| + |
CLOCK/BMAL1 | down-regulates quantity by repression 
transcriptional regulation
|
VWF |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253703 |
|
|
Mus musculus |
Aorta Endothelium |
| pmid |
sentence |
| 20658528 |
We also show that major circadian transcriptional regulators CLOCK and Bmal1 directly regulate the activity of vWF promoter and that lack of Bmal1 results in upregulation of vWF both at mRNA and protein level. Here we report a direct regulation of vWF expression in endothelial cells by biological clock gene Bmal1. This study establishes a mechanistic connection between Bmal1 and cardiovascular phenotype. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PCSK6 | up-regulates activity 
cleavage
|
VWF |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260367 |
|
|
|
|
| pmid |
sentence |
| 8218226 |
Like PACE,PACE4 was able to process pro-vWF to its mature form, and efficient cleavage required both the P4 arginine and the P2 lysine |
|
| Publications: |
1 |
| + |
NBEAL2 | up-regulates 
|
VWF |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261884 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 28082341 |
Recent in vitro megakaryopoiesis studies using HSCs from GPS patients with NBEAL2 mutations showed normal MK differentiation with defective proplatelet formation and reduced α-granule proteins such as von Willebrand factor (VWF), thrombospondin and P-selectin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Blood vessel damage | up-regulates
|
VWF |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261862 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK559062 |
Exposed VWF bound to collagen from vascular injury and endothelial damage adheres to the GPIb receptor on platelets to initiate signaling pathways for platelet activation, the next step in primary hemostasis. VW|VWF released by Weibel-Palade bodies or alpha-granules can enter circulation or accumulate in the subendothelial matrix binding to collagen through its A3 domain. Once exposed under high shear stress conditions in the arterial circulation, VWF can bind to platelets via its A1 domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARNTL | down-regulates quantity by repression
transcriptional regulation
|
VWF |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253704 |
|
|
Mus musculus |
Aorta Endothelium |
| pmid |
sentence |
| 20658528 |
We also show that major circadian transcriptional regulators CLOCK and Bmal1 directly regulate the activity of vWF promoter and that lack of Bmal1 results in upregulation of vWF both at mRNA and protein level. Here we report a direct regulation of vWF expression in endothelial cells by biological clock gene Bmal1. This study establishes a mechanistic connection between Bmal1 and cardiovascular phenotype. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ADAMTS13 | down-regulates activity
cleavage
|
VWF |
0.619 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23020315 |
Proteolytic degradation of VWF by ADAMTS-13 downregulates the proinflammatory potential of VWF. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VWF | up-regulates quantity by stabilization
|
F8 |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644488 |
VWF plays a crucial role in hemostasis through platelet adhesion facilitation and coagulation factor VIII stabilization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ETS1 | up-regulates quantity by expression
transcriptional regulation
|
VWF |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253915 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9444957 |
Cotransfection of Ets-1 and Erg expression plasmids is sufficient to induce the -60/+19 vWF promoter activity in HeLa cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGG | down-regulates activity
binding
|
VWF |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 2243140 |
Fibrinogen y-chain carboxyterminal (GQQHHLGGAKQAGDV) peptides inhibit fibrinogen, fibronectin (Fn), vitronectin, and von Willebrand factor (vWF) binding to the platelet glycoprotein Ilb-Illa complex (GP lIbII1a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERG | up-regulates quantity by expression
transcriptional regulation
|
VWF |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253914 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9444957 |
Cotransfection of Ets-1 and Erg expression plasmids is sufficient to induce the -60/+19 vWF promoter activity in HeLa cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FURIN | up-regulates activity
cleavage
|
VWF |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260368 |
|
|
|
COS-1 Cell |
| pmid |
sentence |
| 8218226 |
Like PACE,PACE4 was able to process pro-vWF to its mature form, and efficient cleavage required both the P4 arginine and the P2 lysine |
|
| Publications: |
1 |
| + |
VWF | up-regulates activity
binding
|
GPIb-IX-V complex |
0.676 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261853 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 25297919 |
Many studies have contributed to shed light on the importance of von Willebrand factor (VWF) interaction with its platelet receptors, glycoprotein (GP) Ib-IX-V and αIIbβ3 integrin, in promoting primary platelet adhesion and aggregation following vessel injury |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VWF | up-regulates activity
binding
|
AIIB/b3 integrin |
0.671 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261854 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 25297919 |
Many studies have contributed to shed light on the importance of von Willebrand factor (VWF) interaction with its platelet receptors, glycoprotein (GP) Ib-IX-V and αIIbβ3 integrin, in promoting primary platelet adhesion and aggregation following vessel injury |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Platelet_alpha_granule_formation | up-regulates
|
VWF |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261863 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK559062 |
Exposed VWF bound to collagen from vascular injury and endothelial damage adheres to the GPIb receptor on platelets to initiate signaling pathways for platelet activation, the next step in primary hemostasis. VW|VWF released by Weibel-Palade bodies or alpha-granules can enter circulation or accumulate in the subendothelial matrix binding to collagen through its A3 domain. Once exposed under high shear stress conditions in the arterial circulation, VWF can bind to platelets via its A1 domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VWF | up-regulates activity
binding
|
F8 |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23020315 |
Binding of FVIII to VWF is needed to maintain appropriate plasma levels, as FVIII plasma levels and half-life are remarkably reduced in the absence of VWF |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
VWF
- 
- 