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Molecular Biology

D-Index
55
Citations
20124
World Ranking
2243
National Ranking
178

Overview

Neil Q. McDonald is affiliated with The Francis Crick Institute in the United Kingdom. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology, as well as Medicine. Specific subfields of study include Molecular Biology, Cell Biology, Genetics, Oncology, and Cellular and Molecular Neuroscience.

The scientist's work covers a range of topics, notably:

  • Cellular transport and secretion
  • Protein Kinase Regulation and GTPase Signaling
  • Microtubule and mitosis dynamics
  • Ubiquitin and proteasome pathways
  • DNA Repair Mechanisms
  • Nerve injury and regeneration
  • Signaling Pathways in Disease

Neil Q. McDonald has collaborated frequently with various researchers, including:

  • David C. Briggs
  • Mathias Cobbaut
  • Peter J. Parker
  • Christopher Earl

Their recent published papers demonstrate contributions to multiple areas in molecular and cellular biology, including cancer signaling pathways and DNA repair mechanisms. Selected recent publications include:

  • Equivocal, explicit and emergent actions of PKC isoforms in cancer, 2020, Nature Reviews. Cancer
  • Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation, 2020, Nature Communications
  • Activation of the receptor tyrosine kinase RET improves long-term hematopoietic stem cell outgrowth and potency, 2020, Blood
  • Bioisosteric Discovery of NPA101.3, a Second-Generation RET/VEGFR2 Inhibitor Optimized for Single-Agent Polypharmacology, 2020, Journal of Medicinal Chemistry
  • A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell division, 2021, Nature Communications

The venues that have published Neil Q. McDonald's work most frequently include:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Journal of Medicinal Chemistry
  • Biochemical Journal
  • The EMBO Journal

Best Publications

  • Intratumor heterogeneity and branched evolution revealed by multiregion sequencing.

    Marco Gerlinger;Andrew J. Rowan;Stuart Horswell;James Larkin

  • A structural superfamily of growth factors containing a cystine knot motif.

    Neil Q. McDonald;Wayne A. Hendrickson

  • New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor

    N.Q McDonald;R Lapatto;J Murray-Rust;J Gunning

  • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1

    Hélène Plun-Favreau;Kristina Klupsch;Nicoleta Moisoi;Sonia Gandhi

  • Disruption of methylarginine metabolism impairs vascular homeostasis

    James M. Leiper;Manasi Nandi;Belen Torondel;Judith Murray-Rust;Judith Murray-Rust

  • Identification of FAAP24, a Fanconi Anemia Core Complex Protein that Interacts with FANCM

    Alberto Ciccia;Chen Ling;Rachel Coulthard;Zhijiang Yan

  • S-nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: Further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase

    James Leiper;Judith Murray-Rust;Neil McDonald;Patrick Vallance

  • Structure and Chemical Inhibition of the Ret Tyrosine Kinase Domain.

    Phillip P. Knowles;Judith Murray-Rust;Svend Kjær;Svend Kjær;Rizaldy P. Scott

  • Structural and Functional Relationships of the XPF/MUS81 Family of Proteins

    Alberto Ciccia;Neil McDonald;Stephen C West

  • Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase.

    Judith Murray-Rust;James Leiper;Mark McAlister;John Phelan

  • Epidermal growth factor binding induces a conformational change in the external domain of its receptor.

    C. Greenfield;I. Hiles;M.D. Waterfield;M. Federwisch

  • The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition

    Giuseppe Nicastro;Rajesh P. Menon;Laura Masino;Philip P. Knowles

  • A heterozygous effect for PINK1 mutations in Parkinson's disease?

    Patrick M Abou-Sleiman;Miratul M K Muqit;Neil Q McDonald;Yan Xiang Yang

  • Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing.

    N.Q. McDonald;N. Panayotatos;W.A. Hendrickson

  • The Dual Mechanism of Separase Regulation by Securin

    Nadine C.D Hornig;Philip P Knowles;Neil Q McDonald;Neil Q McDonald;Frank Uhlmann

  • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation.

    Albert E. Stewart;Stephen Dowd;Stephen M. Keyse;Neil Q. McDonald

  • A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN).

    Erika Rosivatz;Jonathan G. Matthews;Neil Q. McDonald;Neil Q. McDonald;Xavier Mulet

  • SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases

    William E. Hughes;Rudiger Woscholski;Frank T. Cooke;Robert S. Patrick

  • Crystal structure of the C2 domain from protein kinase C-δ

    H Pappa;J Murray-Rust;LV Dekker;PJ Parker

  • Disruption of methylarginine metabolism impairs vascular homeostasis.

    P Vallance;J Murray-Rust;N McDonald;M Beauvois

Frequent Co-Authors

Peter J. Parker
Peter J. Parker The Francis Crick Institute
Mark Bradley
Mark Bradley University of Edinburgh
Christopher Haslett
Christopher Haslett University of Edinburgh
Tom L. Blundell
Tom L. Blundell University of Cambridge
Richard Treisman
Richard Treisman The Francis Crick Institute
Charles Swanton
Charles Swanton The Francis Crick Institute
Nic Jones
Nic Jones University of Manchester
Michael Way
Michael Way The Francis Crick Institute
Roman K. Thomas
Roman K. Thomas University of Cologne
Carlos F. Ibáñez
Carlos F. Ibáñez Karolinska Institute

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