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Submillisecond Elastic Recoil Reveals Molecular Origins of Fibrin Fiber Mechanics

Biophysical journal, 2013-06, Vol.104 (12), p.2671-2680

2013

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The molecular origins of the mechanical properties of fibrin

Biophysical chemistry, 2010-11, Vol.152 (1), p.15-20

2010

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Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions

Blood, 2007-01, Vol.109 (1), p.130-138

2007

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Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense

Blood, 2015-10, Vol.126 (17), p.2047-2058

2015

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Calcium Dependence of Fibrin Nanomechanics: The γ1 Calcium Mediates the Unfolding of Fibrinogen Induced by Force Applied to the “A−a” Bond

Langmuir, 2010-09, Vol.26 (18), p.14716-14722

2010

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The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain

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

2014

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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

Biochemistry (Easton), 2011-10, Vol.50 (42), p.9066-9075

2011

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Direct Evidence for Specific Interactions of the Fibrinogen αC-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 β2, 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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Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level

Blood, 2005-11, Vol.106 (9), p.2944-2951

2005

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The Assembly of Nonadhesive Fibrinogen Matrices Depends on the αC Regions of the Fibrinogen Molecule

The Journal of biological chemistry, 2012-12, Vol.287 (50), p.41979-41990

2012

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

Langmuir, 2008-05, Vol.24 (9), p.4979-4988

2008

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An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links

Thrombosis and haemostasis, 2013-02, Vol.109 (2), p.199

2013

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Kinetics of the Multistep Rupture of Fibrin ‘A-a’ Polymerization Interactions Measured Using Atomic Force Microscopy

Biophysical journal, 2009-11, Vol.97 (10), p.2820-2828

2009

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Fibrinogen residue γAla341 is necessary for calcium binding and 'A-a' interactions

Thrombosis and haemostasis, 2012-05, Vol.107 (5), p.875

2012

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Interactions of Thrombin with Fibrinogen Adsorbed on Methyl-, Hydroxyl-, Amine-, and Carboxyl-Terminated Self-Assembled Monolayers

Biochemistry (Easton), 2005-11, Vol.44 (47), p.15561-15568

2005

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2.8 Å Crystal Structures of Recombinant Fibrinogen Fragment D with and without Two Peptide Ligands: GHRP Binding to the “b” Site Disrupts Its Nearby Calcium-binding Site

Biochemistry (Easton), 2002-10, Vol.41 (40), p.12124-12132

2002

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A Cluster of Basic Amino Acid Residues in the γ370−381 Sequence of Fibrinogen Comprises a Binding Site for Platelet Integrin αIIbβ3 (Glycoprotein IIb/IIIa)

Biochemistry (Easton), 2005-12, Vol.44 (51), p.16920-16930

2005

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Polymerization-Defective Fibrinogen Variant γD364A Binds Knob “A” Peptide Mimic

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

2008

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Probing the γ2 Calcium-Binding Site: Studies with γD298,301A Fibrinogen Reveal Changes in the γ294-301 Loop that Alter the Integrity of the “a” Polymerization Site

Biochemistry (Easton), 2007-05, Vol.46 (17), p.5114-5123

2007

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BβGlu397 and BβAsp398 but Not BβAsp432 Are Required for “B:b” Interactions

Biochemistry (Easton), 2004-03, Vol.43 (9), p.2465-2474

2004

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The Conversion of Fibrinogen to Fibrin: Recombinant Fibrinogen Typifies Plasma Fibrinogen

Blood, 1997-06, Vol.89 (12), p.4407-4414

1997

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Analysis of Engineered Fibrinogen Variants Suggests That an Additional Site Mediates Platelet Aggregation and That “B−b” Interactions Have a Role in Protofibril Formation

Biochemistry (Easton), 2002-04, Vol.41 (16), p.5291-5299

2002

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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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Submillisecond Elastic Recoil Reveals Molecular Origins of Fibrin Fiber Mechanics

The molecular origins of the mechanical properties of fibrin

Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions

Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense

Calcium Dependence of Fibrin Nanomechanics: The γ1 Calcium Mediates the Unfolding of Fibrinogen Induced by Force Applied to the “A−a” Bond

The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain

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

Direct Evidence for Specific Interactions of the Fibrinogen αC-Domains with the Central E Region and with Each Other

Calcium-Binding Site β2, Adjacent to the “b” Polymerization Site, Modulates Lateral Aggregation of Protofibrils during Fibrin Polymerization

Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level

The Assembly of Nonadhesive Fibrinogen Matrices Depends on the αC Regions of the Fibrinogen Molecule

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

An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links

Kinetics of the Multistep Rupture of Fibrin ‘A-a’ Polymerization Interactions Measured Using Atomic Force Microscopy

Fibrinogen residue γAla341 is necessary for calcium binding and 'A-a' interactions

Interactions of Thrombin with Fibrinogen Adsorbed on Methyl-, Hydroxyl-, Amine-, and Carboxyl-Terminated Self-Assembled Monolayers

2.8 Å Crystal Structures of Recombinant Fibrinogen Fragment D with and without Two Peptide Ligands: GHRP Binding to the “b” Site Disrupts Its Nearby Calcium-binding Site

A Cluster of Basic Amino Acid Residues in the γ370−381 Sequence of Fibrinogen Comprises a Binding Site for Platelet Integrin αIIbβ3 (Glycoprotein IIb/IIIa)

Polymerization-Defective Fibrinogen Variant γD364A Binds Knob “A” Peptide Mimic

Probing the γ2 Calcium-Binding Site: Studies with γD298,301A Fibrinogen Reveal Changes in the γ294-301 Loop that Alter the Integrity of the “a” Polymerization Site

BβGlu397 and BβAsp398 but Not BβAsp432 Are Required for “B:b” Interactions

The Conversion of Fibrinogen to Fibrin: Recombinant Fibrinogen Typifies Plasma Fibrinogen

Analysis of Engineered Fibrinogen Variants Suggests That an Additional Site Mediates Platelet Aggregation and That “B−b” Interactions Have a Role in Protofibril Formation

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

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