World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
62
Citations
13674
World Ranking
10805
National Ranking
4692

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • DNA

His primary scientific interests are in Biochemistry, Nuclear magnetic resonance spectroscopy, Crystallography, Stereochemistry and Binding site. Many of his studies on Biochemistry apply to Biophysics as well. He has researched Nuclear magnetic resonance spectroscopy in several fields, including Protein structure and Helix.

His study focuses on the intersection of Crystallography and fields such as Conformational change with connections in the field of Consensus sequence, Peptide binding and Polyproline helix. The Stereochemistry study combines topics in areas such as Mutation, Mutant, Site-directed mutagenesis, Substrate and Peptide. His study looks at the relationship between Binding site and fields such as Peptide sequence, as well as how they intersect with chemical problems.

His most cited work include:

  • S100 proteins in cancer (349 citations)
  • S100A4, a mediator of metastasis. (306 citations)
  • Structure of the negative regulatory domain of p53 bound to S100B(betabeta) (276 citations)

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

David J. Weber spends much of his time researching Biochemistry, Stereochemistry, Cancer research, Binding site and Crystallography. He interconnects Biophysics, Calcium-binding protein and Cell biology in the investigation of issues within Biochemistry. His biological study spans a wide range of topics, including Peptide and Active site.

His Peptide research incorporates elements of Molecular biology, Peptide sequence and Phosphorylation. His work deals with themes such as Cancer, Cell culture, Apoptosis and In vivo, which intersect with Cancer research. His Crystallography study combines topics from a wide range of disciplines, such as Protein structure, Conformational change, Nuclear magnetic resonance spectroscopy and EF hand.

He most often published in these fields:

  • Biochemistry (24.86%)
  • Stereochemistry (19.46%)
  • Cancer research (19.46%)

What were the highlights of his more recent work (between 2017-2021)?

  • Small molecule (7.57%)
  • Pore-forming toxin (5.41%)
  • Cell biology (16.22%)

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

His scientific interests lie mostly in Small molecule, Pore-forming toxin, Cell biology, Biochemistry and Protein subunit. His research on Small molecule also deals with topics like

  • Function which is related to area like Melanoma,
  • Ligand which is related to area like Conformational change, Heteronuclear molecule, Transverse relaxation-optimized spectroscopy, Heteronuclear single quantum coherence spectroscopy and Small G Protein. His research investigates the connection with Melanoma and areas like Chemical biology which intersect with concerns in Cancer research and Drug.

His studies in Drug integrate themes in fields like Stereochemistry and DNA. His work in Cell biology addresses issues such as Conserved sequence, which are connected to fields such as Rational design and Protein engineering. David J. Weber focuses mostly in the field of Binding site, narrowing it down to topics relating to Biophysics and, in certain cases, Posttranslational modification, Substrate-level phosphorylation, Phosphorylation and Protein structure.

Between 2017 and 2021, his most popular works were:

  • Unprecedented anticancer activities of organorhenium sulfonato and carboxylato complexes against hormone-dependent MCF-7 and hormone-independent triple-negative MDA-MB-231 breast cancer cells. (13 citations)
  • Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a di-heptamer macromolecular assembly. (6 citations)
  • Galeterone and The Next Generation Galeterone Analogs, VNPP414 and VNPP433-3β Exert Potent Therapeutic Effects in Castration-/Drug-Resistant Prostate Cancer Preclinical Models In Vitro and In Vivo. (6 citations)

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

  • Gene
  • Enzyme
  • DNA

His main research concerns Binding site, Biochemistry, Stereochemistry, Biophysics and Small molecule. His work carried out in the field of Binding site brings together such families of science as Enterotoxin, Substrate-level phosphorylation, Phosphorylation, MAPK/ERK pathway and Protein structure. David J. Weber performs multidisciplinary study in Biochemistry and Pore-forming toxin in his work.

His Stereochemistry research integrates issues from Active site, Dimer and Nerve agent. His Biophysics research incorporates themes from Transverse relaxation-optimized spectroscopy, Heteronuclear molecule, Protein kinase A and Ligand. His Small molecule research is multidisciplinary, incorporating perspectives in Small G Protein, Cancer, Heteronuclear single quantum coherence spectroscopy, Fluorescence anisotropy and Function.

Best Publications

  • S100 proteins in cancer

    Anne R. Bresnick;David J. Weber;Danna B. Zimmer

  • Common variants at SCN5A-SCN10A and HEY2 are associated with Brugada syndrome, a rare disease with high risk of sudden cardiac death

    Connie R Bezzina;Julien Barc;Yuka Mizusawa;Carol Ann Remme

  • S100A4, a mediator of metastasis.

    Sarah C. Garrett;Kristen M. Varney;David J. Weber;Anne R. Bresnick

  • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)

    R R Rustandi;D M Baldisseri;D J Weber

  • Bacterial contamination of keyboards : Efficacy and functional impact of disinfectants

    William A. Rutala;Matthew S. White;Maria F. Gergen;David J. Weber

  • The Ca(2+)-dependent interaction of S100B(beta beta) with a peptide derived from p53

    Richard R. Rustandi;Alexander C. Drohat;Donna M. Baldisseri;Paul T. Wilder

  • Incidence and Secondary Transmission of SARS-CoV-2 Infections in Schools.

    Kanecia O. Zimmerman;Ibukunoluwa C. Akinboyo;M. Alan Brookhart;Angelique E. Boutzoukas

  • Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,.

    Alexander C. Drohat;Donna M. Baldisseri;Richard R. Rustandi;David J. Weber

  • Inhibition of p53 Transcriptional Activity by the S100B Calcium-binding Protein *

    Jing Lin;Mellissa Blake;Chun Tang;Danna B. Zimmer

  • Quantitative interpretations of double mutations of enzymes

    Albert S. Mildvan;David J. Weber;Athan Kuliopulos

  • Molecular mechanisms of S100‐target protein interactions

    Danna B. Zimmer;Patti Wright Sadosky;David J. Weber

  • Inhibiting S100B Restores p53 Levels in Primary Malignant Melanoma Cancer Cells

    Jing Lin;Qingyuan Yang;Zhe Yan;Joseph Markowitz

  • Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.

    Alexander C. Drohat;Judith C. Amburgey;Frits Abildgaard;Mary R. Starich

  • Evaluation of Cloth Masks and Modified Procedure Masks as Personal Protective Equipment for the Public During the COVID-19 Pandemic.

    Phillip W Clapp;Emily E Sickbert-Bennett;James M Samet;Jon Berntsen

  • Filtration Efficiency of Hospital Face Mask Alternatives Available for Use During the COVID-19 Pandemic.

    Emily E. Sickbert-Bennett;James M. Samet;Phillip W. Clapp;Hao Chen

  • The calcium-binding protein S100B down-regulates p53 and apoptosis in malignant melanoma.

    Jing Lin;Qingyuan Yang;Paul T. Wilder;Paul T. Wilder

  • S100A1 and calmodulin compete for the same binding site on ryanodine receptor.

    Nathan T. Wright;Benjamin L. Prosser;Kristen M. Varney;Danna B. Zimmer

  • Structure of the STRA6 receptor for retinol uptake

    Yunting Chen;Oliver B. Clarke;Jonathan Kim;Sean Stowe

  • The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).

    Alexander C. Drohat;Nico Tjandra;Donna M. Baldisseri;David J. Weber

  • Protein Farnesyltransferase: Structure and Implications for Substrate Binding

    Pete Dunten;Ursula Kammlott;Robert Crowther;David Weber

Frequent Co-Authors

Alexander D. MacKerell
Alexander D. MacKerell University of Maryland, Baltimore
Albert S. Mildvan
Albert S. Mildvan Johns Hopkins University
Martin F. Schneider
Martin F. Schneider University of Maryland, Baltimore
Mordecai P. Blaustein
Mordecai P. Blaustein University of Maryland, Baltimore
Lee G. Pedersen
Lee G. Pedersen University of North Carolina at Chapel Hill
Frank L. Margolis
Frank L. Margolis University of Maryland, Baltimore
Steven C. Almo
Steven C. Almo Albert Einstein College of Medicine
Michael Brenowitz
Michael Brenowitz Albert Einstein College of Medicine
Jeffrey D. Hasday
Jeffrey D. Hasday University of Maryland, Baltimore
Jacques Baudier
Jacques Baudier Aix-Marseille University

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