Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to
assemble and peer-review its pathway modules. The integration of ORCID within Reactome
enables us to meet a key challenge with authoring, curating and reviewing biological
information by incentivizing and crediting the external experts that contribute their
expertise and time to the Reactome curation process. More information is available at
ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please
forward this information to us and we will update your Reactome pathway records.
Details on Person Thrombospondin-1 (THBS1) is a trimeric protein held together...
| Class:Id | Summation:4086221 |
| _displayName | Thrombospondin-1 (THBS1) is a trimeric protein held together... |
| _timestamp | 2013-08-07 15:58:05 |
| created | [InstanceEdit:4086135] Jupe, S, 2013-08-07 |
| literatureReference | [LiteratureReference:4086193] Synthesis of truncated amino-terminal trimers of thrombospondin [LiteratureReference:4086109] Isolation and characterization of a high molecular weight glycoprotein from human blood platelets [LiteratureReference:4086142] Binding and degradation of thrombospondin-1 mediated through heparan sulphate proteoglycans and low-density-lipoprotein receptor-related protein: localization of the functional activity to the trimeric N-terminal heparin-binding region of thrombospondin-1 [LiteratureReference:4086165] Thrombospondin-1: multiple paths to inflammation [LiteratureReference:4086151] Isolation of the thrombospondin membrane receptor [LiteratureReference:4086118] Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin [LiteratureReference:4086196] Identification of integrin alpha 3 beta 1 as a neuronal thrombospondin receptor mediating neurite outgrowth [LiteratureReference:4086159] Activated T-cell adhesion to thrombospondin is mediated by the alpha 4 beta 1 (VLA-4) and alpha 5 beta 1 (VLA-5) integrins [LiteratureReference:4086161] Recognition of the N-terminal modules of thrombospondin-1 and thrombospondin-2 by alpha6beta1 integrin [LiteratureReference:4086129] Alpha4beta1 integrin mediates selective endothelial cell responses to thrombospondins 1 and 2 in vitro and modulates angiogenesis in vivo [LiteratureReference:4086180] Trimeric assembly of the C-terminal region of thrombospondin-1 or thrombospondin-2 is necessary for cell spreading and fascin spike organisation |
| modified | [InstanceEdit:4086244] Jupe, S, 2013-08-07 |
| text | Thrombospondin-1 (THBS1) is a trimeric protein held together by interchain disulphide bonds at Cys-252 and Cys-256 (Sottile et al. 1991). It was originally identified as a platelet alpha granule protein (Lawler et al. 1978) and subsequently found to be produced and secreted by a number of cell types such as endothelial cells, fibroblasts, adipocytes, smooth muscle cells, monocytes, macrophages, and transformed cells such as malignant glioma cells. Proposed functions include an involvement in platelet aggregation, cell adhesion, cell growth, angiogenesis, binding and activation of latent transforming growth factor-b and regulation of protease activities (Chen et al. 1996, Lopez-Dee et al. 2011). Several TSP-1 receptors have been identified, including CD36 (Asch et al. 1987) and several integrins including alphavbeta3 (Sun et al. 1992), alpha3beta1 (DeFreitas et al. 1995), alpha4beta1, alpha5beta1 (Yabowitz et al. 1993), and either alpha2bbeta3 or alpha2beta1 (Tuszynski & Kowalska 1991). Integrins alpha4beta1 and alpha6beta1 binds THBS1 and the related trimeric THBS2 (Anilkumar et al. 2002, Calzada et al. 2003, 2004). |
| (summation) | [Reaction:4086185] Thrombospondin 1 and 2 bind integrin alpha6beta1 [Homo sapiens] |
|
[Change default viewing format]
|
No pathways have been reviewed or authored by Thrombospondin-1 (THBS1) is a trimeric protein held together... (4086221)