| + |
FBLN5 | up-regulates 
binding
|
ELN |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186603 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19570982 |
Our data show that fibulin-5 can interact with tropoelastin or with fibrillin-1, implying a chaperone role for fibulin-5 in directing elastin onto microfibrils |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBN1 | down-regulates activity 
binding
|
FBLN5 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252138 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19570982 |
Fibulin-4 and -5 are extracellular glycoproteins with essential non-compensatory roles in elastic fiber assembly. We have determined how they interact with tropoelastin, lysyl oxidase, and fibrillin-1, thereby revealing how they differentially regulate assembly. Both fibulins differentially bound N-terminal fibrillin-1, which strongly inhibited their binding to lysyl oxidase and tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN5 | up-regulates activity
binding
|
ELN |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252137 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18267938 |
The binding of tropoelastin fragments to fibulin-5 was directly proportional to their propensity to coacervate. Furthermore, the addition of fibulin-5 to tropoelastin facilitated coacervation. Taken together, the present study shows that fibulin-5 enhances elastic fiber formation in part by improving the self-association properties of tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN5 | up-regulates quantity by stabilization
binding
|
FBN1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17255108 |
Using a panel of recombinant fibrillin-1 swapped domain and deletion fragments, we demonstrate here that the conserved first hybrid domain in fibrillin-1 is essential for binding to fibulin-2, -4, and -5.Formation of ternary complexes between fibrillin-1, fibulins, and tropoelastin demonstrated that fibulin-2 and -5 but much less fibulin-4, are able to act as molecular adaptors between fibrillin-1 and tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN5 | up-regulates quantity by stabilization
binding
|
ELN |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282704 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17255108 |
Using a panel of recombinant fibrillin-1 swapped domain and deletion fragments, we demonstrate here that the conserved first hybrid domain in fibrillin-1 is essential for binding to fibulin-2, -4, and -5.Formation of ternary complexes between fibrillin-1, fibulins, and tropoelastin demonstrated that fibulin-2 and -5 but much less fibulin-4, are able to act as molecular adaptors between fibrillin-1 and tropoelastin.However, when fibulin-2 or -5 was added to the binding assay, rF16 strongly interacted with tropoelastin, whereas fibulin-4 only marginally mediated the formation of this ternary complex. These data demonstrate that at least fibulin-2 and -5 can mediate binding of fibrillin-1 to tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
FBLN5
- 
- 