About: Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study

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About: Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study Goto Sponge NotDistinct Permalink

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scientific article published on 01 November 1997

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1997 (uk) im November 1997 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 November 1997 (en) artículu científicu espublizáu en payares de 1997 (ast)
publication date	wds:Q73889955-01412095-054B-40B0-825E-95827B979107
publication date	1997-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73889955-4AFD4C4A-9746-4ADB-8FA2-D8B098A54457
language of work or name	English
cites work	wds:Q73889955-06345823-4B92-4B87-A12D-300FEC45D6B6 wds:Q73889955-250688D5-091A-47B6-A59E-CE95499B165D wds:Q73889955-2BBAC2F8-188A-4C1B-8940-9B5081C3A039 wds:Q73889955-2D4DB59E-CF15-442C-9D4A-C6B85BEC68FA wds:Q73889955-2ED69D40-32BC-47C9-ACA3-408398B1CF83 wds:Q73889955-39117E0B-1244-4640-B672-C1E293ECA8DF wds:Q73889955-6ABAD229-F517-43E7-9893-88BB099C219A wds:Q73889955-79C610D4-F34C-462E-807F-247700B1473D wds:Q73889955-7AB799D2-772F-45B4-90EE-71B6C5C85C7C wds:Q73889955-843F037D-85DF-4B3C-A36D-2518EBCDAA02 wds:Q73889955-8C5BA986-7F08-4C49-8D5A-3FB9FAF19C1E wds:Q73889955-96973828-131E-48DF-B496-A9094B87AEF8 wds:Q73889955-977858F3-13F2-483D-A6B5-E91E5830AD2E wds:Q73889955-9FFF60B4-3E33-47F6-9122-837F22FD5857 wds:Q73889955-AF29D182-A688-428E-B51F-D6FF5FBE6AD1 wds:Q73889955-B48215BD-732B-4AC6-B9ED-7B53764AD626 wds:Q73889955-B52C8A5B-985D-40CF-9B5A-F616B2AAD355 wds:Q73889955-D8BA3D53-53D4-449B-A152-B1E347774DAF wds:Q73889955-E0FF81CC-EBA2-40B7-AD33-8688D9ED36A0 wds:Q73889955-E5A8D5DE-42B7-4816-826D-BE91D05FC200 wds:Q73889955-EDB62C31-FE86-4DC1-B781-D67325C1E4EE wds:Q73889955-EDCAB88C-95CF-4DE1-883B-BA9A515E9F3D wds:Q73889955-F8AE8E27-D5A7-4105-BA5D-CFB07BDD8DEC
cites work	Calculation on fluorescence resonance energy transfer on surfaces The molecular basis of blood coagulation The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor The coagulation cascade: initiation, maintenance, and regulation Involvement of the hydrophobic stack residues 39-44 of factor VIIa in tissue factor interactions Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography The contributions of Ca2+, phospholipids and tissue-factor apoprotein to the activation of human blood-coagulation factor X by activated factor VII. Structural studies on the membrane-bound immunoglobulin E-receptor complex. 1. Characterization of large plasma membrane vesicles from rat basophilic leukemia cells and insertion of amphipathic fluorescent probes Orientation factor in steady-state and time-resolved resonance energy transfer measurements Monoclonal antibody analysis of purified and cell-associated tissue factor. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer Interaction of vitamin K dependent proteins with membranes Surface density determination in membranes by fluorescence energy transfer Phosphatidylethanolamine augments factor VIIa-tissue factor activity: enhancement of sensitivity to phosphatidylserine The crystal structure of the extracellular domain of human tissue factor refined to 1.7 A resolution Structure of the extracellular domain of human tissue factor: location of the factor VIIa binding site Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2Cl The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor. A fluorescence energy transfer study Expression and purification of a soluble tissue factor fusion protein with an epitope for an unusual calcium-dependent antibody Substrate recognition by tissue factor-factor VIIa. Evidence for interaction of residues Lys165 and Lys166 of tissue factor with the 4-carboxyglutamate-rich domain of factor X Molecular mechanism of tissue factor-mediated acceleration of factor VIIa activity Synthesis and characterization of wild-type and variant gamma-carboxyglutamic acid-containing domains of factor VII Spatial relationships between specific sites on reconstituted chloroplast proton adenosine triphosphatase and the phospholipid vesicle surface
author name string	wds:Q73889955-163356B2-8921-4A49-9941-F888431A5D8C wds:Q73889955-B971CA8F-FAD4-4ACD-9D1D-760F7E147FA1 wds:Q73889955-BCFD9DCA-07B6-4C4F-9349-BF6F9C9CF3C4 wds:Q73889955-DEF771B3-0603-49C5-8641-84BADE8044C6
author name string	B Su A E Johnson P F Neuenschwander C D McCallum
rdfs:label	Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (en) Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (nl)
skos:prefLabel	Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (en) Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (nl)
name	Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (en) Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (nl)
author	wds:Q73889955-B637C85C-0E19-49AB-B704-E9C922847203
author	James H Morrissey
title	wds:Q73889955-27F3B284-0D1A-4828-99FE-7C37106255DD
title	Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study (en)
page(s)	wds:Q73889955-23546378-9D9D-45B1-A571-6D875FAA9578
page(s)	30160-30166
instance of	wds:Q73889955-4A2F8B4D-F4C2-48DA-9D30-8AF5958FC63F
instance of	scholarly article
PubMed ID	wds:Q73889955-8683DDC5-D86F-4DB6-AE99-F5A6D3BF40CC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9374497
PubMed ID	9374497
published in	wds:Q73889955-8AF05E03-9DDA-4EDE-BC0D-220656F3DC89
published in	Journal of Biological Chemistry
issue	wds:Q73889955-9BD7B33F-AC6F-447B-AA46-00F2A7E13B25
volume	wds:Q73889955-E8FEE8CE-0976-4673-881C-17C327630466
issue	48
volume	272
DOI	wds:Q73889955-45ADB44E-A7B5-448C-B068-5F46AD0C96EC
DOI	http://dx.doi.org/10.1074/JBC.272.48.30160
DOI	10.1074/JBC.272.48.30160
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73889955
is cites work of	Tissue factor/factor VIIa complex: role of the membrane surface Vitamin K-dependent proteins Tissue factor: a key molecule in hemostatic and nonhemostatic systems Nanoscale studies of protein-membrane interactions in blood clotting. Exactin: A specific inhibitor of Factor X activation by extrinsic tenase complex from the venom of Hemachatus haemachatus. Fusion of the tissue factor extracellular domain to a tumour stroma specific single-chain fragment variable antibody results in an antigen-specific coagulation-promoting molecule FRET studies with factor X mutants provide insight into the topography of the membrane-bound factor X/Xa Accelerating membrane insertion of peripheral proteins with a novel membrane mimetic model. Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution

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