World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
60
Citations
16996
World Ranking
11766
National Ranking
5060

Research.com Recognitions

  • 2001 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

David B. McKay is affiliated with Stanford University in the United States. Their research spans multiple fields including Materials Science, Social Sciences, and Computer Science. Within these broader categories, their subfields of study include Materials Chemistry, Communication, and Information Systems.

Their research topics cover areas such as Enzyme Structure and Function, Wikis in Education and Collaboration, and Web and Library Services. These areas reflect an interdisciplinary approach that combines scientific investigation with educational and informational systems.

McKay has authored publications in notable academic venues. One recent paper is:

  • The First Paragraph Is As Good As It Gets: STEM Articles in Wikipedia and Opportunistic Learning (2021) published in College Teaching

Frequent collaborators in McKay's research include:

  • Irene T. Weber
  • Thomas A. Steitz
  • Peter K. Dunn
  • Elizabeth A. Brunton
  • Margaret Marshman

The scientist's work in enzyme structure and function ties into the broader field of materials chemistry, while their engagement with wikis and web services intersects with communication and information systems research.

McKay was recognized as a Fellow of the American Association for the Advancement of Science (AAAS) in 2001, acknowledging contributions within their scientific community.

Best Publications

  • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

    Kevin M. Flaherty;Camilla DeLuca-Flaherty;David B. McKay

  • Three-dimensional structure of a hammerhead ribozyme

    Heinz W. Pley;Kevin M. Flaherty;David B. McKay

  • The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.

    W. Stöcker;F. Grams;U. Baumann;P. Reinemer

  • Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA

    David B. McKay;Thomas A. Steitz

  • Helicase structure and mechanism.

    Jonathan M Caruthers;David B McKay

  • Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.

    V S Allured;R J Collier;S F Carroll;D B McKay

  • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.

    U. Baumann;Shan Wu;K. M. Flaherty;D. B. Mckay

  • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein.

    Kevin M. Flaherty;David B. McKay;Wolfgang Kabsch;Kenneth C. Holmes

  • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

    Jonathan M. Caruthers;Eric R. Johnson;David B. McKay

  • Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix

    Heinz W. Pley;Kevin M. Flaherty;David B. McKay

  • Crystal and Solution Structures of an HslUV Protease–Chaperone Complex

    Marcelo C. Sousa;Christine B. Trame;Hiro Tsuruta;Sigurd M. Wilbanks

  • Three-dimensional structure of interleukin-2.

    Barbara J. Brandhuber;Tom Boone;William C. Kenney;David B. McKay

  • Three-dimensional structure of recoverin, a calcium sensor in vision

    Kevin M. Flaherty;Sergey Zozulya;Lubert Stryer;David B. McKay

  • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.

    M M Thayer;K M Flaherty;D B McKay

  • Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP.

    D B McKay;I T Weber;T A Steitz

  • Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins

    T. A. Steitz;D. H. Ohlendorf;D. B. McKay;W. F. Anderson

  • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.

    Eduard Bitto;David B. McKay

  • Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription.

    Shuying Wang;Rhonda T. Fleming;Edwin M. Westbrook;Philip Matsumura

  • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.

    K.M. Flaherty;S.M. Wilbanks;C. DeLuca-Flaherty;D.B. McKay

  • Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis

    Camille DeLuca-Flaherty;David B. McKay;Peter Parham;Beth L. Hill

Frequent Co-Authors

Michael Toft Overgaard
Michael Toft Overgaard Aalborg University
Benedikt M. Kessler
Benedikt M. Kessler University of Oxford
Herman S. Overkleeft
Herman S. Overkleeft Leiden University
Ulrich Baumann
Ulrich Baumann University of Cologne
Lubert Stryer
Lubert Stryer Stanford University
Olke C. Uhlenbeck
Olke C. Uhlenbeck Northwestern University
Robert J Collier
Robert J Collier University of Arizona
Gerard Zurawski
Gerard Zurawski Baylor University
Peter Parham
Peter Parham Stanford University
Stanley N. Cohen
Stanley N. Cohen Stanford University

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Best Scientists Citing David B. McKay