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Jeremy R. H. Tame

Jeremy R. H. Tame

D-Index & Metrics

Chemistry

D-Index
53
Citations
8040
World Ranking
13272
National Ranking
1010

Biology and Biochemistry

D-Index
55
Citations
8568
World Ranking
15271
National Ranking
1079

Overview

Jeremy R. H. Tame is affiliated with Yokohama City University in Japan. Their research spans primarily within the field of Biochemistry, Genetics and Molecular Biology, with a focus on Molecular Biology, Materials Chemistry, Cellular and Molecular Neuroscience, Infectious Diseases, and Cell Biology.

The scientist's work covers a range of topics including:

  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Hemoglobin structure and function
  • RNA and protein synthesis mechanisms
  • Viral gastroenteritis research and epidemiology
  • Photoreceptor and optogenetics research
  • Polyoxometalates: Synthesis and Applications

The publication record of Jeremy R. H. Tame includes papers published in several prominent venues. Frequent publication outlets include:

  • Nature Communications
  • Biophysical Reviews
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature
  • Journal of Virology

Among recent papers, notable examples are:

  • Structural insights into the HBV receptor and bile acid transporter NTCP, 2022, Nature
  • NMR-guided directed evolution, 2022, Nature
  • Early-stage dynamics of chloride ion-pumping rhodopsin revealed by a femtosecond X-ray laser, 2021, Proceedings of the National Academy of Sciences
  • Structural basis of CXC chemokine receptor 1 ligand binding and activation, 2023, Nature Communications
  • Hemoglobin allostery and pharmacology, 2021, Molecular Aspects of Medicine

Collaborations form a significant part of their research activity. Frequent co-authors include:

  • Arnout Voet
  • Sam-Yong Park
  • Jae-Hyun Park
  • Naito Ishimoto
  • Hiroki Noguchi

Jeremy R. H. Tame's work integrates investigation into protein structure and enzymatic function, often combining approaches from molecular biology and chemistry. Research outputs reflect a consistent engagement with both fundamental biochemical mechanisms and applications related to infectious diseases and cellular functions.

Best Publications

  • The structural basis for an essential subunit interaction in influenza virus RNA polymerase

    Eiji Obayashi;Hisashi Yoshida;Fumihiro Kawai;Naoya Shibayama

  • 1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms.

    Sam-Yong Park;Takeshi Yokoyama;Naoya Shibayama;Yoshitsugu Shiro

  • The role of the distal histidine in myoglobin and haemoglobin

    John S. Olson;Antony J. Mathews;Ronald J. Rohlfs;Barry A. Springer

  • The structural basis of sequence-independent peptide binding by OppA protein

    Jeremy R. H. Tame;Garib N. Murshudov;Eleanor J. Dodson;Teresa K. Neil

  • Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymerase

    Kanako Sugiyama;Eiji Obayashi;Atsushi Kawaguchi;Yukari Suzuki

  • Crystal structure of T state haemoglobin with oxygen bound at all four haems.

    Massimo Paoli;Robert Liddington;Jeremy Tame;Anthony Wilkinson

  • Crystallographic and calorimetric analysis of peptide binding to OppA protein.

    S.H. Sleigh;P.R. Seavers;A.J. Wilkinson;J.E. Ladbury

  • Crystal Structure of Hemoglobin Protease, a Heme Binding Autotransporter Protein from Pathogenic Escherichia coli

    Ben R. Otto;Robert Sijbrandi;Joen Luirink;Bauke Oudega

  • Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering.

    Timm-H. Jessen;Roy E. Weber;Giulio Fermi;Jeremy Tame

  • The role of water in sequence-independent ligand binding by an oligopeptide transporter protein.

    J. R H Tame;S. H. Sleigh;A. J. Wilkinson;John Edward Simon Durham Ladbury

  • SCORING FUNCTIONS : A VIEW FROM THE BENCH

    Jeremy R.H. Tame

  • Crystal structure of elongation factor P from Thermus thermophilus HB8

    Kyoko Hanawa-Suetsugu;Shun-ichi Sekine;Hiroaki Sakai;Chie Hori-Takemoto

  • Pharmacophore modeling: advances, limitations, and current utility in drug discovery

    Xiaoyu Qing;Xiao Yin Lee;Joren De Raeymaecker;Jeremy Rh Tame

  • The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin.

    A J Mathews;R J Rohlfs;J S Olson;J Tame

  • Computational design of a self-assembling symmetrical β-propeller protein

    Arnout R. D. Voet;Hiroki Noguchi;Christine Addy;David Simoncini

  • Structural insights into the HBV receptor and bile acid transporter NTCP

    Unknown

  • Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine.

    Sara H. Sleigh;Jeremy R. H. Tame;Eleanor J. Dodson;Anthony J. Wilkinson

  • The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands

    Jeremy Rh Tame;Eleanor J Dodson;Garib Murshudov;Christopher F Higgins

  • Limited tolerance towards folded elements during secretion of the autotransporter Hbp.

    Wouter S P Jong;Corinne M ten Hagen-Jongman;Tanneke den Blaauwen;Dirk Jan Slotboom

  • Mutant hemoglobins (alpha 119-Ala and beta 55-Ser): functions related to high-altitude respiration in geese.

    R. E. Weber;T. H. Jessen;H. Malte;J. Tame

  • Substitutions in woolly mammoth hemoglobin confer biochemical properties adaptive for cold tolerance

    Kevin L Campbell;Jason E E Roberts;Laura N Watson;Jörg Stetefeld

Frequent Co-Authors

Seiki Kuramitsu
Seiki Kuramitsu Osaka University
Mikako Shirouzu
Mikako Shirouzu RIKEN Center for Biosystems Dynamics Research
Takaho Terada
Takaho Terada University of Tokyo
Anthony J. Wilkinson
Anthony J. Wilkinson University of York
Kiyoshi Nagai
Kiyoshi Nagai MRC Laboratory of Molecular Biology
Ichiro Yamashita
Ichiro Yamashita Osaka University
Joen Luirink
Joen Luirink Vrije Universiteit Amsterdam
Eleanor J. Dodson
Eleanor J. Dodson University of York

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