| + |
MMP10 | down-regulates quantity by destabilization 
cleavage
|
HAPLN1 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256331 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256332 |
Leu40 |
QAENGPHlLVEAEQA |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP10 | up-regulates 
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272355 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
MMP10 | down-regulates 
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272378 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
ZNF267 | down-regulates quantity by repression
transcriptional regulation
|
MMP10 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266211 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16054593 |
Furthermore, ZNF267 binds to the MMP-10 promoter region as demonstrated by chromatin immunoprecipitation assays. In conclusion, our results suggest that ZNF267 as a negative transcriptional regulator of MMP-10 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP6 | up-regulates quantity by expression
transcriptional regulation
|
MMP10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164943 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20418905 |
In this study we show that tre17 is sufficient to induce expression of mmp-9 and mmp-10, in a manner requiring its usp activity, but not its ability to bind arf6. Tre17 induces transcription of mmp-9 through activation of nuclear factor-kappab (nf-kappab), mediated in part by the gtpase rhoa and its effector kinase, rock. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Vincristine sulfate | down-regulates activity
chemical inhibition
|
MMP10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259253 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30599272 |
Vincristine is commonly administered as an effective anti-brain tumor drug. Vincristine treatment also impaired the microtubule-associated protein tubulin, and fibronectin, and downregulated MMP10 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXC1 | up-regulates quantity by expression 
transcriptional regulation
|
MMP10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275915 |
|
|
|
|
| pmid |
sentence |
| 31650548 |
Therefore, FOXC1 is strongly suggested as a pro-metastatic gene in CRC by transcriptionally activating MMP10, SOX4 and SOX13|MMP10 was demonstrated as the direct target and mediator of FOXC1. |
|
| Publications: |
1 |
3.0
MMP10
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