about
Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complexIdentification and structure of the anti-sigma factor-binding domain of the disulphide-stress regulated sigma factor sigma(R) from Streptomyces coelicolorThe heparin binding site of protein C inhibitor is protease-dependentHighly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot.Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.Thrombin inhibition by serpins disrupts exosite IIRegulation of bone morphogenetic protein 9 (BMP9) by redox-dependent proteolysis.The promise of recombinant BMP ligands and other approaches targeting BMPR-II in the treatment of pulmonary arterial hypertensionStructural insights into the multiple functions of protein C inhibitor.The Prodomain-bound Form of Bone Morphogenetic Protein 10 Is Biologically Active on Endothelial Cells.Regulation of the ALK1 ligands, BMP9 and BMP10.Crystal structure of wild-type human thrombin in the Na+-free state.The Role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor.Identification of rare sequence variation underlying heritable pulmonary arterial hypertension.Increased Antielastase Activity in Idiopathic Pulmonary Arterial Hypertension and Chronic Thromboembolic Pulmonary HypertensionDual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactionsThe Impact of Hypoxia on Neutrophil Degranulation and Consequences for the HostA Bone Morphogenetic Protein (BMP)-derived Peptide Based on the Type I Receptor-binding Site Modifies Cell-type Dependent BMP SignallingMolecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound formsCharacterization of GDF2 Mutations and Levels of BMP9 and BMP10 in Pulmonary Arterial HypertensionLetter by Morrell et al Regarding Article, "Selective BMP-9 Inhibition Partially Protects Against Experimental Pulmonary Hypertension"Advances in the molecular regulation of endothelial BMP9 signalling complexes and implications for cardiovascular diseaseRole of soluble endoglin in BMP9 signaling
P50
Q24657851-A0A0ED8A-8243-48BE-A101-1F52465C0284Q27639824-457BB08B-58ED-46B4-8247-FBFD5E35168AQ27652705-3FC2507E-D7C7-4476-9836-B77404DFD978Q33199487-C81BE64C-60A5-4520-99BA-2B2399EFEB5EQ34341165-8F8AD6CA-365F-4EF7-9F90-3D48F7E322AEQ34352365-EC373D3C-FD80-42FA-BDC1-AE2AD820DACEQ34467523-583AD22B-FBCE-4E52-B4EF-26C84941D1FAQ36457064-D359F332-615A-4C12-BA58-5660E1A0D46FQ37279913-27C04E2D-B8E1-4D5E-B19F-E1A138B8CBDCQ38265566-C6FAAABB-0CC9-47CA-81F6-F3C6812A5CE8Q38928613-DA08E2B9-9C49-49EF-827A-130CA80D11F6Q40726200-AC1CC4EC-23DA-42AB-8459-3303E35A0AC9Q44608376-871F439B-88CE-43D9-846F-6347D7DB163DQ52590989-D895DCCC-46A6-4C4C-9949-056CF0C2F06BQ58078023-3BDB4E9F-14ED-40A0-AEE7-7412C33232DEQ77153242-FDE37D0A-C2C4-49FB-9322-0AA890D1D04AQ89697309-3ADE82B9-BFE1-4903-BB32-9E6DA1E2A5E5Q90149662-1C52B371-E749-491C-877C-624AC3B98BB2Q90835381-E7357997-F27A-444A-86EB-530B036B3223Q90985469-F0BFED06-EA9E-45E8-B1BF-7EA7D787CF7DQ91506699-ECD4FFDB-675E-45A5-9CC6-2DC911D65183Q92282231-2A15DFED-F576-424E-8255-77037CCDA807Q92734444-A8975971-AF61-4EB2-B3D7-1F1BC5278E2C
P50
description
biomedical researcher
@en
wetenschapper
@nl
name
Li W
@nl
Wei Li
@en
type
label
Li W
@nl
Wei Li
@en
altLabel
Li W
@en
prefLabel
Li W
@nl
Wei Li
@en
P106
P31
P496
0000-0002-1924-3120