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Journal Articles

Factor XIIIa-dependent retention of red blood cells in clots is mediated by fibrin α-chain crosslinking

James R. Byrnes, Cédric Duval, Yiming Wang, Caroline E. Hansen, Byungwook Ahn, Micah J. Mooberry, Martha A. Clark, Jill M. Johnsen, Susan T. Lord, Wilbur A. Lam, Joost C. M. Meijers, Heyu Ni, Robert A. S. Ariëns, Alisa S. Wolberg

Blood (2015) 126 (16): 1940–1948.

https://doi.org/10.1182/blood-2015-06-652263

Published: 2015

Includes: Multimedia, Supplemental data

Journal Articles

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

Ivan S Yermolenko, MS, Fuhrmann Alexander, PhD, Oleg V Gorkun, PhD, Valeryi K Lishko, PhD, Susan T Lord, PhD, Robert Ros, PhD, Tatiana P Ugarova, PhD

Blood (2011) 118 (21): 1194.

https://doi.org/10.1182/blood.V118.21.1194.1194

Published: 2011

Journal Articles

Coming full circle with factor XIII

Susan T. Lord

Blood (2011) 117 (12): 3255–3256.

https://doi.org/10.1182/blood-2011-02-332627

Published: 2011

Journal Articles

Increased thrombosis susceptibility and altered fibrin formation in STAT5-deficient mice

Sarah M. Nordstrom, Brian A. Holliday, Brandon C. Sos, James W. Smyth, Robert E. Levy, Jonathan W. Dukes, Susan T. Lord, Ethan J. Weiss

Blood (2010) 116 (25): 5724–5733.

https://doi.org/10.1182/blood-2010-06-292227

Published: 2010

Includes: Multimedia, Supplemental data

Journal Articles

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

Rojin Park, MD, Lifang Ping, Jaewoo Song, MD, Sung-Yu Hong, PhD, Jong-Rak Choi, MD, Oleg V Gorkun, PhD, Susan T Lord, PhD

Blood (2010) 116 (21): 1154.

https://doi.org/10.1182/blood.V116.21.1154.1154

Published: 2010

Journal Articles

From Fibrinogen to Fibrin: Dynamic Light Scattering to Probe the Mechanism of Protofibril Assembly Into Fibers.

Lihong Huang, Susan T Lord, PhD

Blood (2010) 116 (21): 1156.

https://doi.org/10.1182/blood.V116.21.1156.1156

Published: 2010

Journal Articles

Fibrinogen variant BβD432A has normal polymerization but does not bind knob “B”

Sheryl R. Bowley, Susan T. Lord

Blood (2009) 113 (18): 4425–4430.

https://doi.org/10.1182/blood-2008-09-178178

Published: 2009

Includes: Supplemental data

Journal Articles

High Throughput Screening of Fibrin Clots: Transport and Mechanics Measured by Microbeads

Richard Chasen Spero, Rachel Sircar, Susan T. Lord, Ph.D., Alisa S. Wolberg, PhD, Richard Superfine, Ph.D.

Blood (2008) 112 (11): 4095.

https://doi.org/10.1182/blood.V112.11.4095.4095

Published: 2008

Journal Articles

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

Matthew Flick, PhD, Joni M. Ullman, Joseph S. Palumbo, MD, Eric S. Mullins, MD, Keith W Kombrink, Kathryn E. Talmage, Maureen A. Shaw, Susan T. Lord, Ph.D., Jay Degen, Oleg V Gorkun

Blood (2008) 112 (11): 394.

https://doi.org/10.1182/blood.V112.11.394.394

Published: 2008

Journal Articles

Functional analysis of fibrin γ-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness

Kristina F. Standeven, Angela M. Carter, Peter J. Grant, John W. Weisel, Irina Chernysh, Leona Masova, Susan T. Lord, Robert A. S. Ariëns

Blood (2007) 110 (3): 902–907.

https://doi.org/10.1182/blood-2007-01-066837

Published: 2007

Journal Articles

An Investigation of Factor XIII Binding to Recombinant γ′/γ′ and γ/γ′ Fibrinogen.

Kathryn C. Gersh, PhD, Susan T. Lord, PhD

Blood (2006) 108 (11): 1705.

https://doi.org/10.1182/blood.V108.11.1705.1705

Published: 2006

Journal Articles

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

Jean-Philippe Collet, Jennifer L. Moen, Yuri I. Veklich, Oleg V. Gorkun, Susan T. Lord, Gilles Montalescot, John W. Weisel

Blood (2005) 106 (12): 3824–3830.

https://doi.org/10.1182/blood-2005-05-2150

Published: 2005

Journal Articles

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

Nobuo Okumura, Oleg V. Gorkun, Fumiko Terasawa, Susan T. Lord

Blood (2004) 103 (11): 4157–4163.

https://doi.org/10.1182/blood-2003-12-4296

Published: 2004

Journal Articles

Severe hypodysfibrinogenemia in compound heterozygotes of the fibrinogen AαIVS4 + 1G>T mutation and an AαGln328 truncation (fibrinogen Keokuk)

Phil Lefebvre, Pauline T. Velasco, Amy Dear, Karim C. Lounes, Susan T. Lord, Stephen O. Brennan, David Green, Laszlo Lorand

Blood (2004) 103 (7): 2571–2576.

https://doi.org/10.1182/blood-2003-07-2316

Published: 2004

Journal Articles

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

Jennifer L. Moen, Oleg V. Gorkun, John W. Weisel, Susan T. Lord

Blood (2003) 102 (7): 2466–2471.

https://doi.org/10.1182/blood-2003-01-0204

Published: 2003

Journal Articles

Analysis of fibrinogen γ-chain truncations shows the C-terminus, particularly γIle387, is essential for assembly and secretion of this multichain protein

Nobuo Okumura, Fumiko Terasawa, Hitoshi Tanaka, Masako Hirota, Hiroyoshi Ota, Kiyoshi Kitano, Kendo Kiyosawa, Susan T. Lord

Blood (2002) 99 (10): 3654–3660.

https://doi.org/10.1182/blood.V99.10.3654

Published: 2002

Journal Articles

The impaired polymerization of fibrinogen Longmont (Bβ166Arg→Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers

Karim C. Lounes, Jerry B. Lefkowitz, Agnes H. Henschen-Edman, Andrew I. Coates, Roy R. Hantgan, Susan T. Lord

Blood (2001) 98 (3): 661–666.

https://doi.org/10.1182/blood.V98.3.661

Published: 2001

Journal Articles

Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aα R16C and γ G165R

Bettina Bolliger-Stucki, Susan T. Lord, Miha Furlan

Blood (2001) 98 (2): 351–357.

https://doi.org/10.1182/blood.V98.2.351

Published: 2001

Journal Articles

Hypofibrinogenemia Associated With a Heterozygous Missense Mutation γ153Cys to Arg (Matsumoto IV): In Vitro Expression Demonstrates Defective Secretion of the Variant Fibrinogen

Fumiko Terasawa, Nobuo Okumura, Kiyoshi Kitano, Nobuaki Hayashida, Makoto Shimosaka, Mitsuo Okazaki, Susan T. Lord

Blood (1999) 94 (12): 4122–4131.

https://doi.org/10.1182/blood.V94.12.4122

Published: 1999

Journal Articles

γ-Chain Dysfibrinogenemias: Molecular Structure-Function Relationships of Naturally Occurring Mutations in the γ Chain of Human Fibrinogen

Hélène C.F. Côté, Susan T. Lord, Kathleen P. Pratt

Blood (1998) 92 (7): 2195–2212.

https://doi.org/10.1182/blood.V92.7.2195

Published: 1998

NARROW

Factor XIIIa-dependent retention of red blood cells in clots is mediated by fibrin α-chain crosslinking

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

Coming full circle with factor XIII

Increased thrombosis susceptibility and altered fibrin formation in STAT5-deficient mice

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

From Fibrinogen to Fibrin: Dynamic Light Scattering to Probe the Mechanism of Protofibril Assembly Into Fibers.

Fibrinogen variant BβD432A has normal polymerization but does not bind knob “B”

High Throughput Screening of Fibrin Clots: Transport and Mechanics Measured by Microbeads

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

Functional analysis of fibrin γ-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness

An Investigation of Factor XIII Binding to Recombinant γ′/γ′ and γ/γ′ Fibrinogen.

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

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

Severe hypodysfibrinogenemia in compound heterozygotes of the fibrinogen AαIVS4 + 1G>T mutation and an AαGln328 truncation (fibrinogen Keokuk)

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

Analysis of fibrinogen γ-chain truncations shows the C-terminus, particularly γIle387, is essential for assembly and secretion of this multichain protein

The impaired polymerization of fibrinogen Longmont (Bβ166Arg→Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers

Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aα R16C and γ G165R

Hypofibrinogenemia Associated With a Heterozygous Missense Mutation γ153Cys to Arg (Matsumoto IV): In Vitro Expression Demonstrates Defective Secretion of the Variant Fibrinogen

γ-Chain Dysfibrinogenemias: Molecular Structure-Function Relationships of Naturally Occurring Mutations in the γ Chain of Human Fibrinogen

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American Society of Hematology

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American Society of Hematology

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