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Biology and Biochemistry

D-Index
72
Citations
18945
World Ranking
6289
National Ranking
482

Overview

Francis A. Barr is affiliated with the University of Oxford in the United Kingdom. Their research primarily focuses on Biochemistry, Genetics, and Molecular Biology, with significant contributions in Medicine. Subfields of study include Molecular Biology, Cell Biology, Pulmonary and Respiratory Medicine, Oncology, and Plant Science.

The main topics explored in their work are:

  • Microtubule and mitosis dynamics
  • Cellular transport and secretion
  • Photosynthetic Processes and Mechanisms
  • Genomics and Chromatin Dynamics
  • Amino Acid Enzymes and Metabolism
  • Cancer-related Molecular Pathways
  • Ubiquitin and proteasome pathways

Francis A. Barr has published numerous scientific papers, contributing to various peer-reviewed journals. Recent publications include:

  • "Molecular basis for KDEL-mediated retrieval of escaped ER-resident proteins - SWEET talking the COPs" (2020) in Journal of Cell Science
  • "Molecular basis of MKLP2-dependent Aurora B transport from chromatin to the anaphase central spindle" (2020) in The Journal of Cell Biology
  • "PP1 promotes cyclin B destruction and the metaphase-anaphase transition by dephosphorylating CDC20" (2020) in Molecular Biology of the Cell
  • "Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit" (2020) in eLife
  • "A signal capture and proofreading mechanism for the KDEL-receptor explains selectivity and dynamic range in ER retrieval" (2021) in eLife

The scientist frequently collaborates with other researchers. Notable co-authors include Tomoaki Sobajima, Luke J. Fulcher, Caleb Batley, Ulrike Grüneberg, and Simon Newstead.

Their work has appeared often in publication venues such as bioRxiv (Cold Spring Harbor Laboratory), Revue des Maladies Respiratoires Actualités, Journal of Cell Science, The Journal of Cell Biology, and eLife.

Best Publications

  • Polo-like kinases and the orchestration of cell division.

    Francis A. Barr;Herman H. W. Silljé;Erich A. Nigg

  • Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A–C

    Chieh Hsu;Yuichi Morohashi;Shin-ichiro Yoshimura;Natalia Manrique-Hoyos

  • Cytokinesis: placing and making the final cut.

    Francis A. Barr;Ulrike Gruneberg

  • Rab GEFs and GAPs.

    Francis Barr;David G Lambright

  • GRASP65, a Protein Involved in the Stacking of Golgi Cisternae

    Francis A Barr;Magda Puype;Joël Vandekerckhove;Graham Warren

  • Functional dissection of Rab GTPases involved in primary cilium formation

    Shin-ichiro Yoshimura;Johannes Egerer;Evelyn Fuchs;Alexander K. Haas

  • Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis

    Riidiger Neef;Christian Preisinger;Josephine Sutcliffe;Robert Kopajtich

  • Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2

    Ulrike Gruneberg;Rüdiger Neef;Reiko Honda;Erich A. Nigg

  • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system

    James Shorter;Rose Watson;Maria‐Eleni Giannakou;Mairi Clarke

  • Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors

    Shin-ichiro Yoshimura;Andreas Gerondopoulos;Andrea Linford;Daniel J. Rigden

  • TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes

    Andrea Longatti;Christopher A. Lamb;Minoo Razi;Shin-ichiro Yoshimura

  • BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor.

    Andreas Gerondopoulos;Lars Langemeyer;Jin-Rui Liang;Andrea Linford

  • Golgins in the structure and dynamics of the Golgi apparatus.

    Francis A Barr;Benjamin Short

  • KIF14 and citron kinase act together to promote efficient cytokinesis

    Ulrike Gruneberg;Rüdiger Neef;Xiuling Li;Eunice H.Y. Chan

  • Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1

    Rüdiger Neef;Ulrike Gruneberg;Robert Kopajtich;Xiuling Li

  • Rab GTPases and membrane identity: Causal or inconsequential?

    Francis A. Barr

  • YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ

    Christian Preisinger;Benjamin Short;Veerle De Corte;Erik Bruyneel

  • A GTPase-activating protein controls Rab5 function in endocytic trafficking.

    Alexander K Haas;Evelyn Fuchs;Robert Kopajtich;Francis A Barr

  • Golgins and GTPases, giving identity and structure to the Golgi apparatus

    Benjamin Short;Alexander Haas;Francis A. Barr

  • Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae

    Francis A. Barr;Nobuhiro Nakamura;Graham Warren

Frequent Co-Authors

Erich A. Nigg
Erich A. Nigg University of Basel
Wieland B. Huttner
Wieland B. Huttner Max Planck Society
Graham Warren
Graham Warren Medical University of Vienna
Shabaz Mohammed
Shabaz Mohammed University of Oxford
Suzanne R. Pfeffer
Suzanne R. Pfeffer Stanford University
David G. Lambright
David G. Lambright University of Massachusetts Chan Medical School
Sharon A. Tooze
Sharon A. Tooze The Francis Crick Institute
Paul Gissen
Paul Gissen University College London
Manju A. Kurian
Manju A. Kurian University College London
Eamonn R. Maher
Eamonn R. Maher University of Cambridge

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