World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
51
Citations
13945
World Ranking
16972
National Ranking
6997

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • DNA

His primary scientific interests are in DNA repair, Biochemistry, Stereochemistry, Heme and Dimer. The concepts of his DNA repair study are interwoven with issues in MRE11 Homologue Protein, Molecular biology and Homologous recombination. His Biochemistry study is mostly concerned with Binding site, DNA glycosylase, Uracil-DNA glycosylase, Uracil and Regulation of gene expression.

His DNA glycosylase research is under the purview of DNA. In most of his Stereochemistry studies, his work intersects topics such as Biophysics. His studies in Heme integrate themes in fields like Oxygenase, Nitric oxide synthase and NADPH binding.

His most cited work include:

  • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. (558 citations)
  • Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases (519 citations)
  • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. (459 citations)

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

His main research concerns Biochemistry, DNA repair, Stereochemistry, DNA and Protein structure. His study connects Cell biology and Biochemistry. His DNA repair research is multidisciplinary, relying on both Homologous recombination, Nucleotide, Molecular biology and DNA replication.

Andrew S. Arvai interconnects Nitric oxide synthase, Enzyme, Amide and Beta sheet in the investigation of issues within Stereochemistry. His DNA research is multidisciplinary, relying on both Alkyltransferase and Deamination. His studies in Protein structure integrate themes in fields like Biophysics and Plasma protein binding.

He most often published in these fields:

  • Biochemistry (48.75%)
  • DNA repair (32.50%)
  • Stereochemistry (27.50%)

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

  • DNA (25.00%)
  • DNA repair (32.50%)
  • DNA damage (12.50%)

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

Andrew S. Arvai mainly investigates DNA, DNA repair, DNA damage, Genome instability and Computational biology. Andrew S. Arvai is investigating DNA as part of his Genetics and Biochemistry and DNA study. The concepts of his DNA repair study are interwoven with issues in Cytosine and Uracil.

His DNA damage research incorporates elements of Mutation, Gene and Point mutation. He has researched Genome instability in several fields, including Homologous recombination, Exonuclease and Enzyme, Allosteric regulation, Active site. His Flap structure-specific endonuclease 1 study combines topics in areas such as Nucleotide, Molecular biology, Flap endonuclease, DNA replication and Binding site.

Between 2014 and 2021, his most popular works were:

  • The nucleotide‐dependent interaction of FlaH and FlaI is essential for assembly and function of the archaellum motor (37 citations)
  • Phosphate steering by Flap Endonuclease 1 promotes 5′-flap specificity and incision to prevent genome instability (35 citations)
  • Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations. (12 citations)

Best Publications

  • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.

    Brian R. Crane;Brian R. Crane;Andrew S. Arvai;Dipak K. Ghosh;Chaoqun Wu

  • Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

    John R Somoza;Robert J Skene;Bradley A Katz;Clifford Mol

  • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA.

    Geir Slupphaug;Clifford D. Mol;Bodil Kavli;Andrew S. Arvai

  • Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.

    Christopher D Putnam;Andrew S Arvai;Yves Bourne;John A Tainer

  • DNA Double-Strand Break Repair Pathway Choice Is Directed by Distinct MRE11 Nuclease Activities.

    Atsushi Shibata;Atsushi Shibata;Davide Moiani;Davide Moiani;Andrew S. Arvai;Andrew S. Arvai;Jefferson Perry;Jefferson Perry;Jefferson Perry

  • Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.

    Noriyuki Nishimura;Kenichi Hitomi;Kenichi Hitomi;Andrew S. Arvai;Robert P. Rambo

  • Plant uvr8 photoreceptor senses uv-b by tryptophan-mediated disruption of cross-dimer salt bridges

    John M. Christie;John M. Christie;Andrew S. Arvai;Katherine J. Baxter;Monika Heilmann

  • Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions

    Lisa Craig;Niels Volkmann;Andrew S. Arvai;Michael E. Pique

  • The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.

    Brian R. Crane;Andrew S. Arvai;Ratan Gachhui;Chaoqun Wu

  • Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis.

    Clifford D Mol;Andrew S Arvai;Geir Slupphaug;Bodil Kavli

  • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily

    Yue Guan;Raymond C. Manuel;Andrew S. Arvai;Sudip S. Parikh

  • XPD Helicase Structures and Activities: Insights into the Cancer and Aging Phenotypes from XPD Mutations

    Li Fan;Jill O. Fuss;Quen J. Cheng;Andrew S. Arvai

  • Type IV Pilin Structure and Assembly: X-Ray and EM Analyses of Vibrio cholerae Toxin-Coregulated Pilus and Pseudomonas aeruginosa PAK Pilin

    Lisa Craig;Ronald K Taylor;Michael E Pique;Brian D Adair

  • Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA

    Clifford D Mol;Andrew S Arvai;Russell J Sanderson;Geir Slupphaug

  • Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily

    Susan E. Tsutakawa;Scott Classen;Brian R. Chapados;Andrew S. Arvai

  • Full‐length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2

    David S. Shin;Luca Pellegrini;Douglas S. Daniels;Biana Yelent

  • Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.

    Zarah Forsberg;Alasdair K. Mackenzie;Morten Sørlie;Åsmund K. Røhr

  • Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.

    Elsa D. Garcin;Elsa D. Garcin;Andrew S. Arvai;Robin J. Rosenfeld;Matt D. Kroeger;Matt D. Kroeger

  • Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding

    Douglas S. Daniels;Clifford D. Mol;Andrew S. Arvai;Sreenivas Kanugula

  • Structural basis for endothelial nitric oxide synthase binding to calmodulin

    Mika Aoyagi;Andrew S. Arvai;John A. Tainer;Elizabeth D. Getzoff

Frequent Co-Authors

John A. Tainer
John A. Tainer The University of Texas MD Anderson Cancer Center
Elizabeth D. Getzoff
Elizabeth D. Getzoff Scripps Research Institute
Brian R. Crane
Brian R. Crane Cornell University
Dennis J. Stuehr
Dennis J. Stuehr Cleveland Clinic Lerner College of Medicine
Hans E. Krokan
Hans E. Krokan Norwegian University of Science and Technology
Geir Slupphaug
Geir Slupphaug Norwegian University of Science and Technology
Steven I. Reed
Steven I. Reed Scripps Research Institute
Duncan E. McRee
Duncan E. McRee Scripps Research Institute
Christopher D. Putnam
Christopher D. Putnam University of California, San Diego
Michael J. MacCoss
Michael J. MacCoss University of Washington

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