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Chemistry

D-Index
60
Citations
20181
World Ranking
9533
National Ranking
2677

Research.com Recognitions

  • 1995 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Frank Jordan is affiliated with Rutgers, The State University of New Jersey in the United States and specializes in the fields of Biochemistry, Genetics and Molecular Biology. Their research contributions span various subfields including Biochemistry, Clinical Biochemistry, Molecular Biology, Neurology, and Cancer Research.

The scientist's work predominantly addresses topics such as Biochemical Acid Research Studies, Metabolism and Genetic Disorders, Alcoholism and Thiamine Deficiency, Cancer, Hypoxia, and Metabolism, Chemical Synthesis and Analysis, Phenothiazines and Benzothiazines Synthesis and Activities, and Synthesis and Reactivity of Sulfur-Containing Compounds.

Recent publications by Frank Jordan include:

  • "E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants," 2021, Hepatology
  • "DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo," 2020, Human Molecular Genetics
  • "Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure," 2021, Biochimica et Biophysica Acta (BBA) - General Subjects
  • "Toward an Understanding of the Structural and Mechanistic Aspects of Protein-Protein Interactions in 2-Oxoacid Dehydrogenase Complexes," 2021, Life
  • "Exclusive neuronal detection of KGDHC-specific subunits in the adult human brain cortex despite pancellular protein lysine succinylation," 2020, Brain Structure and Function

Frequent coauthors working alongside Frank Jordan include Natalia S. Nemeria, João Leandro, Sander M. Houten, Attila Ambrus, and Bálint Nagy.

Publications have appeared in scientific journals such as:

  • International Journal of Molecular Sciences
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Hepatology
  • Biochimica et Biophysica Acta (BBA) - General Subjects
  • Life

Frank Jordan was awarded the title of Fellow of the American Association for the Advancement of Science (AAAS) in 1995.

Best Publications

  • The pyruvate dehydrogenase complexes: Structure-based function and regulation

    Mulchand S. Patel;Natalia S. Nemeria;William Furey;Frank Jordan

  • Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps

    Natalia S. Nemeria;Sumit Chakraborty;Anand Balakrishnan;Frank Jordan

  • Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

    Junjie Wang;Natalia S. Nemeria;Krishnamoorthy Chandrasekhar;Sowmini Kumaran

  • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

    Xueli Zhu;Yoshiji Ohta;Frank Jordan;Masayori Inouye

  • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution.

    Fred Dyda;William Furey;Subramanyam Swaminathan;Martin Sax

  • Localized bond orbitals and the correlation problem

    S. Diner;J. P. Malrieu;F. Jordan;M. Gilbert

  • Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions.

    Frank Jordan

  • Recent Developments in Ruthenium-Catalyzed C–H Arylation: Array of Mechanistic Manifolds

    Pradeep Nareddy;Frank Jordan;Michal Szostak

  • Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution.

    P. Arjunan;T. Umland;T. Umland;F. Dyda;F. Dyda;S. Swaminathan;S. Swaminathan

  • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase

    Yves A Muller;Yves A Muller;Ylva Lindqvist;Ylva Lindqvist;William Furey;William Furey;Georg E Schulz;Georg E Schulz

  • Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution.

    Palaniappa Arjunan;Natalia Nemeria;Andrew Brunskill;Krishnamoorthy Chandrasekhar

  • NMR analysis of covalent intermediates in thiamin diphosphate enzymes.

    Kai Tittmann;Ralph Golbik;Kathrin Uhlemann;Ludmila Khailova

  • Inhibition of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Subunit and Its Tyrosine 177 Variants by Thiamin 2-Thiazolone and Thiamin 2-Thiothiazolone Diphosphates EVIDENCE FOR REVERSIBLE TIGHT-BINDING INHIBITION

    Natalia Nemeria;Yan Yan;Zhen Zhang;Angela M. Brown

  • Pro‐peptide as an intermolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro‐peptide

    Y. Ohta;H. Hojo;S. Aimoto;T. Kobayashi

  • Structural and Kinetic Analysis of Catalysis by a Thiamin Diphosphate-Dependent Enzyme, Benzoylformate Decarboxylase

    Elena S. Polovnikova;Michael J. McLeish;Eduard A. Sergienko;John T. Burgner

  • Purine nucleoside phosphorylase cleaves the C--O bond of ribose 1-phosphate. Evidence from the 18O shift in 31P NMR.

    F Jordan;J A Patrick;S Salamone

  • Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants

    Yuyun Li;Zhixiang Hu;Frank Jordan;Masayori Inouye

  • Localized bond orbitals and the correlation problem: IV. Stability of the perturbation energies with respect to bond hybridization and polarity

    F. Jordan;M. Gilbert;J. P. Malrieu;U. Pincelli

  • A Thiamin-bound, Pre-decarboxylation Reaction Intermediate Analogue in the Pyruvate Dehydrogenase E1 Subunit Induces Large Scale Disorder-to-Order Transformations in the Enzyme and Reveals Novel Structural Features in the Covalently Bound Adduct

    Palaniappa Arjunan;Martin Sax;Andrew Brunskill;Andrew Brunskill;Krishnamoorthy Chandrasekhar;Krishnamoorthy Chandrasekhar

  • Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme.

    Natalia Nemeria;Ahmet Baykal;Ebenezer Joseph;Sheng Zhang

  • Conformation of fibrous proteins

    Frank Jordan

  • Carbon-13 NMR spectroscopy

    Frank Jordan

Frequent Co-Authors

William Furey
William Furey University of Pittsburgh
Mulchand S. Patel
Mulchand S. Patel University at Buffalo, State University of New York
Michal Szostak
Michal Szostak Rutgers, The State University of New Jersey
Kai Tittmann
Kai Tittmann University of Göttingen
Vera Adam-Vizi
Vera Adam-Vizi Semmelweis University
Sander M. Houten
Sander M. Houten Icahn School of Medicine at Mount Sinai
Stefan Hohmann
Stefan Hohmann Chalmers University of Technology
Masayori Inouye
Masayori Inouye Rutgers, The State University of New Jersey
Richard Mendelsohn
Richard Mendelsohn Rutgers, The State University of New Jersey
Gregory A. Petsko
Gregory A. Petsko Cornell University

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