D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 54 Citations 9,390 145 World Ranking 7112 National Ranking 2142
Biology and Biochemistry D-index 55 Citations 12,785 122 World Ranking 7432 National Ranking 3390

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • Amino acid

David Cowburn mainly focuses on Biochemistry, Protein structure, Nuclear magnetic resonance spectroscopy, Peptide and Crystallography. His Protein structure research includes themes of Stereochemistry and Cell biology. His study looks at the intersection of Stereochemistry and topics like Binding site with SH2 domain.

David Cowburn combines subjects such as Peptide bond, Structural biology and Biophysics with his study of Nuclear magnetic resonance spectroscopy. David Cowburn has included themes like Molecular biology, PDZ domain, Capsid and Phosphorylation in his Peptide study. In his study, Nuclear Overhauser effect, Pleckstrin homology domain and Antiparallel is strongly linked to Protein secondary structure, which falls under the umbrella field of Crystallography.

His most cited work include:

  • Accurate quantitation of protein expression and site-specific phosphorylation (939 citations)
  • Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. (716 citations)
  • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms (662 citations)

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

His primary areas of study are Biochemistry, Nuclear magnetic resonance spectroscopy, Stereochemistry, Crystallography and Biophysics. His work in Proto-oncogene tyrosine-protein kinase Src, Peptide, SH3 domain, Peptide sequence and Peptide bond are all subfields of Biochemistry research. The Nuclear magnetic resonance spectroscopy study combines topics in areas such as Physical chemistry and Analytical chemistry.

David Cowburn frequently studies issues relating to Chemical shift and Stereochemistry. He has researched Biophysics in several fields, including Protein structure, Protein domain, Binding site and Nuclear pore. Protein structure and Plasma protein binding are frequently intertwined in his study.

He most often published in these fields:

  • Biochemistry (24.90%)
  • Nuclear magnetic resonance spectroscopy (18.58%)
  • Stereochemistry (16.21%)

What were the highlights of his more recent work (between 2015-2021)?

  • Biophysics (13.04%)
  • Nuclear pore (4.35%)
  • Nucleoporin (3.16%)

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

His primary areas of investigation include Biophysics, Nuclear pore, Nucleoporin, Biochemistry and Computational biology. His Nuclear pore study also includes

  • Nuclear transport which connect with Intrinsically disordered proteins,
  • Nucleocytoplasmic Transport together with Binding site, Molecular dynamics, Nanotechnology and Plasma protein binding. Biochemistry is represented through his Proto-oncogene tyrosine-protein kinase Src and Peptide research.

His Peptide study combines topics from a wide range of disciplines, such as DNA, SH2 domain and Denaturation. His biological study spans a wide range of topics, including Protein splicing and Intein. His Protein domain research incorporates elements of Protein structure, Nuclear magnetic resonance spectroscopy, Stereochemistry and C-terminal Src kinase.

Between 2015 and 2021, his most popular works were:

  • Design of a Split Intein with Exceptional Protein Splicing Activity (68 citations)
  • A promiscuous split intein with expanded protein engineering applications (61 citations)
  • Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex (58 citations)

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

  • Gene
  • Enzyme
  • Amino acid

His main research concerns Nuclear pore, Nucleoporin, Biophysics, Intein and RNA splicing. His Nucleoporin research incorporates themes from Membrane, Nanotechnology and Molecular dynamics. His Biophysics research is multidisciplinary, incorporating elements of Protein structure, Nucleocytoplasmic Transport, Protein domain and Binding site.

His research integrates issues of dnaE, Chemical biology, Protein dynamics, Structural biology and A protein in his study of Intein. A protein is a subfield of Biochemistry that David Cowburn explores. His studies in Biochemistry integrate themes in fields like Antibody and Antigen.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Accurate quantitation of protein expression and site-specific phosphorylation

Y. Oda;K. Huang;F. R. Cross;D. Cowburn.
Proceedings of the National Academy of Sciences of the United States of America (1999)

1408 Citations

Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions.

Ke Shuai;Curt M. Horvath;Linda H.Tsai Huang;Sajjad A. Qureshi.
Cell (1994)

1003 Citations

Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms

Gabriel Waksman;Steven E. Shoelson;Nalin Pant;David Cowburn.
Cell (1993)

928 Citations

CRYSTAL-STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

Gabriel Waksman;Dorothea Kominos;Scott C. Robertson;Scott C. Robertson;Nalin Pant.
Nature (1993)

833 Citations

MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING

John Kuriyan;David Cowburn.
Annual Review of Biophysics and Biomolecular Structure (1997)

683 Citations

Solution Structure of the Proapoptotic Molecule BID: A Structural Basis for Apoptotic Agonists and Antagonists

James M. McDonnell;David Fushman;Curt L. Milliman;Stanley J. Korsmeyer.
Cell (1999)

472 Citations

Perspectives on NMR in drug discovery: a technique comes of age

Maurizio Pellecchia;Ivano Bertini;David Cowburn;Claudio Dalvit.
Nature Reviews Drug Discovery (2008)

378 Citations

A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein

Chi Hon Lee;Benjamin Leung;Mark A. Lemmon;Jie Zheng.
The EMBO Journal (1995)

352 Citations

Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk

Xiaodong Wu;Beatrice Knudsen;Stephan M Feller;Jie Zheng.
Structure (1995)

317 Citations

Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies

Rong Xu;Brenda Ayers;David Cowburn;Tom W. Muir.
Proceedings of the National Academy of Sciences of the United States of America (1999)

306 Citations

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