| + |
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 |
| + |
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 |
| + |
FBLN2 | up-regulates quantity by stabilization
binding
|
ELN |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282703 |
|
|
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 |
| + |
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 |
| + |
FBN1 | up-regulates quantity by stabilization
binding
|
ELN |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282705 |
|
|
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 |
| + |
ELN | up-regulates activity
binding
|
Av/b3 integrin |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282706 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28544621 |
Tropoelastin is the dominant monomer that assembles to form elastin, which confers elasticity to vertebrate elastic tissues including skin, arteries, and lungs. Tropoelastin interacts with cells through cell surface receptors including integrins and glycosaminoglycans (GAGs). We propose a two-step mechanism by which cell interactions occur at this central region of tropoelastin: initially, cell adhesion is mediated by GAGs, which contact the lysine residues within the target sequence, and subsequently facilitate cell spreading modulated by integrins, specifically αv β3 and αv β5 . We conclude that this region comprises a tropoelastin-derived, cell-interactive sequence that independently mediates potent cell binding and spreading via sequential recognition of GAG and integrin cell surface receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ELN | up-regulates activity
binding
|
Av/b5 integrin |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282707 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28544621 |
Tropoelastin is the dominant monomer that assembles to form elastin, which confers elasticity to vertebrate elastic tissues including skin, arteries, and lungs. Tropoelastin interacts with cells through cell surface receptors including integrins and glycosaminoglycans (GAGs). We propose a two-step mechanism by which cell interactions occur at this central region of tropoelastin: initially, cell adhesion is mediated by GAGs, which contact the lysine residues within the target sequence, and subsequently facilitate cell spreading modulated by integrins, specifically αv β3 and αv β5 . We conclude that this region comprises a tropoelastin-derived, cell-interactive sequence that independently mediates potent cell binding and spreading via sequential recognition of GAG and integrin cell surface receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFEMP2 | up-regulates activity
binding
|
ELN |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252136 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19570982 |
Fibulin-4 directly binds LOX, and this interaction enhances fibulin-4 binding to tropoelastin, thus forming a ternary complex that may be critical for elastin cross-linking. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
ELN
- 
- 