| + |
BMPR1A | up-regulates 
phosphorylation
|
SMAD1 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-210084 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249649 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187181 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
FAM83G |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264765 |
Ser610 |
GPGPRRPsVASSVSE |
Homo sapiens |
|
| pmid |
sentence |
| 24554596 |
These results indicate that ALK3 phosphorylates PAWS1 predominantly at Ser610 but can also phosphorylate at Ser614 and Ser616 in vitro. |Here, we report the discovery and characterization of PAWS1/FAM83G as a novel SMAD1 interactor. PAWS1 forms a complex with SMAD1 in a SMAD4-independent manner, and BMP signalling induces the phosphorylation of PAWS1 through BMPR1A. The phosphorylation of PAWS1 in response to BMP is essential for activation of the SMAD4-independent BMP target genes NEDD9 and ASNS. Our findings identify PAWS1 as the first non-SMAD substrate for type I BMP receptor kinases and as a novel player in the BMP pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264766 |
Ser614 |
RRPSVASsVSEEYFE |
in vitro |
|
| pmid |
sentence |
| 24554596 |
These results indicate that ALK3 phosphorylates PAWS1 predominantly at Ser610 but can also phosphorylate at Ser614 and Ser616 in vitro. |Here, we report the discovery and characterization of PAWS1/FAM83G as a novel SMAD1 interactor. PAWS1 forms a complex with SMAD1 in a SMAD4-independent manner, and BMP signalling induces the phosphorylation of PAWS1 through BMPR1A. The phosphorylation of PAWS1 in response to BMP is essential for activation of the SMAD4-independent BMP target genes NEDD9 and ASNS. Our findings identify PAWS1 as the first non-SMAD substrate for type I BMP receptor kinases and as a novel player in the BMP pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264767 |
Ser616 |
PSVASSVsEEYFEVR |
in vitro |
|
| pmid |
sentence |
| 24554596 |
These results indicate that ALK3 phosphorylates PAWS1 predominantly at Ser610 but can also phosphorylate at Ser614 and Ser616 in vitro. |Here, we report the discovery and characterization of PAWS1/FAM83G as a novel SMAD1 interactor. PAWS1 forms a complex with SMAD1 in a SMAD4-independent manner, and BMP signalling induces the phosphorylation of PAWS1 through BMPR1A. The phosphorylation of PAWS1 in response to BMP is essential for activation of the SMAD4-independent BMP target genes NEDD9 and ASNS. Our findings identify PAWS1 as the first non-SMAD substrate for type I BMP receptor kinases and as a novel player in the BMP pathway. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, In Vitro |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD1 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255263 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity 
|
SMAD1/4 |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255787 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19620713 |
The expression of CA-BMPr1A and CA-BMPr1B mRNA was confirmed by RT-PCR using appropriate primers to distinguish expression of the constitutively active receptors from endogenous BMP receptors; specific antibodies for these receptors were not available. However, the functional effects of their expression, i.e., phosphorylation of Smad1/5/8 and p38 MAPK, verify overexpression of the constitutively active receptors (Fig. 3B). Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway (Fig. 3B) (16, 17). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1A | up-regulates
|
SMAD5 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235361 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1A | up-regulates activity
|
MAP3K7 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255815 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 8533096 |
We also examined whether TAK1 was activated by bone morphogenetic protein (BMP). BMP-4 also stimulated TAK1 activity in a time- and dose-dependent manner |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMURF2 | down-regulates 
ubiquitination
|
BMPR1A |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR2 | up-regulates
binding, phosphorylation
|
BMPR1A |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33440 |
|
|
Chlorocebus aethiops |
|
| 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-180545 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18756288 |
Bmp ligands bind to the bmp receptors bmpr1 and bmpr2, and bmpr2 then phosphorylates and activates bmpr1. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
BMP10 | up-regulates
binding
|
BMPR1A |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139052 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16049014 |
We showed that three orphan ligands known to be important for joint and cartilage formation (gdf6) (10), interneuron, sensory neurons, and seminal vesicle formation (gdf7) (11_13), and heart development (bmp10) (14) used the type i receptors alk3 or alk6 and the type ii receptors bmprii or actriia to activate the smad1/5/8 proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Heart |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD9 |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255772 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
To ascertain whether overexpression of BMPr1A can initiate adipocyte lineage commitment in the absence of its BMP ligand, constitutively active (CA)-BMPr1A and CA-BMPr1B were expressed in C3H10T1/2 stem cells using a mouse stem cell virus (MSCV) retroviral system. […]Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | form complex 
binding
|
BMPR1A/1B/2 |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255257 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7791754 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors (br-ia and br-ib) and the bmp type ii receptor (br-ii). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTDNEP1 | up-regulates
binding
|
BMPR1A |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150998 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17141153 |
We show that dullard promotes the ubiquitin-mediated proteosomal degradation of bmp receptors (bmprs). Dullard preferentially complexes with the bmp type ii receptor (bmprii) and partially colocalizes with the caveolin-1-positive compartment, suggesting that dullard promotes bmpr degradation via the lipid raft-caveolar pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates
|
SOST |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188958 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19874086 |
These results demonstrate that bmpria in osteoblasts negatively regulates endogenous bone mass and wnt/beta-catenin signaling and that this regulation may be mediated by the activities of sost and dkk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD5/SMAD4 |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255788 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19620713 |
The expression of CA-BMPr1A and CA-BMPr1B mRNA was confirmed by RT-PCR using appropriate primers to distinguish expression of the constitutively active receptors from endogenous BMP receptors; specific antibodies for these receptors were not available. However, the functional effects of their expression, i.e., phosphorylation of Smad1/5/8 and p38 MAPK, verify overexpression of the constitutively active receptors (Fig. 3B). Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway (Fig. 3B) (16, 17). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255779 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9442019 |
In this study, we isolated human Smad5 and found that Smad5 was involved in BMP-2 signaling cascades, which mediate the bone-inducing effects of BMP-2. Smad5 was directly serine-phosphorylated by BMPIR through a physical interaction. The activated Smad5 subsequently formed a complex with DPC4, and this complex was then translocated to the nucleus. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
NOG | down-regulates activity
binding
|
BMPR1A |
0.615 |
| 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. |
|
| 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) |
|
| Publications: |
2 |
Organism: |
Gallus Gallus, Homo Sapiens |
| Tissue: |
Bone |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD5 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255261 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD1/4 |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255778 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8893010 |
Conversely, Smad1 and DPC4 formed a complex when the cells were stimulated with BMP4 but not with activin of TGF-beta. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AXIN1 | down-regulates
ubiquitination
|
BMPR1A |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195552 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Other proteins, such as the serine/threonine kinase fused (fu), can function in concert with the e3 ligase smurf to regulate ubiquitination and proteolysis of the bmp receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF | down-regulates
ubiquitination
|
BMPR1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270212 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF1 | down-regulates
ubiquitination
|
BMPR1A |
0.661 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195651 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degradation of smads and receptors for tgf-beta and bmps. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153399 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17317136 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degradation of smads and receptors for tgf-beta and bmps. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD1/5/8 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255831 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 19620713 |
The expression of CA-BMPr1A and CA-BMPr1B mRNA was confirmed by RT-PCR using appropriate primers to distinguish expression of the constitutively active receptors from endogenous BMP receptors; specific antibodies for these receptors were not available. However, the functional effects of their expression, i.e., phosphorylation of Smad1/5/8 and p38 MAPK, verify overexpression of the constitutively active receptors (Fig. 3B). Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway (Fig. 3B) (16, 17). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255830 |
|
|
Homo sapiens |
C2C12 Cell, HEK-293-EBNA Cell, L-6 Myoblast Cell |
| pmid |
sentence |
| 9442019 |
In this study, we isolated human Smad5 and found that Smad5 was involved in BMP-2 signaling cascades, which mediate the bone-inducing effects of BMP-2. Smad5 was directly serine-phosphorylated by BMPIR through a physical interaction. The activated Smad5 subsequently formed a complex with DPC4, and this complex was then translocated to the nucleus. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD8/SMAD4 |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255786 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19620713 |
The expression of CA-BMPr1A and CA-BMPr1B mRNA was confirmed by RT-PCR using appropriate primers to distinguish expression of the constitutively active receptors from endogenous BMP receptors; specific antibodies for these receptors were not available. However, the functional effects of their expression, i.e., phosphorylation of Smad1/5/8 and p38 MAPK, verify overexpression of the constitutively active receptors (Fig. 3B). Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway (Fig. 3B) (16, 17). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMP2 | up-regulates
binding
|
BMPR1A |
0.928 |
| 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 |
| + |
4-[6-[4-(1-piperazinyl)phenyl]-3-pyrazolo[1,5-a]pyrimidinyl]quinoline | down-regulates
chemical inhibition
|
BMPR1A |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193642 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMP2 | up-regulates activity
binding
|
BMPR1A |
0.928 |
| 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 |
| + |
BMPR1A | up-regulates activity
|
MAPK14 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255785 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19620713 |
The expression of CA-BMPr1A and CA-BMPr1B mRNA was confirmed by RT-PCR using appropriate primers to distinguish expression of the constitutively active receptors from endogenous BMP receptors; specific antibodies for these receptors were not available. However, the functional effects of their expression, i.e., phosphorylation of Smad1/5/8 and p38 MAPK, verify overexpression of the constitutively active receptors (Fig. 3B). Thus, their overexpression provoked a substantial rise in the phosphorylation of Smad1/5/8 and p38 MAPK, known downstream phosphorylated intermediates in the BMP signaling pathway (Fig. 3B) (16, 17). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMP4 | up-regulates
binding
|
BMPR1A |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253548 |
|
|
|
|
| pmid |
sentence |
| 26330344 |
BMP interacts with specific receptors on the cell surface, BMP receptor types 1 and 2 (BMPr1 and BMPr2). |
|
| Publications: |
1 |
| + |
SMAD6 | down-regulates 
|
BMPR1A |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236861 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1A | up-regulates
binding
|
BMPR2 |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75652 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1A | up-regulates
phosphorylation
|
SMAD5 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187184 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR2 | up-regulates activity
binding
|
BMPR1A |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255781 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known BMP type I receptors (BR-Ia and BR-Ib) and the BMP type II receptor (BR-II). Coimmunoprecipitation studies detected the formation of heteromeric and homomeric complexes among all the BMP receptor types even in the absence of ligand. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1A | up-regulates
binding
|
BMPR1B |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75649 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GDF6 | up-regulates
binding
|
BMPR1A |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16049014 |
We found that transfection of small hairpin rna for bmprii and actriia in mc3t3 cells suppressed the signaling of gdf6, gdf7, and bmp10. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
BMPR1A
- 
- 