| + |
NOG | down-regulates 
binding
|
BMPR1A/1B/2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217529 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmpby blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12478285 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmpby blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NOG | down-regulates activity
binding
|
BMPR1A |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192799 |
|
|
Homo sapiens |
Osteoblast |
| pmid |
sentence |
| 22298955 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptorsNoggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors (pmid 12478285) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219221 |
|
|
Gallus gallus |
|
| pmid |
sentence |
| 12478285 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors (PMID 22298955).Noggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Gallus Gallus |
| Tissue: |
Bone |
| + |
NOG | down-regulates
binding
|
BMP2 |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100657 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12700180 |
Noggin acts by binding bmps, thus preventing them from binding to their receptors (180). Noggin binds with various degrees of affinity bmp-2, -4, -5, -6, and -7, gdf-5, gdf-6, and vg1, but not other members of the tgf- family of peptides |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOG | down-regulates activity
binding
|
BMPR2 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195612 |
|
|
Homo sapiens |
Osteoblast |
| pmid |
sentence |
| 22298955 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors (pmid 12478285) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219225 |
|
|
Gallus gallus |
|
| pmid |
sentence |
| 12478285 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors (PMID 22298955). Noggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Gallus Gallus |
| Tissue: |
Bone |
| + |
NOG | down-regulates activity
binding
|
GDF5 |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252420 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21976273 |
Growth and differentiation factor 5 (GDF5), a member of the bone morphogenetic protein (BMP) family, is essential for cartilage, bone, and joint formation. Antagonists such as noggin counteract BMP signaling by covering the ligand's BMP type I (BMPRI) and type II (BMPRII, ActRII, ActRIIB) interaction sites. The mutation GDF5-S94N is located within the BMPRII interaction site, the so-called knuckle epitope, and was identified in patients suffering from multiple synostoses syndrome (SYNS). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19956691 |
We identified two mutations (N445K,T) in patients with multiple synostosis syndrome (SYM1) in the BMP–related ligand GDF5. Residue N445, situated within overlapping receptor and antagonist interfaces, is highly conserved among the BMP family with the exception of BMP9 and BMP10, in which it is substituted with lysine. Like the mutant GDF5, both BMPs are insensitive to NOGGIN and show a high chondrogenic activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NOG | down-regulates activity
binding
|
BMP7 |
0.853 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256484 |
|
|
in vitro |
|
| pmid |
sentence |
| 12478285 |
We report the crystal structure of the antagonist Noggin bound to BMP-7, which shows that Noggin inhibits BMP signalling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NOG | down-regulates
binding
|
BMP4 |
0.814 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100660 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12700180 |
Noggin acts by binding bmps, thus preventing them from binding to their receptors (180). Noggin binds with various degrees of affinity bmp-2, -4, -5, -6, and -7, gdf-5, gdf-6, and vg1, but not other members of the tgf- family of peptides |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOG | down-regulates activity
binding
|
BMPR1B |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192802 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors (pmid 12478285) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NOG
- 
- 