Complexity of “A−a” Knob−Hole Fibrin Interaction Revealed by Atomic Force Spectroscopy-Reference-Cited by-同舟云学术

Complexity of “A−a” Knob−Hole Fibrin Interaction Revealed by Atomic Force Spectroscopy

Published:2008-03-20 Issue:9 Volume:24 Page:4979-4988
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Averett Laurel E.¹,Geer Carri B.¹,Fuierer Ryan R.¹,Akhremitchev Boris B.¹,Gorkun Oleg V.¹,Schoenfisch Mark H.¹

Affiliation:

1. Department of Physics and Astronomy, Department of Chemistry, and Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, North Carolina 27599, and Department of Chemistry, Duke University, Durham, North Carolina 27708

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la703264x

Reference43 articles.

1. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides

2. Interaction of the fibrinogen-binding tetrapeptide gly-pro-arg-pro with fine clots and oligomers of ?-fibrin; comparison with ??-fibrin

3. "Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules.

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