(Q33581285)

English

Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

Sriram Krishnaswamy

3

object named as

Sriram Krishnaswamy

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

author name string

Harlan N Bradford

1

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

Joseph A Micucci

2

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

language of work or name

0 references

publication date

26 October 2009

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

285

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

328-338

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

describes a project that uses

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2804180/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

Factor Xa active site substrate specificity with substrate phage display and computational molecular modeling.

1 reference

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14 July 2018

Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase

1 reference

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Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages

1 reference

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14 July 2018

Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase

1 reference

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Exosite-driven substrate specificity and function in coagulation

1 reference

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Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin

1 reference

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Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized

1 reference

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Thrombin formation

1 reference

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Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site

1 reference

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Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase

1 reference

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Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide

1 reference

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Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

1 reference

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New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK

1 reference

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Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

1 reference

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Structure of human des(1-45) factor Xa at 2.2 A resolution

1 reference

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The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin

1 reference

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p-Aminobenzamidine as a fluorescent probe for the active site of serine proteases.

1 reference

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On the size of the active site in proteases. I. Papain

1 reference

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14 July 2018

Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism

1 reference

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14 July 2018

The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction

1 reference

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Cofactor proteins in the assembly and expression of blood clotting enzyme complexes

1 reference

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14 July 2018

Studies of the role of factor Va in the factor Xa-catalyzed activation of prothrombin, fragment 1.2-prethrombin-2, and dansyl-L-glutamyl-glycyl-L-arginine-meizothrombin in the absence of phospholipid.

1 reference

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14 July 2018

Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation

1 reference

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Surface-dependent reactions of the vitamin K-dependent enzyme complexes

1 reference

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Activation of human factor X (Stuart factor) by a protease from Russell's viper venom

1 reference

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Interactions of a fluorescent active-site-directed inhibitor of thrombin: dansylarginine N-(3-ethyl-1,5-pentanediyl)amide

1 reference

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Active site-independent recognition of substrates and product by bovine prothrombinase: a fluorescence resonance energy transfer study

1 reference

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Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.070334

21 January 2018

Mapping of the catalytic groove preferences of factor Xa reveals an inadequate selectivity for its macromolecule substrates.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.070334

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Gly319 --> arg substitution in the dysfunctional prothrombin Segovia

1 reference

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A control switch for prothrombinase: characterization of a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain that regulates the rate and pathway for prothrombin activation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.070334

21 January 2018

Role of the activation peptide domain in human factor X activation by the extrinsic Xase complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

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based on heuristic

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Purification and characterization of a variant of human prothrombin: prothrombin Segovia

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Role of Hirudin-like factor Va heavy chain sequences in prothrombinase function

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proposed structural models of human factor Va and prothrombinase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Exosite binding tethers the macromolecular substrate to the prothrombinase complex and directs cleavage at two spatially distinct sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

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based on heuristic

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A logarithmic approximation to initial rates of enzyme reactions

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

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Solution composition dependent variation in extinction coefficients for p-nitroaniline

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

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Analysis for gamma-carboxyglutamic acid

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

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The action of factor Xa on peptide p-nitroanilide substrates: substrate selectivity and examination of hydrolysis with different reaction conditions

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

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based on heuristic

inferred from PubMed ID database lookup

Meizothrombin, a major product of factor Xa-catalyzed prothrombin activation

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

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based on heuristic

inferred from PubMed ID database lookup

The activation of prothrombin by the prothrombinase complex. The contribution of the substrate-membrane interaction to catalysis

1 reference

https://pubmed.ncbi.nlm.nih.gov/19858193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M109.070334

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 July 2017

ResearchGate publication ID

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