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Lorena S. Beese

Lorena S. Beese

D-Index & Metrics

Biology and Biochemistry

D-Index
47
Citations
12083
World Ranking
18586
National Ranking
7597

Research.com Recognitions

  • 2009 - Member of the National Academy of Sciences

Overview

What is she best known for?

The fields of study she is best known for:

  • Enzyme
  • DNA
  • Amino acid

Her primary areas of study are Biochemistry, DNA clamp, DNA polymerase, DNA polymerase II and DNA polymerase I. Her research in Active site, Farnesyltransferase and Prenylation are components of Biochemistry. Her study looks at the relationship between DNA clamp and topics such as DNA replication, which overlap with Primase.

Within one scientific family, Lorena S. Beese focuses on topics pertaining to Base pair under DNA polymerase, and may sometimes address concerns connected to Polymerase. Her DNA polymerase I research is multidisciplinary, incorporating perspectives in Klenow fragment and Exonuclease. Her study in Klenow fragment is interdisciplinary in nature, drawing from both 3'-5' Exonuclease and Stereochemistry.

Her most cited work include:

  • Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. (827 citations)
  • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. (454 citations)
  • Structure of DNA polymerase I Klenow fragment bound to duplex DNA (419 citations)

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

Lorena S. Beese mainly investigates Biochemistry, Farnesyltransferase, DNA polymerase, Stereochemistry and Enzyme. As part of her studies on Biochemistry, she frequently links adjacent subjects like DNA polymerase I. Her research investigates the connection between DNA polymerase I and topics such as Klenow fragment that intersect with problems in 3'-5' Exonuclease.

Her Farnesyltransferase study combines topics in areas such as Signal transduction, Structure–activity relationship and Prenyltransferase. Her DNA polymerase research includes themes of DNA clamp, Polymerase, Base pair and DNA replication. The study incorporates disciplines such as DNA polymerase II and Primase in addition to DNA clamp.

She most often published in these fields:

  • Biochemistry (66.67%)
  • Farnesyltransferase (33.33%)
  • DNA polymerase (28.21%)

What were the highlights of her more recent work (between 2010-2020)?

  • Biochemistry (66.67%)
  • DNA (16.67%)
  • Farnesyltransferase (33.33%)

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

Biochemistry, DNA, Farnesyltransferase, DNA polymerase and Stereochemistry are her primary areas of study. Her research integrates issues of Molecular biology and Click chemistry in her study of Biochemistry. As a part of the same scientific study, Lorena S. Beese usually deals with the DNA, concentrating on Biophysics and frequently concerns with Flap endonuclease and DNA polymerase II.

Her Farnesyltransferase study incorporates themes from Protein structure and Tetrapeptide. Lorena S. Beese interconnects Protein–DNA interaction, Base pair, Polymerase and DNA polymerase I in the investigation of issues within DNA polymerase. Her study focuses on the intersection of Stereochemistry and fields such as Active site with connections in the field of Enzyme kinetics.

Between 2010 and 2020, her most popular works were:

  • Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis. (162 citations)
  • Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family (115 citations)
  • The Structure of a High Fidelity DNA Polymerase Bound to a Mismatched Nucleotide Reveals an “Ajar” Intermediate Conformation in the Nucleotide Selection Mechanism (70 citations)

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

  • Enzyme
  • DNA
  • Amino acid

Her primary areas of investigation include Biochemistry, DNA, DNA polymerase, Polymerase and Biophysics. Her Biochemistry study combines topics in areas such as Pathogen and Cryptococcus neoformans. Her DNA study is mostly concerned with Flap endonuclease and Nuclease.

Lorena S. Beese has researched DNA polymerase in several fields, including DNA polymerase I, Stereochemistry, Enzyme kinetics and Active site. Lorena S. Beese combines subjects such as Nucleoside triphosphate, Base pair, Tautomer and A-DNA with her study of Polymerase. Her biological study spans a wide range of topics, including HMG-box, DNA/RNA non-specific endonuclease, DNA polymerase II and DNA repair.

Best Publications

  • Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism.

    L. S. Beese;T. A. Steitz

  • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal.

    James R. Kiefer;Chen Mao;Jeffrey C. Braman;Lorena S. Beese

  • Structure of DNA polymerase I Klenow fragment bound to duplex DNA

    Lorena S. Beese;Victoria Derbyshire;Thomas A. Steitz

  • Crystal Structure of Protein Farnesyltransferase at 2.25 Angstrom Resolution

    Hee-Won Park;Sobha R. Boduluri;John F. Moomaw;Patrick J. Casey

  • Cocrystal structure of an editing complex of Klenow fragment with DNA

    P S Freemont;J M Friedman;L S Beese;M R Sanderson

  • Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I

    Victoria Derbyshire;Paul S. Freemont;Mark R. Sanderson;Lorena Beese

  • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase

    Gerald W Hsu;Matthias Ober;Thomas Carell;Lorena S Beese

  • Structures of Mismatch Replication Errors Observed in a DNA Polymerase

    Sean J. Johnson;Lorena S. Beese

  • Structure of the Human MutSalpha DNA Lesion Recognition Complex.

    Joshua J. Warren;Timothy J. Pohlhaus;Anita Changela;Ravi R. Iyer;Ravi R. Iyer

  • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations

    Sean J. Johnson;Jeffrey S. Taylor;Lorena S. Beese

  • Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I.

    Kimberly T. Lane;Lorena S. Beese

  • Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.

    T.S. Reid;K.L. Terry;P.J. Casey;L.S. Beese

  • Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis.

    Weina Wang;Homme W. Hellinga;Lorena S. Beese

  • Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue.

    Corey L. Strickland;William T. Windsor;Rosalinda Syto;Lynn Wang

  • Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate.

    Lorena S. Beese;Jonathan M. Friedman;Thomas A. Steitz

  • Reaction path of protein farnesyltransferase at atomic resolution

    Stephen B. Long;Patrick J. Casey;Lorena S. Beese

  • Crystal structure of a thermostable Bacillus DNA polymerase l large fragment at 2.1 Å resolution

    James R Kiefer;Chen Mao;Connie J Hansen;Scott L Basehore

  • Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7.

    A C Rodriguez;H W Park;C Mao;L S Beese

  • Cocrystal Structure of Protein Farnesyltransferase Complexed with a Farnesyl Diphosphate Substrate

    Stephen B. Long;Patrick J. Casey;Lorena S. Beese

  • The structural basis for the mutagenicity of O6-methyl-guanine lesions

    Joshua J. Warren;Lawrence J. Forsberg;Lorena S. Beese

Frequent Co-Authors

Homme W. Hellinga
Homme W. Hellinga Duke University
Thomas A. Steitz
Thomas A. Steitz Yale University
Paul Modrich
Paul Modrich Duke University
Patrick J. Casey
Patrick J. Casey National University of Singapore
Paul S. Freemont
Paul S. Freemont Imperial College London
Mark D. Distefano
Mark D. Distefano University of Minnesota
Michael H. Gelb
Michael H. Gelb University of Washington
Wesley C. Van Voorhis
Wesley C. Van Voorhis University of Washington
Thomas Carell
Thomas Carell Ludwig-Maximilians-Universität München
Said M. Sebti
Said M. Sebti Virginia Commonwealth University

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