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Details on Person Thrombin-mediated proteolytic cleavage in the central E doma...

Class:Id	Summation:140843
_displayName	Thrombin-mediated proteolytic cleavage in the central E doma...
_timestamp	2025-01-12 02:04:45
created	[InstanceEdit:140579] D'Eustachio, P, 2004-08-24 14:00:00
literatureReference	[LiteratureReference:140844] Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. [LiteratureReference:140588] Fibrinogen and fibrin [LiteratureReference:9929096] Structural basis for sequential cleavage of fibrinopeptides upon fibrin assembly [LiteratureReference:140861] High-resolution NMR studies of fibrinogen-like peptides in solution: interaction of thrombin with residues 1-23 of the A alpha chain of human fibrinogen [LiteratureReference:9929114] Fibrinopeptides A and B release in the process of surface fibrin formation [LiteratureReference:9929157] Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level [LiteratureReference:9929147] Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions [LiteratureReference:9929159] Crystal structure of fragment double-D from human fibrin with two different bound ligands [LiteratureReference:9929154] Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide [LiteratureReference:9929158] Structural basis of the fibrinogen-fibrin transformation: contributions from X-ray crystallography [LiteratureReference:9929149] Fibrin protofibril packing and clot stability are enhanced by extended knob-hole interactions and catch-slip bonds [LiteratureReference:9929127] Why fibrin biomechanical properties matter for hemostasis and thrombosis [LiteratureReference:9929146] Regulatory element in fibrin triggers tension-activated transition from catch to slip bonds [LiteratureReference:9935033] Structural Basis of Interfacial Flexibility in Fibrin Oligomers [LiteratureReference:9935028] Does topology drive fiber polymerization? [LiteratureReference:9935042] Correlation between Fibrin Fibrillation Kinetics and the Resulting Fibrin Network Microstructure [LiteratureReference:9929173] Fibrinogen and Fibrin [LiteratureReference:9935044] Comprehensive Analysis of the Role of Fibrinogen and Thrombin in Clot Formation and Structure for Plasma and Purified Fibrinogen [LiteratureReference:9935045] Atomic Structural Models of Fibrin Oligomers
modified	[InstanceEdit:9929142] Shamovsky, Veronica, 2024-11-20 [InstanceEdit:9935040] Shamovsky, Veronica, 2025-01-12
text	Thrombin-mediated proteolytic cleavage in the central E domain of fibrinogen results in the release of fibrinopeptides A and B from the N-terminal regions of the α and β chains of fibrinogen, respectively, leading to the formation of a soluble fibrin monomer (Ni et al. 1989; Pechik I et al., 2006; Riedel T et al., 2011). The cleavage unmasks four binding sites in the E domain of monomeric fibrin allowing binding to the C-terminal region of the D domain from other fibrin monomers (Everse SJ et al., 1998, 1999; Doolittle RF 2003; Litvinov RI et al., 2005, 2007). Fibrin monomers rapidly and spontaneously associate into large multimers, which elongate into protofibrils that later aggregate to form fibers, creating a three-dimensional network (Laudano AP and Doolittelle RF 1980; Huang L et al., 2014; Zhmurov A et al., 2016; Litvinov RI et al., 2018; Asquith NL et al., 2022; Pietsch K et al. 2023; reviewed by Litvinov RI et al., 2021). The structural organization is essential for the mechanical properties of the clot (Litvinov RI & Weisel JW 2017; Risman RA et al., 2024; reviewed by Feller T et al., 2022). The process of multimerization, and the range of multimer structures that can form in vivo and in vitro, have been studied in detail (Doolittle RF 1984, 2003; Huang L et al., 2014; Zhmurov A et al., 2018; Litvinov RI & Weisel JW 2017; Risman RA et al., 2024). Here, multimer size has arbitrarily been set to three fibrin monomers.
(summation)	[Reaction:140842] n fibrin monomers -> fibrin multimer [Homo sapiens]
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