| + |
MMP1 | down-regulates quantity by destabilization 
cleavage
|
COL2A1 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272338 |
Gly774 |
RGDVGEKgPEGAPGK |
in vitro |
|
| pmid |
sentence |
| 17318226 |
In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775–Ile776 or Gly775–Lys776 in native type I, II or III collagen molecules3,4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256341 |
Gly906 |
EGPPGPQgLAGQRGI |
Homo sapiens |
|
| pmid |
sentence |
| 8609233 |
MMP-1 cleaves type II collagen at the peptide bond Gly906-Leu907 Proteolysis of triple-helical collagen is an important step in the progression toward irreversible tissue damage in osteoarthritis. Earlier work on the expression of enzymes in cartilage suggested that collagenase-1 (MMP-1) contributes to the process. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
MMP1 | down-regulates quantity by destabilization
cleavage
|
COL3A1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272339 |
Gly774 |
IGPPGPAgQPGDKGE |
in vitro |
|
| pmid |
sentence |
| 17318226 |
In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775–Ile776 or Gly775–Lys776 in native type I, II or III collagen molecules3,4. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP1 | down-regulates quantity by destabilization
cleavage
|
COL1A2 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272337 |
Gly775 |
NGPPGPAgSRGDGGP |
in vitro |
|
| pmid |
sentence |
| 17318226 |
In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775–Ile776 or Gly775–Lys776 in native type I, II or III collagen molecules3,4. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP1 | down-regulates quantity by destabilization
cleavage
|
COL1A1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272336 |
Gly776 |
IGPPGPAgAPGDKGE |
in vitro |
|
| pmid |
sentence |
| 17318226 |
In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775–Ile776 or Gly775–Lys776 in native type I, II or III collagen molecules3,4. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FBN1 | up-regulates quantity by expression 
transcriptional regulation
|
MMP1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251887 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16442122 |
In this study we show that a fibrillin-1 fragment containing a EGFEPG sequence that conforms to a putative GxxPG elastin-binding protein (EBP) consensus sequence upregulates the expression and production of matrix metalloproteinase (MMP)-1 by up to ninefold in a cell culture system. Mutations in the gene for fibrillin-1 cause Marfan syndrome (MFS), a common hereditary disorder of connective tissue |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP1 | up-regulates
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272354 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
MMP1 | up-regulates
|
Angiogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252265 |
|
|
Homo sapiens |
SUM-102 Cell |
| pmid |
sentence |
| 19584257 |
However, we show that soluble factors secreted by SUM102 breast cancer cells stimulated the expression of MMP-1 and CXCR4 in HMFs. As a result, these stromal cells acquired an invasive and migratory phenotype |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZNF384 | up-regulates quantity by expression 
transcriptional regulation
|
MMP1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266229 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10669742 |
Luciferase activity driven by the MMP-1 promoter also increased by 2.5- to 3-fold. In contrast, CIZ had no effect on the luciferase activity from the MMP-1 promoter that was mutated at the CIZ binding consensus sequence. These results show that the CIZ transactivates the MMP-1 promoter through this sequence. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CITED2 | down-regulates quantity by repression 
transcriptional regulation
|
MMP1 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253778 |
|
|
Homo sapiens |
C-28/I2 Cell |
| pmid |
sentence |
| 12960175 |
CITED2 plays a major role in shear-induced down-regulation of MMP-1 and MMP-13 via a transforming growth factor-beta-dependent pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP1 | down-regulates
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272377 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
ZMYND8 | down-regulates quantity by repression
transcriptional regulation
|
MMP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262042 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 27477906 |
Our quantitative ChIP experiments confirmed that ZMYND8 and JARID1D were co-localized at Slug, CD44, VEGFA, and EGFR genes (Figures 4F–4I). Our ChIP results also showed that ZMYND8 repressed and occupied other JARID1D target genes, such as the matrix metalloproteinase 1 (MMP1) and MMP3, that we previously reported |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MMP1
- 
- 