World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
66
Citations
12570
World Ranking
8850
National Ranking
3940

Overview

What is he best known for?

The fields of study he is best known for:

  • DNA
  • Enzyme
  • Gene

William A. Beard mostly deals with Biochemistry, DNA polymerase, Polymerase, DNA and DNA clamp. His research brings together the fields of Stereochemistry and Biochemistry. His DNA polymerase research includes elements of Base pair, DNA polymerase beta and Active site.

His research in Polymerase tackles topics such as Protein structure which are related to areas like Enzyme, Alanine scanning, A-DNA and Catalytic complex. His studies deal with areas such as DNA polymerase II and DNA polymerase I as well as DNA clamp. As a member of one scientific family, William A. Beard mostly works in the field of DNA polymerase lambda, focusing on Molecular biology and, on occasion, Mutagenesis and Site-directed mutagenesis.

His most cited work include:

  • Magnesium-induced assembly of a complete DNA polymerase catalytic complex. (204 citations)
  • Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism. (168 citations)
  • Enzyme-DNA interactions required for efficient nucleotide incorporation and discrimination in human DNA polymerase β (151 citations)

What are the main themes of his work throughout his whole career to date?

His scientific interests lie mostly in DNA polymerase, DNA polymerase beta, Biochemistry, Stereochemistry and Polymerase. His DNA polymerase study combines topics from a wide range of disciplines, such as Base pair, DNA replication and Active site. His DNA polymerase beta research is multidisciplinary, incorporating elements of Molecular biology and Substrate.

His Stereochemistry research also works with subjects such as

  • Ternary complex which is related to area like Crystallography,
  • Nucleotide which is related to area like Conformational change. His Polymerase study incorporates themes from Mutant and A-DNA. His work focuses on many connections between DNA clamp and other disciplines, such as DNA polymerase II, that overlap with his field of interest in DNA polymerase mu.

He most often published in these fields:

  • DNA polymerase (60.14%)
  • DNA polymerase beta (38.51%)
  • Biochemistry (39.86%)

What were the highlights of his more recent work (between 2014-2021)?

  • DNA polymerase (60.14%)
  • DNA (31.76%)
  • Polymerase (31.08%)

In recent papers he was focusing on the following fields of study:

William A. Beard mostly deals with DNA polymerase, DNA, Polymerase, DNA polymerase beta and Stereochemistry. The concepts of his DNA polymerase study are interwoven with issues in Ternary complex, Base excision repair, DNA replication and Active site. In the field of Biochemistry and Genetics William A. Beard studies DNA.

His research in Polymerase focuses on subjects like Nucleotide, which are connected to Enzyme. His research on DNA polymerase beta frequently links to adjacent areas such as Molecular biology. His research investigates the link between Stereochemistry and topics such as Base pair that cross with problems in Cytosine.

Between 2014 and 2021, his most popular works were:

  • Uncovering the polymerase-induced cytotoxicity of an oxidized nucleotide (83 citations)
  • Capturing snapshots of APE1 processing DNA damage (62 citations)
  • Eukaryotic Base Excision Repair: New Approaches Shine Light on Mechanism. (38 citations)

In his most recent research, the most cited papers focused on:

  • DNA
  • Enzyme
  • Gene

William A. Beard mainly investigates DNA polymerase, DNA, Polymerase, Biochemistry and DNA replication. His DNA polymerase research is multidisciplinary, incorporating perspectives in Base excision repair and DNA glycosylase. DNA repair and Base pair are subfields of DNA in which his conducts study.

In his research, he performs multidisciplinary study on Polymerase and DNA clamp. His work on DNA damage, Active site and AP site as part of his general Biochemistry study is frequently connected to Magnesium ion, thereby bridging the divide between different branches of science. His Active site research incorporates elements of Combinatorial chemistry, Stereochemistry and Reaction mechanism.

Best Publications

  • Structure and mechanism of DNA polymerase β.

    William A Beard;Samuel H Wilson

  • Mammalian Abasic Site Base Excision Repair: IDENTIFICATION OF THE REACTION SEQUENCE AND RATE-DETERMINING STEPS *

    Deepak K. Srivastava;Brian J. Vande Berg;Rajendra Prasad;James T. Molina

  • Magnesium-induced assembly of a complete DNA polymerase catalytic complex.

    Vinod K. Batra;William A. Beard;David D. Shock;Joseph M. Krahn

  • Enzyme-DNA interactions required for efficient nucleotide incorporation and discrimination in human DNA polymerase β

    William A. Beard;Wendy P. Osheroff;Rajendra Prasad;Michael R. Sawaya

  • Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism.

    Rajendra Prasad;William A. Beard;Phyllis R. Strauss;Samuel H. Wilson

  • Observing a DNA polymerase choose right from wrong.

    Bret D. Freudenthal;William A. Beard;David D. Shock;Samuel H. Wilson

  • The X family portrait: structural insights into biological functions of X family polymerases.

    Andrea F. Moon;Miguel Garcia-Diaz;Vinod K. Batra;William A. Beard

  • [11] Purification and domain-mapping of mammalian DNA polymerase β

    William A. Beard;Samuel H. Wilson

  • DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase beta. Implication for the identity of the rate-limiting conformational change.

    Brian J. Vande Berg;William A. Beard;Samuel H. Wilson

  • Structural insights into the origins of DNA polymerase fidelity.

    William A Beard;Samuel H Wilson

  • Structural design of a eukaryotic DNA repair polymerase: DNA polymerase β

    William A Beard;Samuel H Wilson

  • The fidelity of DNA polymerase beta during distributive and processive DNA synthesis

    Wendy P. Osheroff;Hai Kwan Jung;William A. Beard;Samuel H. Wilson

  • Substrate Binding by Human Apurinic/Apyrimidinic Endonuclease Indicates a Briggs-Haldane Mechanism

    Phyllis R. Strauss;William A. Beard;Thomas A. Patterson;Samuel H. Wilson

  • DNA Polymerase β and Flap Endonuclease 1 Enzymatic Specificities Sustain DNA Synthesis for Long Patch Base Excision Repair

    Yuan Liu;William A. Beard;David D. Shock;Rajendra Prasad

  • Substrate Channeling in Mammalian Base Excision Repair Pathways: Passing the Baton

    Rajendra Prasad;David D. Shock;William A. Beard;Samuel H. Wilson

  • Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β

    Yuan Liu;Rajendra Prasad;William A. Beard;Padmini S. Kedar

  • Critical role of magnesium ions in DNA polymerase beta's closing and active site assembly.

    Linjing Yang;Karunesh Arora;William A. Beard;Samuel H. Wilson

  • Functional Analysis of the Amino-terminal 8-kDa Domain of DNA Polymerase β as Revealed by Site-directed Mutagenesis DNA BINDING AND 5′-DEOXYRIBOSE PHOSPHATE LYASE ACTIVITIES

    Rajendra Prasad;Rajendra Prasad;William A. Beard;William A. Beard;Jan Y. Chyan;Mark W. Maciejewski

  • Studies of gapped DNA substrate binding by mammalian DNA polymerase beta. Dependence on 5'-phosphate group.

    Rajendra Prasad;W. A. Beard;S. H. Wilson

  • Structure of DNA Polymerase beta with the Mutagenic DNA Lesion 8-oxodeoxyguanine Reveals Structural Insights into its Coding Potential

    Joseph M Krahn;William A Beard;Holly Miller;Arthur P Grollman

Frequent Co-Authors

Samuel H. Wilson
Samuel H. Wilson National Institutes of Health
Lars C. Pedersen
Lars C. Pedersen National Institutes of Health
Rajendra Prasad
Rajendra Prasad Amity University
Lee G. Pedersen
Lee G. Pedersen University of North Carolina at Chapel Hill
Thomas A. Kunkel
Thomas A. Kunkel National Institutes of Health
Tamar Schlick
Tamar Schlick New York University
Katarzyna Bebenek
Katarzyna Bebenek National Institutes of Health
Myron F. Goodman
Myron F. Goodman University of Southern California
Lalith Perera
Lalith Perera National Institutes of Health
Robert E. London
Robert E. London National Institutes of Health

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