Literature DB >> 6224704

Structural organization of C-terminal parts of fibrinogen A alpha-chains.

L V Medved, O V Gorkun, P L Privalov.   

Abstract

Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the A alpha-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.

Entities:  

Mesh：

Substances：

Year:  1983        PMID： 6224704     DOI： 10.1016/0014-5793(83)80985-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  26 in total

1.  Polymerization of rod-like macromolecular monomers studied by stopped-flow, multiangle light scattering: set-up, data processing, and application to fibrin formation.

Authors:  S Bernocco; F Ferri; A Profumo; C Cuniberti; M Rocco
Journal:  Biophys J       Date:  2000-07       Impact factor: 4.033

2.  Transglutaminase-catalyzed crosslinking of the Aalpha and gamma constituent chains in fibrinogen.

Authors:  S N Murthy; J H Wilson; T J Lukas; Y Veklich; J W Weisel; L Lorand
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-04       Impact factor: 11.205

3.  The crystal structure of modified bovine fibrinogen.

Authors:  J H Brown; N Volkmann; G Jun; A H Henschen-Edman; C Cohen
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-04       Impact factor: 11.205

4.  Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers.

Authors:  Lifang Ping; Lihong Huang; Barbara Cardinali; Aldo Profumo; Oleg V Gorkun; Susan T Lord
Journal:  Biochemistry       Date:  2011-09-27       Impact factor: 3.162

5.  Oxidation-induced destabilization of the fibrinogen αC-domain dimer investigated by molecular dynamics simulations.

Authors:  Eric N Pederson; Gianluca Interlandi
Journal:  Proteins       Date:  2019-06-14

6.  The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis.

Authors:  Jean-Philippe Collet; Jennifer L Moen; Yuri I Veklich; Oleg V Gorkun; Susan T Lord; Gilles Montalescot; John W Weisel
Journal:  Blood       Date:  2005-08-09       Impact factor: 22.113

7.  Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR.

Authors:  Robert A Burton; Galina Tsurupa; Leonid Medved; Nico Tjandra
Journal:  Biochemistry       Date:  2006-02-21       Impact factor: 3.162

8.  NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment.

Authors:  Robert A Burton; Galina Tsurupa; Roy R Hantgan; Nico Tjandra; Leonid Medved
Journal:  Biochemistry       Date:  2007-06-23       Impact factor: 3.162

9.  Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.

Authors:  Rustem I Litvinov; Sergiy Yakovlev; Galina Tsurupa; Oleg V Gorkun; Leonid Medved; John W Weisel
Journal:  Biochemistry       Date:  2007-07-13       Impact factor: 3.162

10.  Interaction of the fibronectin COOH-terminal Fib-2 regions with fibrin: further characterization and localization of the Fib-2-binding sites.

Authors:  Evgeny Makogonenko; Kenneth C Ingham; Leonid Medved
Journal:  Biochemistry       Date:  2007-04-11       Impact factor: 3.162
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.