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Chemistry

D-Index
55
Citations
9614
World Ranking
12264
National Ranking
3272

Research.com Recognitions

  • 2010 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Paul F. Fitzpatrick is affiliated with The University of Texas Health Science Center at San Antonio in the United States. Their research predominantly falls within the field of Biochemistry, Genetics and Molecular Biology, with specialized focus in Molecular Biology, Electrical and Electronic Engineering, Inorganic Chemistry, Biochemistry, and Cell Biology.

The main topics addressed in their work include:

  • Metal-Catalyzed Oxygenation Mechanisms
  • Amino Acid Enzymes and Metabolism
  • Protein Structure and Dynamics
  • Endoplasmic Reticulum Stress and Disease
  • Metabolomics and Mass Spectrometry Studies
  • Microbial Metabolism and Applications
  • Enzyme Catalysis and Immobilization

Research outputs by Fitzpatrick have been published primarily in the journal Archives of Biochemistry and Biophysics, where they have contributed to four articles. Additionally, one publication appears on arXiv (Cornell University), alongside work listed in Methods in enzymology on CD-ROM/Methods in enzymology.

Recent scientific papers authored or co-authored by Fitzpatrick include:

  • The aromatic amino acid hydroxylases: Structures, catalysis, and regulation of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase (2023, Archives of Biochemistry and Biophysics)
  • Conservation of mechanism in flavoprotein-catalyzed amine oxidation (2024, Archives of Biochemistry and Biophysics)

Other notable recent publications in the same journal, though authored by collaborators rather than Fitzpatrick, include: Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum (2022), Archives of Biochemistry and Biophysics: 80th Anniversary (2022), along with a contribution to the preprint repository arXiv on a topic related to MU-MIMO transmissions (2023).

Frequent collaborators with Fitzpatrick include Mingjie Li, Bishnu P. Subedi, Joseph P. Emerson, Helmut Sies, and Anthony Newman.

Fitzpatrick has been recognized as a Fellow of the American Association for the Advancement of Science (AAAS) since 2010.

Best Publications

  • Tetrahydropterin-dependent amino acid hydroxylases.

    Paul F. Fitzpatrick

  • Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.

    Kenneth E. Goodwill;Christelle Sabatier;Cara Marks;Cara Marks;Reetta Raag

  • Mechanism of Aromatic Amino Acid Hydroxylation

    Paul F. Fitzpatrick

  • Structures and mechanism of the monoamine oxidase family

    Helena Gaweska;Paul F. Fitzpatrick

  • Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat.

    Isabelle Becher;Thilo Werner;Carola Doce;Esther A Zaal

  • Oxidation of amines by flavoproteins

    Paul F. Fitzpatrick

  • Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase.

    Bekir E. Eser;Eric W. Barr;Patrick A. Frantom;Lana Saleh

  • Site-directed mutagenesis of serine 40 of rat tyrosine hydroxylase. Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity.

    S C Daubner;C Lauriano;J W Haycock;P F Fitzpatrick

  • Preclinical evaluation of multiple species of PEGylated recombinant phenylalanine ammonia lyase for the treatment of phenylketonuria.

    Christineh N. Sarkissian;Alejandra Gámez;Lin Wang;Marilyse Charbonneau

  • Characterization of the active site iron in tyrosine hydroxylase. Redox states of the iron

    Andrew J. Ramsey;Patrick J. Hillas;Paul F. Fitzpatrick

  • STEADY-STATE KINETIC MECHANISM OF RAT TYROSINE HYDROXYLASE

    Paul F. Fitzpatrick

  • Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.

    Steve P. Meisburger;Alexander B. Taylor;Crystal A. Khan;Shengnan Zhang

  • The Aromatic Amino Acid Hydroxylases

    Paul F. Fitzpatrick

  • Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: Evidence for a novel regulatory mechanism

    Andrew J. Ramsey;Paul F. Fitzpatrick

  • Substrate dehydrogenation by flavoproteins.

    Paul F. Fitzpatrick

  • Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations

    Paul F. Fitzpatrick

  • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines.

    Patrick J. Hillas;Paul F. Fitzpatrick

  • Mechanisms of tryptophan and tyrosine hydroxylase.

    Kenneth M. Roberts;Paul F. Fitzpatrick

  • Evidence for a High-Spin Fe(IV) Species in the Catalytic Cycle of a Bacterial Phenylalanine Hydroxylase

    Aram Joel Panay;Michael Lee;Carsten Krebs;J. Martin Bollinger

  • Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase [17]

    Kevin A. Kurtz;Mark A. Rishavy;W. W. Cleland;Paul F. Fitzpatrick

  • Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase

    Erik C. Ralph;Jennifer S. Hirschi;Mark A. Anderson;W. Wallace Cleland

Frequent Co-Authors

P. John Hart
P. John Hart The University of Texas Health Science Center at San Antonio
Vincent Massey
Vincent Massey University of Michigan–Ann Arbor
John M. Denu
John M. Denu University of Wisconsin–Madison
Hans V. Westerhoff
Hans V. Westerhoff Vrije Universiteit Amsterdam
David H. Russell
David H. Russell Texas A&M University
Raymond C. Stevens
Raymond C. Stevens University of Southern California
J. Martin Bollinger
J. Martin Bollinger Pennsylvania State University
Carsten Krebs
Carsten Krebs Pennsylvania State University
Peter J. Halling
Peter J. Halling University of Strathclyde
Dan Thomas Major
Dan Thomas Major Bar-Ilan University

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