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Biology and Biochemistry

D-Index
109
Citations
50712
World Ranking
993
National Ranking
605

Overview

H. Jane Dyson is affiliated with the Scripps Research Institute in the United States. Their research spans the fields of Biochemistry, Genetics, and Molecular Biology, with significant contributions across several subfields including Molecular Biology, Cell Biology, Physiology, Cancer Research, and Oncology.

The scientist's work addresses several main topics including:

  • Protein Structure and Dynamics
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Cellular transport and secretion
  • Monoclonal and Polyclonal Antibodies Research
  • RNA Research and Splicing
  • Enzyme Structure and Function
  • Cancer-related Molecular Pathways

H. Jane Dyson has contributed to a variety of recent papers, demonstrating focused research interests in protein dynamics and intrinsically disordered proteins. Notable publications include:

  • NMR illuminates intrinsic disorder, 2021, Current Opinion in Structural Biology
  • Vital for Viruses: Intrinsically Disordered Proteins, 2023, Journal of Molecular Biology

Other recent relevant papers in the broader collaborative network include works by coauthors such as Xun Sun and James A. Ferguson, covering subjects like phosphorylation-dependent regulation of p53 and thermodynamic stability of transthyretin variants.

Frequent collaborators in their research include:

  • Peter E. Wright
  • Xun Sun
  • James A. Ferguson
  • Robyn L. Stanfield
  • Maria A. Martinez-Yamout

The scholar has published extensively in several scientific journals and venues, with multiple papers appearing in:

  • Faculty Opinions - Post-Publication Peer Review of the Biomedical Literature
  • Biochemistry
  • Biophysical Journal
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Biopolymers

Best Publications

  • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

    Peter E Wright;H.Jane Dyson

  • Intrinsically disordered proteins in cellular signalling and regulation.

    Peter E. Wright;H. Jane Dyson

  • 1H, 13C and 15N chemical shift referencing in biomolecular NMR

    D S Wishart;C G Bigam;J Yao;F Abildgaard

  • Coupling of folding and binding for unstructured proteins

    H.Jane Dyson;Peter E Wright

  • Mechanism of coupled folding and binding of an intrinsically disordered protein

    Kenji Sugase;H. Jane Dyson;Peter E. Wright

  • Linking Folding and Binding

    Peter E Wright;H Jane Dyson

  • The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

    David D. Boehr;Dan McElheny;H. Jane Dyson;Peter E. Wright

  • Folding of immunogenic peptide fragments of proteins in water solution: I. Sequence requirements for the formation of a reverse turn

    Dyson Hj;Rance M;Houghten Ra;Lerner Ra

  • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.

    Ishwar Radhakrishnan;Gabriela C Pérez-Alvarado;David Parker;H.Jane Dyson

  • Unfolded proteins and protein folding studied by NMR.

    H. Jane Dyson;Peter E. Wright

  • Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.

    Donne Dg;Viles Jh;Groth D;Mehlhorn I

  • Sequence-dependent correction of random coil NMR chemical shifts.

    S Schwarzinger;G J Kroon;T R Foss;J Chung

  • COPPER BINDING TO THE PRION PROTEIN : STRUCTURAL IMPLICATIONS OF FOUR IDENTICAL COOPERATIVE BINDING SITES

    John H. Viles;Fred E. Cohen;Stanley B. Prusiner;David B. Goodin

  • ‘Random coil’ 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG

    Gene Merutka;H. Jane Dyson;Peter E. Wright

  • Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding.

    Wright Pe;Dyson Hj;Lerner Ra

  • Structure, Dynamics, and Catalytic Function of Dihydrofolate Reductase

    Jason R Schnell;H Jane Dyson;Peter E Wright

  • An NMR perspective on enzyme dynamics.

    David D. Boehr;H. Jane Dyson;Peter E. Wright

  • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin.

    H.Jane Dyson;James R. Sayre;Gene Merutka;Hang-Cheol Shin

  • A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

    Gira Bhabha;Jeeyeon Lee;Damian C. Ekiert;Jongsik Gam

  • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding.

    David Eliezer;Jian Yao;H. Jane Dyson;Peter E. Wright

Frequent Co-Authors

Peter E. Wright
Peter E. Wright Scripps Research Institute
Elizabeth A. Komives
Elizabeth A. Komives University of California, San Diego
Jeffery W. Kelly
Jeffery W. Kelly Scripps Research Institute
Robyn L. Stanfield
Robyn L. Stanfield Scripps Research Institute
Ian A. Wilson
Ian A. Wilson Scripps Research Institute
David A. Case
David A. Case Rutgers, The State University of New Jersey
Stephen J. Benkovic
Stephen J. Benkovic Pennsylvania State University
David Eliezer
David Eliezer Cornell University
Julie D. Forman-Kay
Julie D. Forman-Kay University of Toronto
Vladimir N. Uversky
Vladimir N. Uversky University of South Florida

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