M. Maurer

发表

Expression and Folding of Recombinant Bovine Prethrombin-2 and Its Activation to Thrombin (*)

H. Scheraga, E. Dibella, M. Maurer, 1995, The Journal of Biological Chemistry.

Structural examination of the influence of phosphorylation on the binding of fibrinopeptide A to bovine thrombin.

H. Scheraga, M. Maurer, J. Peng, 1998, Biochemistry.

High-affinity Ca(2+)- and substrate-binding sites on protein kinase C alpha as determined by nuclear magnetic resonance spectroscopy.

M. Maurer, C. Grisham, J. J. Sando, 1992, Biochemistry.

The role of β‐barrels 1 and 2 in the enzymatic activity of factor XIII A‐subunit

S. Radford, M. Maurer, P. Adamson, 2018, Journal of thrombosis and haemostasis : JTH.

Establishing the inhibitory effects of bradykinin on thrombin.

M. Maurer, W. Ehringer, D. B. Cleary, 2003, Archives of biochemistry and biophysics.

Thrombin hydrolysis of V29F and V34L mutants of factor XIII (28-41) reveals roles of the P(9) and P(4) positions in factor XIII activation.

M. Maurer, Toni A. Trumbo, 2002, Biochemistry.

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

M. Merchant, M. Maurer, Daniel W. Wilkey, 2019, Thrombosis and Haemostasis.

Evaluating Factor XIII Specificity for Glutamine-Containing Substrates Using a MALDI-TOF Mass Spectrometry Assay

M. Maurer, P. G. Doiphode, K. Mouapi, 2015 .

Effects of introducing fibrinogen Aalpha character into the factor XIII activation peptide segment.

M. Maurer, Toni A. Trumbo, Madhavi A Jadhav, 2010, Biochemistry.

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

M. Maurer, D. B. Cleary, 2006, Biochimica et biophysica acta.

Liberating R169 promotes anticoagulant protein C.

M. Maurer, 2012, Blood.

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

M. Maurer, Ricky T. Woofter, 2011, Archives of biochemistry and biophysics.

A non‐reactive glutamine residue of α2‐antiplasmin promotes interactions with the factor XIII active site region

M. Maurer, P. G. Doiphode, T. M. Sabo, 2009, Journal of thrombosis and haemostasis : JTH.

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

M. Maurer, P. G. Doiphode, K. Mouapi, 2014, Analytical biochemistry.

Perturbations in factor XIII resulting from activation and inhibition examined by solution based methods and detected by MALDI-TOF MS.

M. Maurer, T. M. Sabo, P. Brasher, 2007, Biochemistry.

Mapping of factor XIII solvent accessibility as a function of activation state using chemical modification methods.

M. Maurer, Brian T Turner, T. M. Sabo, 2004, Biochemistry.

Evaluating the roles of thrombin and calcium in the activation of coagulation factor XIII using H/D exchange and MALDI-TOF MS.

M. Maurer, Brian T Turner, 2002, Biochemistry.

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

M. Maurer, 2011, Proceedings of the National Academy of Sciences.

THROMBOSIS AND HEMOSTASIS Ranking reactive glutamines in the ﬁ brinogen a C region that are targeted by blood coagulant factor XIII

M. Maurer, H. Philippou, R. Ariëns, 2016 .

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

M. Maurer, W. Dean, B. Anokhin, 2020, The FEBS journal.

Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants.

M. Maurer, W. Goldsberry, Madhavi A Jadhav, 2011, Biochimica et biophysica acta.

Examining Thrombin Hydrolysis of the Factor XIII Activation Peptide Segment Leads to a Proposal for Explaining the Cardioprotective Effects Observed with the Factor XIII V34L Mutation*

M. Maurer, Toni A. Trumbo, 2000, The Journal of Biological Chemistry.

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

M. Maurer, Mohammed M. Hindi, F. Ablan, 2022, Thrombosis and Haemostasis.

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

M. Maurer, H. Philippou, R. Ariëns, 2016, Blood.

Role of cofactors in protein kinase C activation.

M. Maurer, C. Grisham, J. J. Sando, 1992, Cellular signalling.

Activation and inhibition of protein kinase C isozymes α and β by Gd3

M. Maurer, C. Grisham, Julianne J. Sandof, 1992 .

Probing interactions between the coagulants thrombin, Factor XIII, and fibrin(ogen).

M. Maurer, Muriel C Maurer, Toni A Trumbo, 2006, Archives of biochemistry and biophysics.

New general approach for determining the solution structure of a ligand bound weakly to a receptor: structure of a fibrinogen Aα‐like peptide bound to thrombin(S195A) obtained using NOE distance constraints and an ECEPP/3 flexible docking program

H A Scheraga, H. Scheraga, C. Lester, 1999, Proteins.

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

M. Maurer, T. M. Sabo, Ramya Billur, 2019, Biochemistry.

Conformational analysis of gamma' peptide (410-427) interactions with thrombin anion binding exosite II.

M. Maurer, D. Farrell, T. M. Sabo, 2006, Biochemistry.

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

M. Maurer, W. Dean, B. Anokhin, 2017, The FEBS journal.

Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.

M. Maurer, T. M. Sabo, 2009, Biochemistry.

Conformational analysis of γ′ peptide (410-427) interactions with thrombin anion binding exosite II

M. Maurer, D. Farrell, T. M. Sabo, 2006 .

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

M. Maurer, T. M. Sabo, M. Malovichko, 2013, The Journal of Biological Chemistry.

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

M. Maurer, David Ban, T. M. Sabo, 2017, Biochemistry.

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

M. Maurer, B. Anokhin, Kelsey N. Lamb, 2017, Biochimica et biophysica acta. Proteins and proteomics.

Protease-activated receptor 4-like peptides bind to thrombin through an optimized interaction with the enzyme active site surface.

M. Maurer, D. B. Cleary, Toni A. Trumbo, 2002, Archives of biochemistry and biophysics.

Employing mutants to study thrombin residues responsible for factor XIII activation peptide recognition: a kinetic study.

M. Maurer, G. Isetti, 2007, Biochemistry.

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

M. Maurer, F. Ablan, 2023, Biochemistry.

Structural features associated with the binding of glutamine-containing peptides to Factor XIII.

M. Maurer, D. B. Cleary, A. Marinescu, 2002, Archives of biochemistry and biophysics.

The role of barrels 1 and 2 in the enzymatic activity of factor XIII‐A

M. Maurer, P. Adamson, R. Pease, 2018 .

Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.

M. Maurer, T. M. Sabo, 2009, Biochemistry.

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

L. Alberio, M. Maurer, V. Schroeder, 2018, Thrombosis and Haemostasis.