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Chemistry

D-Index
47
Citations
8995
World Ranking
15556
National Ranking
3925

Overview

Edith Wilson Miles is affiliated with the National Institutes of Health in the United States. Their academic profile does not currently list recent papers, co-authors, or frequent publication venues. This absence of data provides no indication of specific collaborative networks or preferred journals for dissemination of research findings.

The profile does not include information on book publications or detailed fields and subfields of study, so it is not possible to detail the scientific domains or disciplinary areas they focus on. Similarly, no main research topics have been documented to clarify the thematic concentration of their work.

There are no recorded awards associated with Edith Wilson Miles. This leaves the profile without information on recognitions or honors received throughout their career.

The available data confirms that Edith Wilson Miles is not deceased, indicating an ongoing potential for contributions in their area of expertise. However, without additional specifics on their research outputs or scholarly focus, the profile remains limited to affiliation and status.

Best Publications

  • Modification of histidyl residues in proteins by diethylpyrocarbonate.

    Edith Wilson Miles

  • Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

    C C Hyde;S A Ahmed;E A Padlan;E W Miles

  • The molecular basis of substrate channeling.

    Edith Wilson Miles;Sangkee Rhee;David R. Davies

  • Cystathionine β-Synthase: Structure, Function, Regulation, and Location of Homocystinuria-causing Mutations

    Edith Wilson Miles;Jan P. Kraus

  • Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase.

    Jerson L. Silva;Edith W. Miles;Gregorio Weber

  • Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism.

    K. S. Anderson;E. W. Miles;Kenneth Johnson

  • Tryptophan synthase: structure, function, and subunit interaction.

    Edith Wilson Miles

  • Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.

    S Rhee;K.D Parris;C.C Hyde;S.A Ahmed

  • Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.

    H Kawasaki;R Bauerle;G Zon;S A Ahmed

  • The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.

    E. W. Miles;H. Kawasaki;Syed Ashrafuddin Ahmed;H. Morita

  • An active proteolytic derivative of the alpha subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments.

    William Higgins;Thomas Fairwell;Edith Wilson Miles

  • Structural Basis for Catalysis by Tryptophan Synthase

    Edith Wilson Miles

  • Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.

    S Rhee;K.D Parris;S.A Ahmed;E.W Miles

  • [49] Tryptophan synthase from Escherichia coli and Salmonella typhimurium

    Edith Wilson Miles;Ronald Bauerle;Syed Ashrafuddin Ahmed

  • Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.

    Edith Wilson Miles

  • Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains.

    Edith Wilson Miles;Katsuhide Yutani;Kyoko Ogasahara

  • Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation.

    Kwang-Hwan Jhee;Peter McPhie;Edith Wilson Miles

  • Crystalline α2β2 Complexes of Tryptophan Synthetase of Escherichia coli: A COMPARISON BETWEEN THE NATIVE COMPLEX AND THE RECONSTITUTED COMPLEX

    Osao Adachi;Leonard D. Kohn;Edith Wilson Miles

  • The B protein of Escherichia coli tryptophan synthetase. I. Effects of sulfhydryl modification on enzymatic activities and subunit interaction.

    Edith Wilson Miles

  • The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site.

    S Nagata;C C Hyde;E W Miles

  • A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetase.

    Edith Wilson. Miles;M. Hatanaka;I. P. Crawford

Frequent Co-Authors

Peter McPhie
Peter McPhie National Institutes of Health
Robert S. Phillips
Robert S. Phillips University of Georgia
David R. Davies
David R. Davies National Institutes of Health
Nobuyoshi Esaki
Nobuyoshi Esaki Kyoto University
Katsuhide Yutani
Katsuhide Yutani Osaka University
Michael F. Dunn
Michael F. Dunn University of California, Riverside
Roger S. Goody
Roger S. Goody Max Planck Society
Kenji Soda
Kenji Soda Kansai University
Eduardo A. Padlan
Eduardo A. Padlan National Institutes of Health
Leonard D. Kohn
Leonard D. Kohn National Institutes of Health

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