinase 3, matrix metalloproteinase-3, matrixin, MMP-3, MMP3, Neutral proteoglycanase, Procollagenase activator, Proteoglycanase, PTR1 protein, ST1, Stromelysin, stromelysin-1, Transin
ECTree
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Engineering
Engineering on EC 3.4.24.17 - stromelysin 1
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E219A
additional information
E219A
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NMR studies used MMP-12 preserved by E219A substitution of the general base
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catalytic domain (residues 83-247) are used in this study
additional information
overexpression of wild-type MMP-3 results in an increase in the 35 kD caspase-9 accompanied by increased caspase-9 enzymatic activity, while overexpression of mutant E219A cDNA that produces enzymatically inactive MMP-3, yields no apparent change
additional information
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enzyme overexpression im lymphoma transfectants significantly improves their ability to migrate through the matrix. Animals injected with lymphoma cells expressing enzyme constitutively develop thymic lymphoma more rapidly than those injected with control cells. Local expression of enzyme promotes lymphoma progression
additional information
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Less disruption of blood-brain barrier after intracerebral lipopolysaccharide injection in enzyme knockout animals than in wild-type. Mutant animals show lower level of matrix metalloproteinase MMP-9 but similar levels of activation as wild-type
additional information
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generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-3 catalytic domain
additional information
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MMP-3-/- mice kept on high fat diet show adipocyte hypertrophy in adipose tissues
additional information
MMP-3 deficient mice are crossed back to a homozygous BL10 background for 10 generations as described above. Male MMP-3 knock-out and BL10 wild-type mice are used for the experimental setting
additional information
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MMP-3 deficient mice are crossed back to a homozygous BL10 background for 10 generations as described above. Male MMP-3 knock-out and BL10 wild-type mice are used for the experimental setting
additional information
Mus musculus BL10
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MMP-3 deficient mice are crossed back to a homozygous BL10 background for 10 generations as described above. Male MMP-3 knock-out and BL10 wild-type mice are used for the experimental setting
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additional information
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generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-3 catalytic domain
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