+ |
BMP2 | up-regulates activity
binding
|
BMPR2 |
0.793 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144101 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
7791754 |
Under our assay conditions, bmp-2 binds better to bmpr-ii in combination with actr-i or bmpr-ib than in combination with bmpr-ia |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
BMP2 | up-regulates activity
binding
|
BMPR1A |
0.927 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255771 |
|
|
in vitro |
|
pmid |
sentence |
18937504 |
Here we report the high-resolution NMR structure of BMPR-IA ECD in solution, revealing that a large part of the ligand-binding epitope is unfolded and flexible before formation of the complex. The binding beta4beta5 loop of BMPR-IA passes through a structural rearrangement upon BMP-2 binding. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
IHH | up-regulates
|
BMP2 |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195609 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Ihh is found to be required for bmp-induced os-teogenesis of a limb-bud cell line in culture. Ihh sig-naling is directly required for the osteoblast lineage in developing long bones. Ihh functions in conjunction with other factors such as bmps to induce osteoblast differentiation. In vivo, ihh acts on potential progeni-tor cells to promote osteoblast differentiation and prevent chondrocyte differentiation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-122200 |
|
|
Homo sapiens |
|
pmid |
sentence |
14973297 |
Ihh is found to be required for bmp-induced os-teogenesis of a limb-bud cell line in culture. Ihh sig-naling is directly required for the osteoblast lineage in developing long bones. Ihh functions in conjunction with other factors such as bmps to induce osteoblast differentiation. In vivo, ihh acts on potential progeni-tor cells to promote osteoblast differentiation and prevent chondrocyte differentiation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates quantity by expression
transcriptional regulation
|
OMD |
0.316 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149562 |
|
|
Homo sapiens |
|
pmid |
sentence |
16970923 |
Bmp-2 up regulates osad |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
binding
|
BMP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236166 |
|
|
Homo sapiens |
|
pmid |
sentence |
11178121 |
Bmps are dimeric proteins with a single interchain disulfide bond. The dimeric conformation is an absolute requirement for the biological action and interaction with receptors |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
BMP2 | down-regulates quantity by repression
transcriptional regulation
|
SHH |
0.532 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188853 |
|
|
Homo sapiens |
|
pmid |
sentence |
19855020 |
On the other hand, bmp activity negatively regulates shh transcription and a bmp-shh nega-tive-feedback loop serves to confine shh expression during limb development. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
|
SMAD5 |
0.688 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195564 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Neogenin, a transmembranous protein, was re-ported to regulate bmp receptor association with lipid raft, where bmp induces canonical smad1/5/8 phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
|
SMAD1 |
0.64 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195561 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Neogenin, a transmembranous protein, was reported to regulate bmp receptor association with lipid raft, where bmp induces canonical smad1/5/8 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
binding
|
BMPR1A/1B/2 |
0.856 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217532 |
|
|
Homo sapiens |
|
pmid |
sentence |
7791754 |
Bmpr-ii is a transmembrane serine/threonine kinase that binds bmp-2 and bmp-7 in association with multiple type i receptors, including bmpr-ia/brk1, bmpr-ib, and actr-i, which is also an activin type i receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-237000 |
|
|
Mus musculus |
MC3T3-E1 Cell |
pmid |
sentence |
11714695 |
For this, bmp-2 binds first to the high affinity receptor bri and then recruits brii into the signaling complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
+ |
BMP2 | up-regulates
|
SMAD1/5/8 |
0.69 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269848 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Neogenin, a transmembranous protein, was reported to regulate bmp receptor association with lipid raft, where bmp induces canonical smad1/5/8 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
|
SMAD9 |
0.635 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195567 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Neogenin, a transmembranous protein, was re-ported to regulate bmp receptor association with lipid raft, where bmp induces canonical smad1/5/8 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FGF9 | up-regulates quantity by expression
transcriptional regulation
|
BMP2 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195591 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Fgf-2 and fgf-9 increased expression of other osteogenic factors bmp-2 and tgf-beta1, and endogenous fgf/fgfr signaling is a positive upstream regulator of the bmp-2 gene in calvarial osteoblasts. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134794 |
|
|
Homo sapiens |
|
pmid |
sentence |
15780951 |
Fgf-2 and fgf-9 increased expression of other osteogenic factors bmp-2 and tgf-beta1, and endogenous fgf/fgfr signaling is a positive upstream regulator of the bmp-2 gene in calvarial osteoblasts. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
FGF2 | up-regulates quantity by expression
transcriptional regulation
|
BMP2 |
0.486 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134785 |
|
|
Homo sapiens |
|
pmid |
sentence |
15780951 |
Furthermore, FGF-2 and FGF-9 increased expression of other osteogenic factors BMP-2 and TGFbeta-1. Meanwhile, blocking endogenous FGF signaling, using a virally transduced dominant-negative FGF receptor (FgfR), resulted in drastically reduced expression of the BMP-2 gene, demonstrating for the first time that endogenous FGF/FgfR signaling is a positive upstream regulator of the BMP-2 gene in calvarial osteoblasts |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RUNX2 | up-regulates quantity by expression
transcriptional regulation
|
BMP2 |
0.51 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134515 |
|
|
Homo sapiens |
|
pmid |
sentence |
15765505 |
Runx2 is an important mediator of the expression of bmp-2 in response to fgf stimulation in cranial bone development |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
binding
|
BMPR1A |
0.927 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253547 |
|
|
|
|
pmid |
sentence |
26330344 |
BMP interacts with specific receptors on the cell surface, BMP receptor types 1 and 2 (BMPr1 and BMPr2). |
|
Publications: |
1 |
+ |
SOSTDC1 | down-regulates activity
|
BMP2 |
0.582 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-242746 |
|
|
Mus musculus |
|
pmid |
sentence |
18032587 |
SOSTDC1 is orthologous to a recently characterized murine antagonist of BMPs-2, -4, and -7 |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
NOG | down-regulates
binding
|
BMP2 |
0.804 |
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 |
+ |
BMP2 | up-regulates
|
MAPK14 |
0.401 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98369 |
|
|
Homo sapiens |
|
pmid |
sentence |
12589053 |
Specific inhibitors for p38 kinase inhibited bmp2-induced adipocytic differentiation and transcriptional activation of ppargamma, whereas overexpression of smad6 had no effect on transcriptional activity of ppargamma. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GLI2 | up-regulates quantity by expression
transcriptional regulation
|
BMP2 |
0.441 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-148346 |
|
|
Homo sapiens |
|
pmid |
sentence |
16880529 |
The zinc finger transcription factor gli2 mediates bone morphogenetic protein 2 expression in osteoblasts in response to hedgehog signaling |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
binding
|
BMPR2 |
0.793 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-33425 |
|
|
Homo sapiens |
|
pmid |
sentence |
7791754 |
Bmpr-ii is a transmembrane serine/threonine kinase that binds bmp-2 and bmp-7 in association with multiple type i receptors, including bmpr-ia/brk1, bmpr-ib, and actr-i, which is also an activin type i receptor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
|
ALPL |
0.449 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-114589 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
FGF-2 null mice have impaired nuclear accumulation of Runx2 and hindered BMP-2 induced bone formation and ALP activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BMP2 | up-regulates
|
SMAD2 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-175273 |
|
|
Homo sapiens |
|
pmid |
sentence |
21793042 |
Upon bmp binding to the bmpr-ii, bmpr-i is recruited to form an activated quaternary complex, which then phosphorylates and activates intracellular smad proteins. Receptor smads bind to a co-smad and translocate to the nucleus to serve as transcription factors. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |