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Literature DB >> 16288455

Natively unfolded regions of the vertebrate fibrinogen molecule.

Abstract

Although it has long been realized that a large portion of the fibrinogen alpha chain has little if any defined structure, the physiological significance of this flexible appendage remains mysterious. 2005 Wiley-Liss, Inc.

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Year: 2006 PMID： 16288455 DOI： 10.1002/prot.20758

Source DB: PubMed Journal: Proteins ISSN： 0887-3585

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Cited

15 in total

1. Mechanism of fibrin(ogen) forced unfolding.

Authors: Artem Zhmurov; Andre E X Brown; Rustem I Litvinov; Ruxandra I Dima; John W Weisel; Valeri Barsegov
Journal: Structure Date: 2011-11-09 Impact factor: 5.006

2. Structural hierarchy governs fibrin gel mechanics.

Authors: Izabela K Piechocka; Rommel G Bacabac; Max Potters; Fred C Mackintosh; Gijsje H Koenderink
Journal: Biophys J Date: 2010-05-19 Impact factor: 4.033

Review 3. A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers.

Authors: M Guthold; W Liu; E A Sparks; L M Jawerth; L Peng; M Falvo; R Superfine; R R Hantgan; S T Lord
Journal: Cell Biochem Biophys Date: 2007-10-02 Impact factor: 2.194

4. 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

5. 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

6. 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

Natively unfolded regions of the vertebrate fibrinogen molecule.

1. Mechanism of fibrin(ogen) forced unfolding.

2. Structural hierarchy governs fibrin gel mechanics.

Review 3. A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers.

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

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

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

Review 7. The molecular origins of the mechanical properties of fibrin.

8. Length of tandem repeats in fibrin's alphaC region correlates with fiber extensibility.

9. Structure, stability, and interaction of the fibrin(ogen) alphaC-domains.

10. Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry.