Muriel C. Maurer

A novel way for transglutaminase 2 to mitigate liver damage

Muriel C. Maurer

confer resistance to venetoclax-based therapy in patients with acute

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BPS2025 - Factor XIII residues crucial for forming a substrate recognition site

Rameesa D. Syed Mohammed, Lianay Gutierrez Luque, Daniel Joseph Deredge, Muriel C. Maurer

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Factor XIII Activation Peptide Residues Play Important Roles in Stability, Activation, and Transglutaminase Activity

Rameesa D. Syed Mohammed, Lianay Gutierrez Luque, Muriel C. Maurer

A subunit of factor XIII (FXIII-A) contains a unique activation peptide (AP) that protects the catalytic triad and prevents degradation. In plasma, FXIII is activated proteolytically (FXIII-A*) by thrombin and Ca 2+ cleaving AP, while in cytoplasm, it is activated nonproteolytically (FXIII-A°) …

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

Rameesa D. Syed Mohammed, Kellianne M. Piell, Muriel C. Maurer

BACKGROUND: Factor XIII (FXIII) forms covalent crosslinks across plasma and cellular substrates and has roles in hemostasis, wound healing, and bone metabolism. FXIII activity is implicated in venous thromboembolism (VTE) and is a target for developing pharmaceuticals, which requires understanding FXIII - …

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OC 28.5 Exploring Interdomain Interactions Mediated by the Factor XIII Activation Peptide

Muriel C. Maurer, Ruba J Mohammed, Lianay Gutierrez Luque

Background: Factor XIII-A (FXIII-A) transglutaminase, fibrin clot stabilizer, was identified as an obesity gene in humans.We demonstrated that its

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

Francis Dean O. Ablan, Muriel C. Maurer

Coagulation Factor XIII (FXIII) stabilizes blood clots by cross-linking glutamines and lysines in fibrin and other proteins. FXIII activity in the fibrinogen αC region (Fbg αC 221-610) is critical for clot stability and growth. Fbg αC 389-402 is a binding site for …

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

Rameesa Darul Amne, Syed Mohammed, Muriel C. Maurer

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

Richard L. Lumata, Divya A. Kumaravelu, Anoushka Bhat, Rameesa Darul Amne et autres

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Fbg αC 389-402 enhances factor XIII crosslinking in the fibrinogen αC region via electrostatic and hydrophobic interactions

Francis Dean O. Ablan, Muriel C. Maurer

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

Rameesa D. Syed Mohammed, Francis Dean O. Ablan, Nicholas M. McCann, Mohammed M. Hindi et autres

Factor XIII (FXIII) catalyzes formation of γ-glutamyl-ε-lysyl crosslinks between reactive glutamines (Q) and lysines (K). In plasma, FXIII is activated proteolytically (FXIII-A*) by the concerted action of thrombin and Ca2+. Cellular FXIII is activated nonproteolytically (FXIII-A°) by elevation of physiological Ca2+ concentrations. …

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

Francis Dean O. Ablan, Muriel C. Maurer

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Activity and Substrate Specificity of Factor XIII Resulting from Different Activation Pathways

Rameesa Darul Amne Syed Mohammed, Heli Butala, Muriel C. Maurer