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Switching cation-binding loops paves the way for redesigning allosteric activation

Proceedings of the National Academy of Sciences - PNAS, 2011-03, Vol.108 (13), p.5145-5146

Maurer, Muriel C.

2011

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Mapping residues within the factor XIII-A∗ activation peptide cleft that interact with glutamine containing substrates

Biophysical journal, 2023-02, Vol.122 (3), p.479a-479a

2023

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Fbg αC 389–402 Enhances Factor XIII Cross-Linking in the Fibrinogen αC Region Via Electrostatic and Hydrophobic Interactions

Biochemistry (Easton), 2023-07, Vol.62 (14), p.2170-2181

2023

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Identification of Factor XIII β-Sandwich Residues Mediating Glutamine Substrate Binding and Activation Peptide Cleavage

Thrombosis and haemostasis, 2024-05, Vol.124 (5), p.408

2024

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Factor XIII activation and substrate crosslinking can be influenced by amino acid substitutions from transglutaminase-2

Biophysical journal, 2023-02, Vol.122 (3), p.481a-481a

2023

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Thrombin Exosite Maturation and Ligand Binding at ABE II Help Stabilize PAR-Binding Competent Conformation at ABE I

Biochemistry (Easton), 2019-02, Vol.58 (8), p.1048-1060

2019

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Activation of factor XIII is accompanied by a change in oligomerization state

The FEBS journal, 2017-11, Vol.284 (22), p.3849-3861

2017

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Deciphering Conformational Changes Associated with the Maturation of Thrombin Anion Binding Exosite I

Biochemistry (Easton), 2017-12, Vol.56 (48), p.6343-6354

2017

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Transglutaminase Activities of Blood Coagulant Factor XIII Are Dependent on the Activation Pathways and on the Substrates

Thrombosis and haemostasis, 2023-04, Vol.123 (4), p.380

2023

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Ligand Binding to Anion-binding Exosites Regulates Conformational Properties of Thrombin

The Journal of biological chemistry, 2013-03, Vol.288 (12), p.8667-8678

2013

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Proline 36 of the Factor XIII Activation Peptide Plays a Crucial Role in Substrate Recognition and Zymogen Activation

Thrombosis and haemostasis, 2018-12, Vol.118 (12), p.2037

2018

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Proteolytic and nonproteolytic activation mechanisms result in conformationally and functionally different forms of coagulation factor XIII A

The FEBS journal, 2020-02, Vol.287 (3), p.452-464

2020

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Liberating R169 promotes anticoagulant protein C

Blood, 2012-07, Vol.120 (3), p.501-502

Maurer, Muriel C.

2012

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Evaluating the Effects of Fibrinogen αC Mutations on the Ability of Factor XIII to Crosslink the Reactive αC Glutamines (Q237, Q328, Q366)

Thrombosis and haemostasis, 2019-07, Vol.119 (7), p.1048

2019

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Ranking reactive glutamines in the fibrinogen αC region that are targeted by blood coagulant factor XIII

Blood, 2016-05, Vol.127 (18), p.2241-2248

2016

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Biophysical Investigation of GpIbα Binding to Thrombin Anion Binding Exosite II

Biochemistry (Easton), 2009-08, Vol.48 (30), p.7110-7122

2009

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Evaluating factor XIII specificity for glutamine-containing substrates using a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay

Analytical biochemistry, 2014-07, Vol.457, p.74-84

2014

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Role of calcium in the conformational dynamics of factor XIII activation examined by hydrogen–deuterium exchange coupled with MALDI-TOF MS

Archives of biochemistry and biophysics, 2011-08, Vol.512 (1), p.87-95

2011

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Screening cleavage of Factor XIII V34X Activation Peptides by thrombin mutants: A strategy for controlling fibrin architecture

Biochimica et biophysica acta. Proteins and proteomics, 2017-10, Vol.1865 (10), p.1246-1254

2017

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V34I and V34A substitutions within the factor XIII activation peptide segment (28-41) affect interactions with the thrombin active site

Thrombosis and haemostasis, 2003-04, Vol.89 (4), p.647

2003

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Factor XIII crosslinking in fibrinogen αc(233-425) is assisted by electrostatic and hydrophobic residues in αc(389-403)

Biophysical journal, 2022-02, Vol.121 (3), p.348a-348a

2022

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Conformational Analysis of γ‘ Peptide (410−427) Interactions with Thrombin Anion Binding Exosite II

Biochemistry (Easton), 2006-06, Vol.45 (24), p.7434-7445

2006

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Employing Mutants to Study Thrombin Residues Responsible for Factor XIII Activation Peptide Recognition: A Kinetic Study

Biochemistry (Easton), 2007-03, Vol.46 (9), p.2444-2452

2007

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Characterizing the specificity of activated Factor XIII for glutamine-containing substrate peptides

Biochimica et biophysica acta, 2006-07, Vol.1764 (7), p.1207-1217

2006

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Perturbations in Factor XIII Resulting from Activation and Inhibition Examined by Solution Based Methods and Detected by MALDI-TOF MS

Biochemistry (Easton), 2007-09, Vol.46 (35), p.10089-10101

2007

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Switching cation-binding loops paves the way for redesigning allosteric activation

Mapping residues within the factor XIII-A∗ activation peptide cleft that interact with glutamine containing substrates

Fbg αC 389–402 Enhances Factor XIII Cross-Linking in the Fibrinogen αC Region Via Electrostatic and Hydrophobic Interactions

Identification of Factor XIII β-Sandwich Residues Mediating Glutamine Substrate Binding and Activation Peptide Cleavage

Factor XIII activation and substrate crosslinking can be influenced by amino acid substitutions from transglutaminase-2

Thrombin Exosite Maturation and Ligand Binding at ABE II Help Stabilize PAR-Binding Competent Conformation at ABE I

Activation of factor XIII is accompanied by a change in oligomerization state

Deciphering Conformational Changes Associated with the Maturation of Thrombin Anion Binding Exosite I

Transglutaminase Activities of Blood Coagulant Factor XIII Are Dependent on the Activation Pathways and on the Substrates

Ligand Binding to Anion-binding Exosites Regulates Conformational Properties of Thrombin

Proline 36 of the Factor XIII Activation Peptide Plays a Crucial Role in Substrate Recognition and Zymogen Activation

Proteolytic and nonproteolytic activation mechanisms result in conformationally and functionally different forms of coagulation factor XIII A

Liberating R169 promotes anticoagulant protein C

Evaluating the Effects of Fibrinogen αC Mutations on the Ability of Factor XIII to Crosslink the Reactive αC Glutamines (Q237, Q328, Q366)

Ranking reactive glutamines in the fibrinogen αC region that are targeted by blood coagulant factor XIII

Biophysical Investigation of GpIbα Binding to Thrombin Anion Binding Exosite II

Evaluating factor XIII specificity for glutamine-containing substrates using a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay

Role of calcium in the conformational dynamics of factor XIII activation examined by hydrogen–deuterium exchange coupled with MALDI-TOF MS

Screening cleavage of Factor XIII V34X Activation Peptides by thrombin mutants: A strategy for controlling fibrin architecture

V34I and V34A substitutions within the factor XIII activation peptide segment (28-41) affect interactions with the thrombin active site

Factor XIII crosslinking in fibrinogen αc(233-425) is assisted by electrostatic and hydrophobic residues in αc(389-403)

Conformational Analysis of γ‘ Peptide (410−427) Interactions with Thrombin Anion Binding Exosite II

Employing Mutants to Study Thrombin Residues Responsible for Factor XIII Activation Peptide Recognition: A Kinetic Study

Characterizing the specificity of activated Factor XIII for glutamine-containing substrate peptides

Perturbations in Factor XIII Resulting from Activation and Inhibition Examined by Solution Based Methods and Detected by MALDI-TOF MS

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