Publications by authors named "Richard J Youle"

100Publications

Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective.

Cell Death Differ 2020 Nov 18. Epub 2020 Nov 18.

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, 20892, USA.

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http://dx.doi.org/10.1038/s41418-020-00667-xDOI Listing
November 2020

Loss of TAX1BP1-Directed Autophagy Results in Protein Aggregate Accumulation in the Brain.

Mol Cell 2020 Nov 12. Epub 2020 Nov 12.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA; Program in Neuroscience and Cognitive Science, University of Maryland, College Park, MD 20742, USA. Electronic address:

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http://dx.doi.org/10.1016/j.molcel.2020.10.041DOI Listing
November 2020

STING induces LC3B lipidation onto single-membrane vesicles via the V-ATPase and ATG16L1-WD40 domain.

J Cell Biol 2020 Dec;219(12)

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD.

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http://dx.doi.org/10.1083/jcb.202009128DOI Listing
December 2020

Mitochondrial Quality Control and Restraining Innate Immunity.

Annu Rev Cell Dev Biol 2020 Oct;36:265-289

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA; email:

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http://dx.doi.org/10.1146/annurev-cellbio-021820-101354DOI Listing
October 2020

Two different axes CALCOCO2-RB1CC1 and OPTN-ATG9A initiate PRKN-mediated mitophagy.

Autophagy 2020 Nov 7;16(11):2105-2107. Epub 2020 Sep 7.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health , Bethesda, MD, USA.

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http://dx.doi.org/10.1080/15548627.2020.1815457DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7595642PMC
November 2020

ULK complex organization in autophagy by a C-shaped FIP200 N-terminal domain dimer.

J Cell Biol 2020 Jul;219(7)

Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA.

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http://dx.doi.org/10.1083/jcb.201911047DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337493PMC
July 2020

PINK1/Parkin Influences Cell Cycle by Sequestering TBK1 at Damaged Mitochondria, Inhibiting Mitosis.

Cell Rep 2019 10;29(1):225-235.e5

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD 20892, USA; School of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA. Electronic address:

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http://dx.doi.org/10.1016/j.celrep.2019.08.085DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6880866PMC
October 2019

Mitochondria-Striking a balance between host and endosymbiont.

Authors:
Richard J Youle

Science 2019 08;365(6454)

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1126/science.aaw9855DOI Listing
August 2019

Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy.

Mol Cell 2019 04 7;74(2):347-362.e6. Epub 2019 Mar 7.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.molcel.2019.02.010DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6642318PMC
April 2019

Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1.

Mol Cell 2019 03 4;73(5):1028-1043.e5. Epub 2019 Feb 4.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.molcel.2019.01.002DOI Listing
March 2019

Parkin and PINK1 mitigate STING-induced inflammation.

Nature 2018 09 22;561(7722):258-262. Epub 2018 Aug 22.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.

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http://www.nature.com/articles/s41586-018-0448-9
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http://dx.doi.org/10.1038/s41586-018-0448-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7362342PMC
September 2018

Active state of Parkin.

Nat Struct Mol Biol 2018 08;25(8):644-646

National Institutes of Health, Bethesda, MD, USA.

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http://dx.doi.org/10.1038/s41594-018-0101-1DOI Listing
August 2018

Parkin mediates mitophagy during beige-to-white fat conversion.

Sci Signal 2018 04 24;11(527). Epub 2018 Apr 24.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1126/scisignal.aat1082DOI Listing
April 2018

Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance.

Curr Biol 2018 02;28(4):R170-R185

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.cub.2018.01.004DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7255410PMC
February 2018

Endosomal Rab cycles regulate Parkin-mediated mitophagy.

Elife 2018 01 23;7. Epub 2018 Jan 23.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.

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http://dx.doi.org/10.7554/eLife.31326DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5780041PMC
January 2018

PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol.

BMC Biol 2018 01 10;16(1). Epub 2018 Jan 10.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, 20892, USA.

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http://dx.doi.org/10.1186/s12915-017-0470-7DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795276PMC
January 2018

Vps13D Encodes a Ubiquitin-Binding Protein that Is Required for the Regulation of Mitochondrial Size and Clearance.

Curr Biol 2018 01 4;28(2):287-295.e6. Epub 2018 Jan 4.

Department of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address:

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http://dx.doi.org/10.1016/j.cub.2017.11.064DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5787036PMC
January 2018

Mitochondrial fission facilitates the selective mitophagy of protein aggregates.

J Cell Biol 2017 10 11;216(10):3231-3247. Epub 2017 Sep 11.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD

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http://dx.doi.org/10.1083/jcb.201612106DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5626535PMC
October 2017

Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria.

Proc Natl Acad Sci U S A 2016 Apr 30;113(15):4039-44. Epub 2016 Mar 30.

Institute of Biochemistry II, Goethe University School of Medicine, 60590 Frankfurt, Germany; Buchmann Institute for Molecular Life Sciences, Goethe University, 60438 Frankfurt, Germany; Institute of Immunology, School of Medicine, University of Split, 21 000 Split, Croatia

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http://dx.doi.org/10.1073/pnas.1523926113DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4839414PMC
April 2016

The Mitochondrial Basis of Aging.

Mol Cell 2016 Mar;61(5):654-666

Center for Molecular Medicine, National Heart, Lung and Blood Institute, NIH, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.molcel.2016.01.028DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4779179PMC
March 2016

Characterization of the membrane-inserted C-terminus of cytoprotective BCL-XL.

Protein Expr Purif 2016 06 23;122:56-63. Epub 2016 Feb 23.

Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address:

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http://dx.doi.org/10.1016/j.pep.2016.02.010DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4842142PMC
June 2016

The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy.

Nature 2015 Aug 12;524(7565):309-314. Epub 2015 Aug 12.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1038/nature14893DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5018156PMC
August 2015

MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5.

J Cell Biol 2015 Aug;210(3):435-50

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892

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http://dx.doi.org/10.1083/jcb.201501002DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4523611PMC
August 2015

Neurolastin, a Dynamin Family GTPase, Regulates Excitatory Synapses and Spine Density.

Cell Rep 2015 Aug 23;12(5):743-51. Epub 2015 Jul 23.

Receptor Biology Section, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.celrep.2015.06.064DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4567839PMC
August 2015

Endogenous Parkin Preserves Dopaminergic Substantia Nigral Neurons following Mitochondrial DNA Mutagenic Stress.

Neuron 2015 Jul;87(2):371-81

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.neuron.2015.06.034DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4803114PMC
July 2015

Conformation of BCL-XL upon Membrane Integration.

J Mol Biol 2015 Jul 27;427(13):2262-70. Epub 2015 Feb 27.

Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address:

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http://dx.doi.org/10.1016/j.jmb.2015.02.019DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4457587PMC
July 2015

Chemogenomic profiling of endogenous PARK2 expression using a genome-edited coincidence reporter.

ACS Chem Biol 2015 May 26;10(5):1188-97. Epub 2015 Feb 26.

‡National Center for Advancing Translational Sciences, Rockville, Maryland 20850, United States.

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http://dx.doi.org/10.1021/cb5010417DOI Listing
May 2015

The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease.

Neuron 2015 Jan;85(2):257-73

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke (NINDS), NIH, Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.neuron.2014.12.007DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764997PMC
January 2015

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.

J Cell Biol 2014 Apr 21;205(2):143-53. Epub 2014 Apr 21.

Biochemistry Section, Surgical Neurology Branch, and 2 Protein/Peptide Sequencing Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20824.

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http://dx.doi.org/10.1083/jcb.201402104DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003245PMC
April 2014

Self and nonself: how autophagy targets mitochondria and bacteria.

Cell Host Microbe 2014 Apr;15(4):403-11

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health Bethesda, MD 20892, USA. Electronic address:

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http://dx.doi.org/10.1016/j.chom.2014.03.012DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4238923PMC
April 2014

Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy.

Elife 2014 Feb 25;3:e01612. Epub 2014 Feb 25.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3930140PMC
http://dx.doi.org/10.7554/eLife.01612DOI Listing
February 2014

Mitochondrial disease: mtDNA and protein segregation mysteries in iPSCs.

Curr Biol 2013 Dec;23(23):R1052-4

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1016/j.cub.2013.10.048DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4746723PMC
December 2013

High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.

Nature 2013 Dec 24;504(7479):291-5. Epub 2013 Nov 24.

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://dx.doi.org/10.1038/nature12748DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5841086PMC
December 2013

Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy.

Nat Commun 2013 ;4:2789

1] The Institute for Biochemistry, Food Science, and Nutrition, Robert H. Smith Faculty of Agriculture, Food and Environment, Hebrew University of Jerusalem, P.O. Box 12, Rehovot, Israel 76100 [2] Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, Porter Neuroscience Research Center Building 35, Room 2C-917 35 Convent Drive, Bethesda, Maryland 20892-3704, USA.

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http://dx.doi.org/10.1038/ncomms3789DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909740PMC
July 2014

Mutations in Fis1 disrupt orderly disposal of defective mitochondria.

Mol Biol Cell 2014 Jan 6;25(1):145-59. Epub 2013 Nov 6.

Department of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095 Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892 Department of Neurology, Juntendo University School of Medicine, Tokyo 113-8421, Japan.

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http://dx.doi.org/10.1091/mbc.E13-09-0525DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873885PMC
January 2014

The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria.

Autophagy 2013 Nov 5;9(11):1750-7. Epub 2013 Sep 5.

Biochemistry Section; Surgical Neurology Branch; National Institute of Neurological Disorders and Stroke; National Institutes of Health; Bethesda, MD USA.

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http://www.tandfonline.com/doi/abs/10.4161/auto.26122
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4028334PMC
http://dx.doi.org/10.4161/auto.26122DOI Listing
November 2013

PINK1 is degraded through the N-end rule pathway.

Autophagy 2013 Nov 17;9(11):1758-69. Epub 2013 Apr 17.

Biochemistry Section; Surgical Neurology Branch; National Institute of Neurological Disorders and Stroke; National Institutes of Health; Bethesda, MD USA.

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http://dx.doi.org/10.4161/auto.24633DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4028335PMC
November 2013

Atypical mitochondrial fission upon bacterial infection.

Proc Natl Acad Sci U S A 2013 Oct 16;110(40):16003-8. Epub 2013 Sep 16.

Unité des Interactions Bactéries-Cellules, Institut Pasteur, 75015 Paris, France.

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http://dx.doi.org/10.1073/pnas.1315784110DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791707PMC
October 2013

Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy.

Mol Cell Biol 2013 Sep 22;33(18):3675-88. Epub 2013 Jul 22.

Biochemistry Section, National Institute for Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, USA.

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http://dx.doi.org/10.1128/MCB.00079-13DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753860PMC
September 2013

Make or break for mitochondria.

Elife 2013 May 14;2:e00804. Epub 2013 May 14.

is at the Medical Research Council Mitochondrial Biology Unit , Cambridge , United Kingdom and at the National Institute of Neurological Disorders and Stroke , National Institutes of Health , Bethesda , United States

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http://dx.doi.org/10.7554/eLife.00804DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654434PMC
May 2013

Sequestration and autophagy of mitochondria do not cut proteins across the board.

Proc Natl Acad Sci U S A 2013 Apr 8;110(16):6252-3. Epub 2013 Apr 8.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1073/pnas.1303921110DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3631660PMC
April 2013

PINK1 rendered temperature sensitive by disease-associated and engineered mutations.

Hum Mol Genet 2013 Jul 3;22(13):2572-89. Epub 2013 Mar 3.

Medical Research Council Mitochondrial Biology Unit, Hills Road, Cambridge, UK.

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http://dx.doi.org/10.1093/hmg/ddt106DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3674799PMC
July 2013

PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding.

J Cell Biol 2013 Jan 14;200(2):163-72. Epub 2013 Jan 14.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1083/jcb.201210111DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3549971PMC
January 2013

Balancing cell growth and death.

Curr Opin Cell Biol 2012 Dec 13;24(6):802-3. Epub 2012 Dec 13.

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http://dx.doi.org/10.1016/j.ceb.2012.11.003DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4749036PMC
December 2012

Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA.

Proc Natl Acad Sci U S A 2012 Dec 3;109(51):20901-6. Epub 2012 Dec 3.

Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1073/pnas.1217094110DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3529058PMC
December 2012

Ubiquitin ligase RNF167 regulates AMPA receptor-mediated synaptic transmission.

Proc Natl Acad Sci U S A 2012 Nov 5;109(47):19426-31. Epub 2012 Nov 5.

Receptor Biology Section and Biochemistry Section/Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1073/pnas.1217477109DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3511152PMC
November 2012

Guidelines for the use and interpretation of assays for monitoring autophagy.

Authors:
Daniel J Klionsky Fabio C Abdalla Hagai Abeliovich Robert T Abraham Abraham Acevedo-Arozena Khosrow Adeli Lotta Agholme Maria Agnello Patrizia Agostinis Julio A Aguirre-Ghiso Hyung Jun Ahn Ouardia Ait-Mohamed Slimane Ait-Si-Ali Takahiko Akematsu Shizuo Akira Hesham M Al-Younes Munir A Al-Zeer Matthew L Albert Roger L Albin Javier Alegre-Abarrategui Maria Francesca Aleo Mehrdad Alirezaei Alexandru Almasan Maylin Almonte-Becerril Atsuo Amano Ravi Amaravadi Shoba Amarnath Amal O Amer Nathalie Andrieu-Abadie Vellareddy Anantharam David K Ann Shailendra Anoopkumar-Dukie Hiroshi Aoki Nadezda Apostolova Giuseppe Arancia John P Aris Katsuhiko Asanuma Nana Y O Asare Hisashi Ashida Valerie Askanas David S Askew Patrick Auberger Misuzu Baba Steven K Backues Eric H Baehrecke Ben A Bahr Xue-Yuan Bai Yannick Bailly Robert Baiocchi Giulia Baldini Walter Balduini Andrea Ballabio Bruce A Bamber Edward T W Bampton Gábor Bánhegyi Clinton R Bartholomew Diane C Bassham Robert C Bast Henri Batoko Boon-Huat Bay Isabelle Beau Daniel M Béchet Thomas J Begley Christian Behl Christian Behrends Soumeya Bekri Bryan Bellaire Linda J Bendall Luca Benetti Laura Berliocchi Henri Bernardi Francesca Bernassola Sébastien Besteiro Ingrid Bhatia-Kissova Xiaoning Bi Martine Biard-Piechaczyk Janice S Blum Lawrence H Boise Paolo Bonaldo David L Boone Beat C Bornhauser Karina R Bortoluci Ioannis Bossis Frédéric Bost Jean-Pierre Bourquin Patricia Boya Michaël Boyer-Guittaut Peter V Bozhkov Nathan R Brady Claudio Brancolini Andreas Brech Jay E Brenman Ana Brennand Emery H Bresnick Patrick Brest Dave Bridges Molly L Bristol Paul S Brookes Eric J Brown John H Brumell Nicola Brunetti-Pierri Ulf T Brunk Dennis E Bulman Scott J Bultman Geert Bultynck Lena F Burbulla Wilfried Bursch Jonathan P Butchar Wanda Buzgariu Sergio P Bydlowski Ken Cadwell Monika Cahová Dongsheng Cai Jiyang Cai Qian Cai Bruno Calabretta Javier Calvo-Garrido Nadine Camougrand Michelangelo Campanella Jenny Campos-Salinas Eleonora Candi Lizhi Cao Allan B Caplan Simon R Carding Sandra M Cardoso Jennifer S Carew Cathleen R Carlin Virginie Carmignac Leticia A M Carneiro Serena Carra Rosario A Caruso Giorgio Casari Caty Casas Roberta Castino Eduardo Cebollero Francesco Cecconi Jean Celli Hassan Chaachouay Han-Jung Chae Chee-Yin Chai David C Chan Edmond Y Chan Raymond Chuen-Chung Chang Chi-Ming Che Ching-Chow Chen Guang-Chao Chen Guo-Qiang Chen Min Chen Quan Chen Steve S-L Chen WenLi Chen Xi Chen Xiangmei Chen Xiequn Chen Ye-Guang Chen Yingyu Chen Yongqiang Chen Yu-Jen Chen Zhixiang Chen Alan Cheng Christopher H K Cheng Yan Cheng Heesun Cheong Jae-Ho Cheong Sara Cherry Russ Chess-Williams Zelda H Cheung Eric Chevet Hui-Ling Chiang Roberto Chiarelli Tomoki Chiba Lih-Shen Chin Shih-Hwa Chiou Francis V Chisari Chi Hin Cho Dong-Hyung Cho Augustine M K Choi DooSeok Choi Kyeong Sook Choi Mary E Choi Salem Chouaib Divaker Choubey Vinay Choubey Charleen T Chu Tsung-Hsien Chuang Sheau-Huei Chueh Taehoon Chun Yong-Joon Chwae Mee-Len Chye Roberto Ciarcia Maria R Ciriolo Michael J Clague Robert S B Clark Peter G H Clarke Robert Clarke Patrice Codogno Hilary A Coller María I Colombo Sergio Comincini Maria Condello Fabrizio Condorelli Mark R Cookson Graham H Coombs Isabelle Coppens Ramon Corbalan Pascale Cossart Paola Costelli Safia Costes Ana Coto-Montes Eduardo Couve Fraser P Coxon James M Cregg José L Crespo Marianne J Cronjé Ana Maria Cuervo Joseph J Cullen Mark J Czaja Marcello D'Amelio Arlette Darfeuille-Michaud Lester M Davids Faith E Davies Massimo De Felici John F de Groot Cornelis A M de Haan Luisa De Martino Angelo De Milito Vincenzo De Tata Jayanta Debnath Alexei Degterev Benjamin Dehay Lea M D Delbridge Francesca Demarchi Yi Zhen Deng Jörn Dengjel Paul Dent Donna Denton Vojo Deretic Shyamal D Desai Rodney J Devenish Mario Di Gioacchino Gilbert Di Paolo Chiara Di Pietro Guillermo Díaz-Araya Inés Díaz-Laviada Maria T Diaz-Meco Javier Diaz-Nido Ivan Dikic Savithramma P Dinesh-Kumar Wen-Xing Ding Clark W Distelhorst Abhinav Diwan Mojgan Djavaheri-Mergny Svetlana Dokudovskaya Zheng Dong Frank C Dorsey Victor Dosenko James J Dowling Stephen Doxsey Marlène Dreux Mark E Drew Qiuhong Duan Michel A Duchosal Karen Duff Isabelle Dugail Madeleine Durbeej Michael Duszenko Charles L Edelstein Aimee L Edinger Gustavo Egea Ludwig Eichinger N Tony Eissa Suhendan Ekmekcioglu Wafik S El-Deiry Zvulun Elazar Mohamed Elgendy Lisa M Ellerby Kai Er Eng Anna-Mart Engelbrecht Simone Engelender Jekaterina Erenpreisa Ricardo Escalante Audrey Esclatine Eeva-Liisa Eskelinen Lucile Espert Virginia Espina Huizhou Fan Jia Fan Qi-Wen Fan Zhen Fan Shengyun Fang Yongqi Fang Manolis Fanto Alessandro Fanzani Thomas Farkas Jean-Claude Farré Mathias Faure Marcus Fechheimer Carl G Feng Jian Feng Qili Feng Youji Feng László Fésüs Ralph Feuer Maria E Figueiredo-Pereira Gian Maria Fimia Diane C Fingar Steven Finkbeiner Toren Finkel Kim D Finley Filomena Fiorito Edward A Fisher Paul B Fisher Marc Flajolet Maria L Florez-McClure Salvatore Florio Edward A Fon Francesco Fornai Franco Fortunato Rati Fotedar Daniel H Fowler Howard S Fox Rodrigo Franco Lisa B Frankel Marc Fransen José M Fuentes Juan Fueyo Jun Fujii Kozo Fujisaki Eriko Fujita Mitsunori Fukuda Ruth H Furukawa Matthias Gaestel Philippe Gailly Malgorzata Gajewska Brigitte Galliot Vincent Galy Subramaniam Ganesh Barry Ganetzky Ian G Ganley Fen-Biao Gao George F Gao Jinming Gao Lorena Garcia Guillermo Garcia-Manero Mikel Garcia-Marcos Marjan Garmyn Andrei L Gartel Evelina Gatti Mathias Gautel Thomas R Gawriluk Matthew E Gegg Jiefei Geng Marc Germain Jason E Gestwicki David A Gewirtz Saeid Ghavami Pradipta Ghosh Anna M Giammarioli Alexandra N Giatromanolaki Spencer B Gibson Robert W Gilkerson Michael L Ginger Henry N Ginsberg Jakub Golab Michael S Goligorsky Pierre Golstein Candelaria Gomez-Manzano Ebru Goncu Céline Gongora Claudio D Gonzalez Ramon Gonzalez Cristina González-Estévez Rosa Ana González-Polo Elena Gonzalez-Rey Nikolai V Gorbunov Sharon Gorski Sandro Goruppi Roberta A Gottlieb Devrim Gozuacik Giovanna Elvira Granato Gary D Grant Kim N Green Aleš Gregorc Frédéric Gros Charles Grose Thomas W Grunt Philippe Gual Jun-Lin Guan Kun-Liang Guan Sylvie M Guichard Anna S Gukovskaya Ilya Gukovsky Jan Gunst Asa B Gustafsson Andrew J Halayko Amber N Hale Sandra K Halonen Maho Hamasaki Feng Han Ting Han Michael K Hancock Malene Hansen Hisashi Harada Masaru Harada Stefan E Hardt J Wade Harper Adrian L Harris James Harris Steven D Harris Makoto Hashimoto Jeffrey A Haspel Shin-ichiro Hayashi Lori A Hazelhurst Congcong He You-Wen He Marie-Joseé Hébert Kim A Heidenreich Miep H Helfrich Gudmundur V Helgason Elizabeth P Henske Brian Herman Paul K Herman Claudio Hetz Sabine Hilfiker Joseph A Hill Lynne J Hocking Paul Hofman Thomas G Hofmann Jörg Höhfeld Tessa L Holyoake Ming-Huang Hong David A Hood Gökhan S Hotamisligil Ewout J Houwerzijl Maria Høyer-Hansen Bingren Hu Chien-An A Hu Hong-Ming Hu Ya Hua Canhua Huang Ju Huang Shengbing Huang Wei-Pang Huang Tobias B Huber Won-Ki Huh Tai-Ho Hung Ted R Hupp Gang Min Hur James B Hurley Sabah N A Hussain Patrick J Hussey Jung Jin Hwang Seungmin Hwang Atsuhiro Ichihara Shirin Ilkhanizadeh Ken Inoki Takeshi Into Valentina Iovane Juan L Iovanna Nancy Y Ip Yoshitaka Isaka Hiroyuki Ishida Ciro Isidoro Ken-ichi Isobe Akiko Iwasaki Marta Izquierdo Yotaro Izumi Panu M Jaakkola Marja Jäättelä George R Jackson William T Jackson Bassam Janji Marina Jendrach Ju-Hong Jeon Eui-Bae Jeung Hong Jiang Hongchi Jiang Jean X Jiang Ming Jiang Qing Jiang Xuejun Jiang Xuejun Jiang Alberto Jiménez Meiyan Jin Shengkan Jin Cheol O Joe Terje Johansen Daniel E Johnson Gail V W Johnson Nicola L Jones Bertrand Joseph Suresh K Joseph Annie M Joubert Gábor Juhász Lucienne Juillerat-Jeanneret Chang Hwa Jung Yong-Keun Jung Kai Kaarniranta Allen Kaasik Tomohiro Kabuta Motoni Kadowaki Katarina Kagedal Yoshiaki Kamada Vitaliy O Kaminskyy Harm H Kampinga Hiromitsu Kanamori Chanhee Kang Khong Bee Kang Kwang Il Kang Rui Kang Yoon-A Kang Tomotake Kanki Thirumala-Devi Kanneganti Haruo Kanno Anumantha G Kanthasamy Arthi Kanthasamy Vassiliki Karantza Gur P Kaushal Susmita Kaushik Yoshinori Kawazoe Po-Yuan Ke John H Kehrl Ameeta Kelekar Claus Kerkhoff David H Kessel Hany Khalil Jan A K W Kiel Amy A Kiger Akio Kihara Deok Ryong Kim Do-Hyung Kim Dong-Hou Kim Eun-Kyoung Kim Hyung-Ryong Kim Jae-Sung Kim Jeong Hun Kim Jin Cheon Kim John K Kim Peter K Kim Seong Who Kim Yong-Sun Kim Yonghyun Kim Adi Kimchi Alec C Kimmelman Jason S King Timothy J Kinsella Vladimir Kirkin Lorrie A Kirshenbaum Katsuhiko Kitamoto Kaio Kitazato Ludger Klein Walter T Klimecki Jochen Klucken Erwin Knecht Ben C B Ko Jan C Koch Hiroshi Koga Jae-Young Koh Young Ho Koh Masato Koike Masaaki Komatsu Eiki Kominami Hee Jeong Kong Wei-Jia Kong Viktor I Korolchuk Yaichiro Kotake Michael I Koukourakis Juan B Kouri Flores Attila L Kovács Claudine Kraft Dimitri Krainc Helmut Krämer Carole Kretz-Remy Anna M Krichevsky Guido Kroemer Rejko Krüger Oleg Krut Nicholas T Ktistakis Chia-Yi Kuan Roza Kucharczyk Ashok Kumar Raj Kumar Sharad Kumar Mondira Kundu Hsing-Jien Kung Tino Kurz Ho Jeong Kwon Albert R La Spada Frank Lafont Trond Lamark Jacques Landry Jon D Lane Pierre Lapaquette Jocelyn F Laporte Lajos László Sergio Lavandero Josée N Lavoie Robert Layfield Pedro A Lazo Weidong Le Laurent Le Cam Daniel J Ledbetter Alvin J X Lee Byung-Wan Lee Gyun Min Lee Jongdae Lee Ju-Hyun Lee Michael Lee Myung-Shik Lee Sug Hyung Lee Christiaan Leeuwenburgh Patrick Legembre Renaud Legouis Michael Lehmann Huan-Yao Lei Qun-Ying Lei David A Leib José Leiro John J Lemasters Antoinette Lemoine Maciej S Lesniak Dina Lev Victor V Levenson Beth Levine Efrat Levy Faqiang Li Jun-Lin Li Lian Li Sheng Li Weijie Li Xue-Jun Li Yan-bo Li Yi-Ping Li Chengyu Liang Qiangrong Liang Yung-Feng Liao Pawel P Liberski Andrew Lieberman Hyunjung J Lim Kah-Leong Lim Kyu Lim Chiou-Feng Lin Fu-Cheng Lin Jian Lin Jiandie D Lin Kui Lin Wan-Wan Lin Weei-Chin Lin Yi-Ling Lin Rafael Linden Paul Lingor Jennifer Lippincott-Schwartz Michael P Lisanti Paloma B Liton Bo Liu Chun-Feng Liu Kaiyu Liu Leyuan Liu Qiong A Liu Wei Liu Young-Chau Liu Yule Liu Richard A Lockshin Chun-Nam Lok Sagar Lonial Benjamin Loos Gabriel Lopez-Berestein Carlos López-Otín Laura Lossi Michael T Lotze Peter Lőw Binfeng Lu Bingwei Lu Bo Lu Zhen Lu Frédéric Luciano Nicholas W Lukacs Anders H Lund Melinda A Lynch-Day Yong Ma Fernando Macian Jeff P MacKeigan Kay F Macleod Frank Madeo Luigi Maiuri Maria Chiara Maiuri Davide Malagoli May Christine V Malicdan Walter Malorni Na Man Eva-Maria Mandelkow Stéphen Manon Irena Manov Kai Mao Xiang Mao Zixu Mao Philippe Marambaud Daniela Marazziti Yves L Marcel Katie Marchbank Piero Marchetti Stefan J Marciniak Mateus Marcondes Mohsen Mardi Gabriella Marfe Guillermo Mariño Maria Markaki Mark R Marten Seamus J Martin Camille Martinand-Mari Wim Martinet Marta Martinez-Vicente Matilde Masini Paola Matarrese Saburo Matsuo Raffaele Matteoni Andreas Mayer Nathalie M Mazure David J McConkey Melanie J McConnell Catherine McDermott Christine McDonald Gerald M McInerney Sharon L McKenna BethAnn McLaughlin Pamela J McLean Christopher R McMaster G Angus McQuibban Alfred J Meijer Miriam H Meisler Alicia Meléndez Thomas J Melia Gerry Melino Maria A Mena Javier A Menendez Rubem F S Menna-Barreto Manoj B Menon Fiona M Menzies Carol A Mercer Adalberto Merighi Diane E Merry Stefania Meschini Christian G Meyer Thomas F Meyer Chao-Yu Miao Jun-Ying Miao Paul A M Michels Carine Michiels Dalibor Mijaljica Ana Milojkovic Saverio Minucci Clelia Miracco Cindy K Miranti Ioannis Mitroulis Keisuke Miyazawa Noboru Mizushima Baharia Mograbi Simin Mohseni Xavier Molero Bertrand Mollereau Faustino Mollinedo Takashi Momoi Iryna Monastyrska Martha M Monick Mervyn J Monteiro Michael N Moore Rodrigo Mora Kevin Moreau Paula I Moreira Yuji Moriyasu Jorge Moscat Serge Mostowy Jeremy C Mottram Tomasz Motyl Charbel E-H Moussa Sylke Müller Sylviane Muller Karl Münger Christian Münz Leon O Murphy Maureen E Murphy Antonio Musarò Indira Mysorekar Eiichiro Nagata Kazuhiro Nagata Aimable Nahimana Usha Nair Toshiyuki Nakagawa Kiichi Nakahira Hiroyasu Nakano Hitoshi Nakatogawa Meera Nanjundan Naweed I Naqvi Derek P Narendra Masashi Narita Miguel Navarro Steffan T Nawrocki Taras Y Nazarko Andriy Nemchenko Mihai G Netea Thomas P Neufeld Paul A Ney Ioannis P Nezis Huu Phuc Nguyen Daotai Nie Ichizo Nishino Corey Nislow Ralph A Nixon Takeshi Noda Angelika A Noegel Anna Nogalska Satoru Noguchi Lucia Notterpek Ivana Novak Tomoyoshi Nozaki Nobuyuki Nukina Thorsten Nürnberger Beat Nyfeler Keisuke Obara Terry D Oberley Salvatore Oddo Michinaga Ogawa Toya Ohashi Koji Okamoto Nancy L Oleinick F Javier Oliver Laura J Olsen Stefan Olsson Onya Opota Timothy F Osborne Gary K Ostrander Kinya Otsu Jing-hsiung James Ou Mireille Ouimet Michael Overholtzer Bulent Ozpolat Paolo Paganetti Ugo Pagnini Nicolas Pallet Glen E Palmer Camilla Palumbo Tianhong Pan Theocharis Panaretakis Udai Bhan Pandey Zuzana Papackova Issidora Papassideri Irmgard Paris Junsoo Park Ohkmae K Park Jan B Parys Katherine R Parzych Susann Patschan Cam Patterson Sophie Pattingre John M Pawelek Jianxin Peng David H Perlmutter Ida Perrotta George Perry Shazib Pervaiz Matthias Peter Godefridus J Peters Morten Petersen Goran Petrovski James M Phang Mauro Piacentini Philippe Pierre Valérie Pierrefite-Carle Gérard Pierron Ronit Pinkas-Kramarski Antonio Piras Natik Piri Leonidas C Platanias Stefanie Pöggeler Marc Poirot Angelo Poletti Christian Poüs Mercedes Pozuelo-Rubio Mette Prætorius-Ibba Anil Prasad Mark Prescott Muriel Priault Nathalie Produit-Zengaffinen Ann Progulske-Fox Tassula Proikas-Cezanne Serge Przedborski Karin Przyklenk Rosa Puertollano Julien Puyal Shu-Bing Qian Liang Qin Zheng-Hong Qin Susan E Quaggin Nina Raben Hannah Rabinowich Simon W Rabkin Irfan Rahman Abdelhaq Rami Georg Ramm Glenn Randall Felix Randow V Ashutosh Rao Jeffrey C Rathmell Brinda Ravikumar Swapan K Ray Bruce H Reed John C Reed Fulvio Reggiori Anne Régnier-Vigouroux Andreas S Reichert John J Reiners Russel J Reiter Jun Ren José L Revuelta Christopher J Rhodes Konstantinos Ritis Elizete Rizzo Jeffrey Robbins Michel Roberge Hernan Roca Maria C Roccheri Stephane Rocchi H Peter Rodemann Santiago Rodríguez de Córdoba Bärbel Rohrer Igor B Roninson Kirill Rosen Magdalena M Rost-Roszkowska Mustapha Rouis Kasper M A Rouschop Francesca Rovetta Brian P Rubin David C Rubinsztein Klaus Ruckdeschel Edmund B Rucker Assaf Rudich Emil Rudolf Nelson Ruiz-Opazo Rossella Russo Tor Erik Rusten Kevin M Ryan Stefan W Ryter David M Sabatini Junichi Sadoshima Tapas Saha Tatsuya Saitoh Hiroshi Sakagami Yasuyoshi Sakai Ghasem Hoseini Salekdeh Paolo Salomoni Paul M Salvaterra Guy Salvesen Rosa Salvioli Anthony M J Sanchez José A Sánchez-Alcázar Ricardo Sánchez-Prieto Marco Sandri Uma Sankar Poonam Sansanwal Laura Santambrogio Shweta Saran Sovan Sarkar Minnie Sarwal Chihiro Sasakawa Ausra 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Efthimios Sivridis Vojtech Skop Vladimir P Skulachev Ruth S Slack Soraya S Smaili Duncan R Smith Maria S Soengas Thierry Soldati Xueqin Song Anil K Sood Tuck Wah Soong Federica Sotgia Stephen A Spector Claudia D Spies Wolfdieter Springer Srinivasa M Srinivasula Leonidas Stefanis Joan S Steffan Ruediger Stendel Harald Stenmark Anastasis Stephanou Stephan T Stern Cinthya Sternberg Björn Stork Peter Strålfors Carlos S Subauste Xinbing Sui David Sulzer Jiaren Sun Shi-Yong Sun Zhi-Jun Sun Joseph J Y Sung Kuninori Suzuki Toshihiko Suzuki Michele S Swanson Charles Swanton Sean T Sweeney Lai-King Sy Gyorgy Szabadkai Ira Tabas Heinrich Taegtmeyer Marco Tafani Krisztina Takács-Vellai Yoshitaka Takano Kaoru Takegawa Genzou Takemura Fumihiko Takeshita Nicholas J Talbot Kevin S W Tan Keiji Tanaka Kozo Tanaka Daolin Tang Dingzhong Tang Isei Tanida Bakhos A Tannous Nektarios Tavernarakis Graham S Taylor Gregory A Taylor J Paul Taylor Lance S Terada Alexei Terman Gianluca Tettamanti Karin Thevissen Craig B Thompson Andrew Thorburn Michael Thumm FengFeng Tian Yuan Tian Glauco Tocchini-Valentini Aviva M Tolkovsky Yasuhiko Tomino Lars Tönges Sharon A Tooze Cathy Tournier John Tower Roberto Towns Vladimir Trajkovic Leonardo H Travassos Ting-Fen Tsai Mario P Tschan Takeshi Tsubata Allan Tsung Boris Turk Lorianne S Turner Suresh C Tyagi Yasuo Uchiyama Takashi Ueno Midori Umekawa Rika Umemiya-Shirafuji Vivek K Unni Maria I Vaccaro Enza Maria Valente Greet Van den Berghe Ida J van der Klei Wouter van Doorn Linda F van Dyk Marjolein van Egmond Leo A van Grunsven Peter Vandenabeele Wim P Vandenberghe Ilse Vanhorebeek Eva C Vaquero Guillermo Velasco Tibor Vellai Jose Miguel Vicencio Richard D Vierstra Miquel Vila Cécile Vindis Giampietro Viola Maria Teresa Viscomi Olga V Voitsekhovskaja Clarissa von Haefen Marcela Votruba Keiji Wada Richard Wade-Martins Cheryl L Walker Craig M Walsh Jochen Walter Xiang-Bo Wan Aimin Wang Chenguang Wang Dawei Wang Fan Wang Fen Wang Guanghui Wang Haichao Wang Hong-Gang Wang Horng-Dar Wang Jin Wang Ke Wang Mei Wang Richard C Wang Xinglong Wang Xuejun Wang Ying-Jan Wang Yipeng Wang Zhen Wang Zhigang Charles Wang Zhinong Wang Derick G Wansink Diane M Ward Hirotaka Watada Sarah L Waters Paul Webster Lixin Wei Conrad C Weihl William A Weiss Scott M Welford Long-Ping Wen Caroline A Whitehouse J Lindsay Whitton Alexander J Whitworth Tom Wileman John W Wiley Simon Wilkinson Dieter Willbold Roger L Williams Peter R Williamson Bradly G Wouters Chenghan Wu Dao-Cheng Wu William K K Wu Andreas Wyttenbach Ramnik J Xavier Zhijun Xi Pu Xia Gengfu Xiao Zhiping Xie Zhonglin Xie Da-zhi Xu Jianzhen Xu Liang Xu Xiaolei Xu Ai Yamamoto Akitsugu Yamamoto Shunhei Yamashina Michiaki Yamashita Xianghua Yan Mitsuhiro Yanagida Dun-Sheng Yang Elizabeth Yang Jin-Ming Yang Shi Yu Yang Wannian Yang Wei Yuan Yang Zhifen Yang Meng-Chao Yao Tso-Pang Yao Behzad Yeganeh Wei-Lien Yen Jia-jing Yin Xiao-Ming Yin Ook-Joon Yoo Gyesoon Yoon Seung-Yong Yoon Tomohiro Yorimitsu Yuko Yoshikawa Tamotsu Yoshimori Kohki Yoshimoto Ho Jin You Richard J Youle Anas Younes Li Yu Long Yu Seong-Woon Yu Wai Haung Yu Zhi-Min Yuan Zhenyu Yue Cheol-Heui Yun Michisuke Yuzaki Olga Zabirnyk Elaine Silva-Zacarin David Zacks Eldad Zacksenhaus Nadia Zaffaroni Zahra Zakeri Herbert J Zeh Scott O Zeitlin Hong Zhang Hui-Ling Zhang Jianhua Zhang Jing-Pu Zhang Lin Zhang Long Zhang Ming-Yong Zhang Xu Dong Zhang Mantong Zhao Yi-Fang Zhao Ying Zhao Zhizhuang J Zhao Xiaoxiang Zheng Boris Zhivotovsky Qing Zhong Cong-Zhao Zhou Changlian Zhu Wei-Guo Zhu Xiao-Feng Zhu Xiongwei Zhu Yuangang Zhu Teresa Zoladek Wei-Xing Zong Antonio Zorzano Jürgen Zschocke Brian Zuckerbraun

Autophagy 2012 Apr;8(4):445-544

Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.

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April 2012

Mitochondrial fission, fusion, and stress.

Science 2012 Aug;337(6098):1062-5

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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August 2012

PINK1- and Parkin-mediated mitophagy at a glance.

J Cell Sci 2012 Feb;125(Pt 4):795-9

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Center Drive, 10-5D37 Bethesda, MD USA.

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February 2012

Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling.

Nat Methods 2012 Feb 5;9(3):303-9. Epub 2012 Feb 5.

Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA.

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Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin.

Dev Cell 2012 Feb 25;22(2):320-33. Epub 2012 Jan 25.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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February 2012

PINK1 and Parkin flag Miro to direct mitochondrial traffic.

Cell 2011 Nov;147(4):721-3

National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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November 2011

Coupling mitochondrial and cell division.

Nat Cell Biol 2011 Sep 2;13(9):1026-7. Epub 2011 Sep 2.

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September 2011

Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics.

Dev Cell 2011 Jul;21(1):92-101

Department of Cell Biology, University of Geneva, Faculty of Sciences, 30 quai Ernest-Ansermet, Geneva 4, Switzerland.

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July 2011

Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation.

Curr Opin Cell Biol 2011 Aug 24;23(4):476-82. Epub 2011 Jun 24.

Center for Biomedical Engineering and Technology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

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August 2011

The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes.

Mol Cell 2011 Jan;41(2):150-60

Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.

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January 2011

Targeting mitochondrial dysfunction: role for PINK1 and Parkin in mitochondrial quality control.

Antioxid Redox Signal 2011 May 3;14(10):1929-38. Epub 2011 Mar 3.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.

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May 2011

Mechanisms of mitophagy.

Nat Rev Mol Cell Biol 2011 Jan;12(1):9-14

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, 2C-917, Bethesda, Maryland 20892, USA.

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January 2011

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin.

J Cell Biol 2010 Dec 20;191(7):1367-80. Epub 2010 Dec 20.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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December 2010

Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells.

J Cell Biol 2010 Dec;191(6):1141-58

Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan.

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http://dx.doi.org/10.1083/jcb.201007152DOI Listing
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December 2010

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL.

J Cell Biol 2010 Nov;191(5):933-42

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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November 2010

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

Autophagy 2010 Nov;6(8):1090-106

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke National Institutes of Health, Bethesda, MD, USA.

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November 2010

Mitochondrial fission and fusion and their roles in the heart.

J Mol Med (Berl) 2010 Oct 14;88(10):971-9. Epub 2010 Sep 14.

National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.

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October 2010

Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells.

Proc Natl Acad Sci U S A 2010 Jun 14;107(26):11835-40. Epub 2010 Jun 14.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1073/pnas.0914569107DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2900690PMC
June 2010

Mitochondrial fission and fusion.

Essays Biochem 2010 ;47:85-98

National Heart, Lung and Blood Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1042/bse0470085DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762097PMC
December 2010

Pseudomonas exotoxin A-mediated apoptosis is Bak dependent and preceded by the degradation of Mcl-1.

Mol Cell Biol 2010 Jul 10;30(14):3444-52. Epub 2010 May 10.

Laboratory of Molecular Biology, National Cancer Institute, 37 Convent Drive, Bethesda, MD 20892-4264, USA.

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http://dx.doi.org/10.1128/MCB.00813-09DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2897547PMC
July 2010

IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation.

EMBO J 2010 Apr 18;29(8):1458-71. Epub 2010 Mar 18.

Center for Biomedical Engineering and Technology, University of Maryland, Baltimore, MD, USA.

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http://dx.doi.org/10.1038/emboj.2010.39DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2868578PMC
April 2010

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin.

PLoS Biol 2010 Jan 26;8(1):e1000298. Epub 2010 Jan 26.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, USA.

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http://dx.doi.org/10.1371/journal.pbio.1000298DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811155PMC
January 2010

Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1.

J Cell Sci 2010 Feb 26;123(Pt 4):619-26. Epub 2010 Jan 26.

Department of Biochemistry, Ajou University School of Medicine, Yeongtong-gu, Suwon 443-721, Korea.

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http://dx.doi.org/10.1242/jcs.061481DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2818198PMC
February 2010

Bax activates endophilin B1 oligomerization and lipid membrane vesiculation.

J Biol Chem 2009 Dec 5;284(49):34390-9. Epub 2009 Oct 5.

Laboratory of Physical and Structural Biology, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://dx.doi.org/10.1074/jbc.M109.021873DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797207PMC
December 2009

The role of mitochondria in apoptosis*.

Annu Rev Genet 2009 ;43:95-118

Biochemistry Section, Surgical Neurology Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://www.annualreviews.org/doi/10.1146/annurev-genet-10210
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http://dx.doi.org/10.1146/annurev-genet-102108-134850DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762029PMC
December 2009

SnapShot: BCL-2 proteins.

Cell 2009 Jul;138(2):404, 404.e1

Johns Hopkins, Baltimore, MD 21205, USA.

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http://linkinghub.elsevier.com/retrieve/pii/S009286740900839
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http://dx.doi.org/10.1016/j.cell.2009.07.003DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2902885PMC
July 2009

Parkin-induced mitophagy in the pathogenesis of Parkinson disease.

Autophagy 2009 Jul 22;5(5):706-8. Epub 2009 Jul 22.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.4161/auto.5.5.8505DOI Listing
July 2009

Role of the ubiquitin conjugation system in the maintenance of mitochondrial homeostasis.

Ann N Y Acad Sci 2008 Dec;1147:242-53

Surgical Neurology Branch/National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD, USA.

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http://dx.doi.org/10.1196/annals.1427.012DOI Listing
December 2008

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy.

J Cell Biol 2008 Dec 24;183(5):795-803. Epub 2008 Nov 24.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1083/jcb.200809125DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2592826PMC
December 2008

Mitochondrial dynamics and apoptosis.

Genes Dev 2008 Jun;22(12):1577-90

Biochemistry Section, Surgical Neurology Branch, NINDS, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1101/gad.1658508DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732420PMC
June 2008

Endosome fusion induced by diphtheria toxin translocation domain.

Proc Natl Acad Sci U S A 2008 Jun 6;105(23):8020-5. Epub 2008 Jun 6.

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive MSC 3704, Bethesda, MD 20892, USA.

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http://www.pnas.org/cgi/doi/10.1073/pnas.0711707105
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http://dx.doi.org/10.1073/pnas.0711707105DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2430352PMC
June 2008

Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins.

J Virol 2008 Jul 16;82(13):6232-43. Epub 2008 Apr 16.

Biochemistry Section, Surgical Neurology Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://dx.doi.org/10.1128/JVI.02710-07DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2447053PMC
July 2008

A chemical inhibitor of DRP1 uncouples mitochondrial fission and apoptosis.

Mol Cell 2008 Feb;29(4):409-10

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20824, USA.

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http://dx.doi.org/10.1016/j.molcel.2008.02.005DOI Listing
February 2008

The BCL-2 protein family: opposing activities that mediate cell death.

Nat Rev Mol Cell Biol 2008 Jan;9(1):47-59

Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, The National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://www.nature.com/doifinder/10.1038/nrm2308
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http://dx.doi.org/10.1038/nrm2308DOI Listing
January 2008

Outer mitochondrial membrane protein degradation by the proteasome.

Novartis Found Symp 2007 ;287:4-14; discussion 14-20

Biochemistry Section, SNB, NINDS, NIH, Bethesda, MD 20892, USA.

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January 2008

The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division.

J Cell Biol 2007 Jul;178(1):71-84

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20852, USA.

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http://www.jcb.org/lookup/doi/10.1083/jcb.200611064
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http://dx.doi.org/10.1083/jcb.200611064DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064424PMC
July 2007

Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence.

J Biol Chem 2007 Aug 1;282(31):22977-83. Epub 2007 Jun 1.

Department of Biochemistry, Ajou University School of Medicine, Ajou University, 5 Wonchon-dong, Yeongtong-gu, Suwon 443-721, Korea.

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http://dx.doi.org/10.1074/jbc.M700679200DOI Listing
August 2007

Role of mitochondrial remodeling in programmed cell death in Drosophila melanogaster.

Dev Cell 2007 May;12(5):807-16

National Centre for Biological Sciences, Tata Institute of Fundamental Research, GKVK-Campus, Bellary Road, Bangalore 560 065, India.

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http://dx.doi.org/10.1016/j.devcel.2007.02.002DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1885957PMC
May 2007

The cytokine, granulocyte-macrophage colony-stimulating factor (GM-CSF), can deliver Bcl-XL as an extracellular fusion protein to protect cells from apoptosis and retain differentiation induction.

J Biol Chem 2007 Apr 20;282(15):11246-54. Epub 2007 Feb 20.

Biochemistry Section, Surgical Neurology Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.

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http://dx.doi.org/10.1074/jbc.M609824200DOI Listing
April 2007

Cell biology. Cellular demolition and the rules of engagement.

Authors:
Richard J Youle

Science 2007 Feb;315(5813):776-7

Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

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http://dx.doi.org/10.1126/science.1138870DOI Listing
February 2007