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Biology and Biochemistry

D-Index
73
Citations
16419
World Ranking
6032
National Ranking
463

Overview

Ian M. Fearnley is affiliated with the University of Cambridge in the United Kingdom. Their research primarily focuses on biochemistry, genetics, and molecular biology, with particular emphasis in subfields such as molecular biology, clinical biochemistry, biochemistry, spectroscopy, and materials chemistry.

The main topics covered in their work include:

  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Metabolism and Genetic Disorders
  • Photosynthetic Processes and Mechanisms
  • RNA and protein synthesis mechanisms
  • Amino Acid Enzymes and Metabolism
  • Biochemical and Molecular Research

Fearnley's recent papers cover a range of subjects within mitochondrial biology and bioenergetics:

  • Respiratory supercomplexes act as a platform for complex III -mediated maturation of human mitochondrial complexes I and IV, 2020, The EMBO Journal
  • Two independent respiratory chains adapt OXPHOS performance to glycolytic switch, 2022, Cell Metabolism
  • Loss of COX4I1 Leads to Combined Respiratory Chain Deficiency and Impaired Mitochondrial Protein Synthesis, 2021, Cells
  • ND3 Cys39 in complex I is exposed during mitochondrial respiration, 2021, Cell chemical biology
  • TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I, 2021, Proceedings of the National Academy of Sciences

Throughout their career, Fearnley has frequently published in the following venues:

  • Biochimica et Biophysica Acta (BBA) - Bioenergetics
  • Proceedings of the National Academy of Sciences
  • bioRxiv (Cold Spring Harbor Laboratory)
  • The EMBO Journal
  • Cell Metabolism

The scientist collaborates regularly with a core group of coauthors, including:

  • Shujing Ding
  • Massimo Zeviani
  • Erika Fernández-Vizarra
  • John E. Walker
  • Joe Carroll

Best Publications

  • p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

    Derek P Narendra;Lesley A Kane;David N Hauser;Ian M Fearnley

  • Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I

    Edward T Chouchani;Carmen Methner;Sergiy M Nadtochiy;Angela Logan

  • Bovine complex I is a complex of 45 different subunits.

    Joe Carroll;Ian M. Fearnley;J. Mark Skehel;Richard J. Shannon

  • Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria

    J.E. Walker;I.M. Fearnley;B.W. Gibson

  • The nuclear encoded subunits of complex I from bovine heart mitochondria.

    Judy Hirst;Joe Carroll;Ian M. Fearnley;Richard J. Shannon

  • Analysis of the Subunit Composition of Complex I from Bovine Heart Mitochondria

    Joe Carroll;Ian M. Fearnley;Richard J. Shannon;Judy Hirst

  • Mitochondrial ATP synthase subunit c storage in the ceroid-lipofuscinoses (Batten disease).

    David N. Palmer;Ian M. Fearnley;John E. Walker;Nicholas A. Hall

  • Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins

    Ian M. Fearnley;John E. Walker

  • Measurement of H2O2 within Living Drosophila during Aging Using a Ratiometric Mass Spectrometry Probe Targeted to the Mitochondrial Matrix

    Helena M. Cochemé;Caroline Quin;Stephen J. McQuaker;Filipe Cabreiro

  • GRIM-19, a Cell Death Regulatory Gene Product, Is a Subunit of Bovine Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I)

    Ian M. Fearnley;Joe Carroll;Richard J. Shannon;Michael J. Runswick

  • Sequences of 20 subunits of NADH : ubiquinone oxidoreductase from bovine heart mitochondria : application of a novel strategy for sequencing proteins using the polymerase chain reaction

    Walker Je;Arizmendi Jm;Dupuis A;Fearnley Im

  • Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase

    Jiuya He;Holly C. Ford;Joe Carroll;Shujing Ding

  • The AAA+ protein ATAD3 has displacement loop binding properties and is involved in mitochondrial nucleoid organization

    Jiuya He;Chih-Chieh Mao;Aurelio Reyes;Hiroshi Sembongi

  • On the structure of the stator of the mitochondrial ATP synthase.

    Veronica Kane Dickson;Jocelyn A Silvester;Ian M Fearnley;Andrew G W Leslie

  • Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage.

    Thomas R. Hurd;Raquel Requejo;Aleksandra Filipovska;Stephanie Brown

  • Consequences of long-term oral administration of the mitochondria-targeted antioxidant MitoQ to wild-type mice

    Sergio Rodriguez-Cuenca;Helena M. Cochemé;Helena M. Cochemé;Angela Logan;Irina Abakumova

  • F0 Membrane Domain of ATP Synthase from Bovine Heart Mitochondria: Purification, Subunit Composition, and Reconstitution with F1-ATPase

    Collinson Ir;Runswick Mj;Buchanan Sk;Fearnley Im

  • Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme.

    Leonid A. Sazanov;Sew Y. Peak-Chew;Ian M. Fearnley;John E. Walker

  • Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase.

    I M Fearnley;J E Walker

  • Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis

    J. He;H. M. Cooper;A. Reyes;M. Di Re

Frequent Co-Authors

John E. Walker
John E. Walker University of Cambridge
Michael J. Runswick
Michael J. Runswick Medical Research Council
Michael P. Murphy
Michael P. Murphy University of Cambridge
Andrew M. James
Andrew M. James MRC Mitochondrial Biology Unit
J. Mark Skehel
J. Mark Skehel MRC Laboratory of Molecular Biology
Judy Hirst
Judy Hirst University of Cambridge
Robin A. J. Smith
Robin A. J. Smith University of Otago
Massimo Zeviani
Massimo Zeviani University of Padua
Linda Partridge
Linda Partridge Max Planck Society
Andrew G. W. Leslie
Andrew G. W. Leslie MRC Laboratory of Molecular Biology

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