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Recombinant BβArg14His fibrinogen implies participation of N-terminus of Bβ chain in desA fibrin polymerization

Blood, 2003-10, Vol.102 (7), p.2466-2471

2003

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Substitution of the γ-chain Asn308 disturbs the D:D interface affecting fibrin polymerization, fibrinopeptide B release, and FXIIIa-catalyzed cross-linking

Blood, 2004-06, Vol.103 (11), p.4157-4163

2004

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Recombinant Fibrinogen Studies Reveal That Thrombin Specificity Dictates Order of Fibrinopeptide Release

The Journal of biological chemistry, 2000-08, Vol.275 (33), p.25239-25246

2000

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Analysis of Aα251 Fibrinogen: The αC Domain Has a Role in Polymerization, Albeit More Subtle Than Anticipated from the Analogous Proteolytic Fragment X

Biochemistry (Easton), 1998-11, Vol.37 (44), p.15434-15441

1998

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Decreased Lateral Aggregation of a Variant Recombinant Fibrinogen Provides Insight into the Polymerization Mechanism

Biochemistry (Easton), 2000-08, Vol.39 (32), p.9843-9849

2000

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Single-Molecule Force-Clamp Studies of Fibrin'S ‘A-A’ Knob-Hole Interaction

Biophysical journal, 2013-01, Vol.104 (2), p.166a-166a

2013

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

Blood, 2005-12, Vol.106 (12), p.3824-3830

2005

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The Interaction of Integrin αIIbβ3 with Fibrin Occurs through Multiple Binding Sites in the αIIb β-Propeller DomainThis work was supported, in whole or in part, by National Institutes of Health grants HL63199 and HL107539 (to T. P. U.). This work was also supported by American Heart Association Grant 0835257N (to N. P.).▪▪This article contains supplemental Figs. 1S–8S

The Journal of biological chemistry, 2014-01, Vol.289 (4), p.2371-2383

2014

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A functional assay suggests that heterodimers exist in two C-terminal gamma-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV

Thrombosis and haemostasis, 2000-04, Vol.83 (4), p.592-597

2000

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Role of the .alpha.C Domains of Fibrin in Clot Formation

Biochemistry (Easton), 1994-06, Vol.33 (22), p.6986-6997

1994

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Effects of Solution Chemistry on Fibrin Nanomechanics

Biophysical journal, 2010-01, Vol.98 (3), p.595a-595a

2010

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The Role of the αC Domains in the Formation of Nonadhesive Fibrinogen Matrices

Blood, 2011-11, Vol.118 (21), p.1194-1194

2011

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Interactions Mediated by the N-Terminus of Fibrinogen's Bβ Chain

Biochemistry (Easton), 2006-12, Vol.45 (49), p.14843-14852

2006

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Calcium Dependence of Fibrin Nanomechanics: The y1 Calcium Mediates the Unfolding of Fibrinogen Induced by Force Applied to the A—a Bond

Langmuir, 2010, Vol.26 (18), p.14716-14722

2010

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Fibrinogen residue γAla341 Is Necessary for Calcium Binding and ‘A-a’ interaction

Blood, 2010-11, Vol.116 (21), p.1154-1154

2010

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Recombinant Fibrinogen Vlissingen/Frankfurt IV

The Journal of biological chemistry, 2000-06, Vol.275 (23), p.17778-17785

2000

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Characterizing Fibrin ‘A-a’ Interactions By Single Molecule Force Spectroscopy

Biophysical journal, 2009-02, Vol.96 (3), p.217a-217a

2009

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Carboxyl-terminal portions of the α chains of fibrinogen and fibrin : localization by electron microscopy and the effects of isolated αC fragments on polymerization

The Journal of biological chemistry, 1993-06, Vol.268 (18), p.13577-13585

1993

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Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the alphaC-domain of human fibrinogen

Microbiology (Society for General Microbiology), 2008-02, Vol.154 (Pt 2), p.550

2008

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

Biochemistry (Easton), 2007-08, Vol.46 (31), p.9133-9142

2007

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Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization

Biochemistry (Easton), 2004-03, Vol.43 (9), p.2475-2483

2004

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Loss of Clotting Function in Mice Expressing a Mutant Form of Fibrinogen Lacking the α Chain Thrombin Cleavage Site

Blood, 2008-11, Vol.112 (11), p.394-394

2008

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Polymerization-defective fibrinogen variant gammaD364A binds knob "A" peptide mimic

Biochemistry (Easton), 2008-08, Vol.47 (33), p.8607-8613

2008

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Interactions mediated by the N-terminus of fibrinogen's Bbeta chain

Biochemistry (Easton), 2006-12, Vol.45 (49), p.14843-14852

2006

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Role of the alpha C domains of fibrin in clot formation

Biochemistry (Easton), 1994-06, Vol.33 (22), p.6986-6997

1994

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Recombinant BβArg14His fibrinogen implies participation of N-terminus of Bβ chain in desA fibrin polymerization

Substitution of the γ-chain Asn308 disturbs the D:D interface affecting fibrin polymerization, fibrinopeptide B release, and FXIIIa-catalyzed cross-linking

Recombinant Fibrinogen Studies Reveal That Thrombin Specificity Dictates Order of Fibrinopeptide Release

Analysis of Aα251 Fibrinogen: The αC Domain Has a Role in Polymerization, Albeit More Subtle Than Anticipated from the Analogous Proteolytic Fragment X

Decreased Lateral Aggregation of a Variant Recombinant Fibrinogen Provides Insight into the Polymerization Mechanism

Single-Molecule Force-Clamp Studies of Fibrin'S ‘A-A’ Knob-Hole Interaction

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

A functional assay suggests that heterodimers exist in two C-terminal gamma-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV

Role of the .alpha.C Domains of Fibrin in Clot Formation

Effects of Solution Chemistry on Fibrin Nanomechanics

The Role of the αC Domains in the Formation of Nonadhesive Fibrinogen Matrices

Interactions Mediated by the N-Terminus of Fibrinogen's Bβ Chain

Calcium Dependence of Fibrin Nanomechanics: The y1 Calcium Mediates the Unfolding of Fibrinogen Induced by Force Applied to the A—a Bond

Fibrinogen residue γAla341 Is Necessary for Calcium Binding and ‘A-a’ interaction

Recombinant Fibrinogen Vlissingen/Frankfurt IV

Characterizing Fibrin ‘A-a’ Interactions By Single Molecule Force Spectroscopy

Carboxyl-terminal portions of the α chains of fibrinogen and fibrin : localization by electron microscopy and the effects of isolated αC fragments on polymerization

Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the alphaC-domain of human fibrinogen

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

Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization

Loss of Clotting Function in Mice Expressing a Mutant Form of Fibrinogen Lacking the α Chain Thrombin Cleavage Site

Polymerization-defective fibrinogen variant gammaD364A binds knob "A" peptide mimic

Interactions mediated by the N-terminus of fibrinogen's Bbeta chain

Role of the alpha C domains of fibrin in clot formation

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