Arthur L. Horwich

Arthur L. Horwich's AcademicInfluence.com Rankings

Arthur L. Horwich

Biology

#848

World Rank

#1479

Historical Rank

#455

USA Rank

Molecular Biology

#273

World Rank

#278

Historical Rank

#112

USA Rank

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Biology

Arthur L. Horwich's Degrees

Doctorate Medicine University of Chicago
PhD Biochemistry University of California, San Francisco

Why Is Arthur L. Horwich Influential?

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According to Wikipedia, Arthur L. Horwich is an American biologist and Sterling Professor of Genetics and Pediatrics at the Yale School of Medicine. Horwich has also been a Howard Hughes Medical Institute investigator since 1990. His research into protein folding uncovered the action of chaperonins, protein complexes that assist the folding of other proteins; Horwich first published this work in 1989.

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Arthur L. Horwich's Published Works

Number of citations in a given year to any of this author's works

Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author

Published Works

The Hsp70 and Hsp60 Chaperone Machines (1998) (2750)
Molecular Chaperones and Protein Quality Control (2006) (1485)
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å (1994) (1201)
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex (1997) (1163)
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria (1989) (853)
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate (1991) (757)
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis (1989) (607)
Structure and function in GroEL-mediated protein folding. (1998) (553)
Mechanisms of protein folding. (2001) (433)
TCP1 complex is a molecular chaperone in tubulin biogenesis (1992) (431)
Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell (1994) (427)
Two families of chaperonin: physiology and mechanism. (2007) (426)
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA (1999) (422)
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction (1996) (392)
NMR analysis of a 900K GroEL–GroES complex (2002) (391)
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL (1997) (377)
GroEL‐Mediated protein folding (1997) (342)
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms (1994) (332)
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL (1993) (327)
Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification (1990) (326)
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 (1991) (319)
GroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings (1999) (303)
Prevention of protein denaturation under heat stress by the chaperonin Hsp60. (1992) (290)
ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy (2001) (287)
ClpS, a substrate modulator of the ClpAP machine. (2002) (283)
Deadly Conformations—Protein Misfolding in Prion Disease (1997) (267)
The Hsp 70 and Hsp 60 Review Chaperone Machines (1998) (255)
Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation (2005) (240)
Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space (1992) (227)
Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. (2002) (224)
GroEL‐GroES‐mediated protein folding (2006) (209)
Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. (1994) (208)
Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase. (1984) (196)
Chaperone rings in protein folding and degradation. (1999) (191)
An ALS-Linked Mutant SOD1 Produces a Locomotor Defect Associated with Aggregation and Synaptic Dysfunction When Expressed in Neurons of Caenorhabditis elegans (2009) (186)
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL (2000) (185)
A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. (1985) (179)
Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms (1997) (173)
GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated (2001) (172)
A polypeptide bound by the chaperonin groEL is localized within a central cavity. (1993) (165)
ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin (2012) (160)
Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes (2006) (158)
Chaperonin-mediated protein folding: fate of substrate polypeptide (2003) (158)
Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT (1998) (155)
The mitochondrial chaperonin hsp60 is required for its own assembly. (1990) (155)
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding (2009) (148)
Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS (2009) (147)
ClpA mediates directional translocation of substrate proteins into the ClpP protease (2001) (145)
Structure and allostery of the chaperonin GroEL. (2013) (145)
Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration (2013) (142)
Linkage mapping of a mouse gene, iv, that controls left-right asymmetry of the heart and viscera. (1989) (139)
Chaperonin-mediated Protein Folding (2011) (137)
Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL (2006) (136)
Solution NMR techniques for large molecular and supramolecular structures. (2002) (133)
Targeting of pre-ornithine transcarbamylase to mitochondria: Definition of critical regions and residues in the leader peptide (1986) (129)
Role of the γ‐phosphate of ATP in triggering protein folding by GroEL–GroES: function, structure and energetics (2003) (125)
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo (1991) (122)
Human ornithine transcarbamylase locus mapped to band Xp21.1 near the Duchenne muscular dystrophy locus. (1984) (121)
Gene deletion and restriction fragment length polymorphisms at the human ornithine transcarbamylase locus (1985) (121)
THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS (1995) (117)
Direct NMR observation of a substrate protein bound to the chaperonin GroEL. (2005) (116)
The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related. (1988) (114)
Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. (2004) (108)
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. (1993) (108)
Topologies of a Substrate Protein Bound to the Chaperonin GroEL (2007) (102)
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation (2008) (99)
The GroEL/GroES cis cavity as a passive anti‐aggregation device (2009) (99)
Folding of malate dehydrogenase inside the GroEL–GroES cavity (2001) (88)
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. (1998) (85)
Localization of DNA sequences in region Xp21 of the human X chromosome: search for molecular markers close to the Duchenne muscular dystrophy locus. (1985) (85)
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. (1997) (80)
Uniform and Residue-specific 15N-labeling of Proteins on a Highly Deuterated Background (2004) (73)
Sorting pathways of mitochondrial inner membrane proteins. (1990) (71)
Folding with and without encapsulation by cis‐ and trans‐only GroEL–GroES complexes (2003) (71)
Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. (1992) (70)
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. (2004) (68)
Synthesis of hepadnavirus particles that contain replication-defective duck hepatitis B virus genomes in cultured HuH7 cells (1990) (66)
Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm (2013) (63)
RNA-Seq Profiling of Spinal Cord Motor Neurons from a Presymptomatic SOD1 ALS Mouse (2013) (62)
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. (1996) (61)
A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. (1985) (58)
Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. (1985) (58)
Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110 (2016) (56)
Folding trajectories of human dihydrofolate reductase inside the GroEL–GroES chaperonin cavity and free in solution (2007) (52)
Perturbed ATPase activity and not “close confinement” of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL (2007) (52)
Selective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS (2014) (49)
Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol (1996) (48)
Protein folding in the cell: an inside story (2011) (47)
GroEL/GroES‐mediated protein folding (2006) (46)
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation (2004) (44)
Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. (2001) (43)
Trisomy 18 associated with ectopia cordis and occipital meningocele. (1988) (43)
A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12 (1994) (41)
From the cradle to the grave: ring complexes in the life of a protein. (1995) (40)
Molecular Chaperones in Cellular Protein Folding: The Birth of a Field (2014) (40)
A father and son with cholestasis and peripheral pulmonic stenosis: a distinct form of intrahepatic cholestasis. (1978) (40)
GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state (2009) (38)
Short‐term response to dietary therapy in molybdenum cofactor deficiency (1993) (37)
Roles of the N-domains of the ClpA Unfoldase in Binding Substrate Proteins and in Stable Complex Formation with the ClpP Protease* (2005) (36)
A biochemical screen for GroEL/GroES inhibitors. (2014) (35)
Multiple states of a nucleotide-bound group 2 chaperonin. (2008) (35)
The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge (1987) (34)
Absence of lipofuscin in motor neurons of SOD1-linked ALS mice (2014) (34)
GroEL/ES inhibitors as potential antibiotics. (2016) (34)
Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae. (1987) (33)
Hsp110 mitigates α-synuclein pathology in vivo (2019) (33)
The thermosome: chaperonin with a built-in lid (1998) (33)
Protein-catalysed protein folding. (1990) (33)
Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. (1983) (32)
Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented (2011) (32)
Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. (1996) (30)
CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7 (1997) (30)
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state (2008) (30)
Expression and Stabilization of Microinjected Plasmids Containing the Herpes Simplex Virus Thymidine Kinase Gene and Polyoma Virus DNA in Mouse Cells (1983) (30)
Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor (1985) (29)
Sulfonamido-2-arylbenzoxazole GroEL/ES Inhibitors as Potent Antibacterials against Methicillin-Resistant Staphylococcus aureus (MRSA). (2018) (29)
Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR. (2011) (28)
Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid. (2011) (27)
Proton–proton Overhauser NMR spectroscopy with polypeptide chains in large structures (2006) (27)
Targeting the HSP60/10 chaperonin systems of Trypanosoma brucei as a strategy for treating African sleeping sickness. (2016) (25)
Establishment of left-right asymmetry in vertebrates: genetically distinct steps are involved. (2007) (24)
Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. (1998) (23)
Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy. (2005) (23)
Molecular Chaperones: Resurrection or destruction? (1995) (22)
Brief clinical report: aqueductal stenosis leading to hydrocephalus--an unusual manifestation of neurofibromatosis. (1983) (20)
No evidence for a forced‐unfolding mechanism during ATP/GroES binding to substrate‐bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL‐bound Rubisco from tritium exchange (2005) (20)
Targeting of Nuclear‐Encoded Proteins to the Mitochondrial Matrix: Implications for Human Genetic Defects (1986) (18)
Reduced high-frequency motor neuron firing, EMG fractionation, and gait variability in awake walking ALS mice (2016) (18)
A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL. (2009) (18)
Chaperonin-assisted protein folding: a chronologue (2020) (17)
Duplication/deficiency mapping of situs inversus viscerum (iv), a gene that determines left-right asymmetry in the mouse. (1992) (16)
Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice (2017) (16)
Hydrogen–deuterium exchange in vivo to measure turnover of an ALS‐associated mutant SOD1 protein in spinal cord of mice (2011) (14)
Unliganded GroEL at 2.8 A: structure and functional implications. (1995) (14)
Sight at the end of the tunnel (2004) (14)
The effects of early treatment of hereditary tyrosinemia type I in infancy by orthotopic liver transplantation. (1990) (14)
Disulfide formation as a probe of folding in GroEL–GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones (2007) (12)
Chaperoned Protein Disaggregation—The ClpB Ring Uses Its Central Channel (2004) (12)
Expression of the gene for the polyoma small T antigen in Escherichia coli (1980) (10)
Meiotic expression of human ornithine transcarbamylase in the testes of transgenic mice (1988) (10)
The crystal structure of GROEL at 2.8 . (1995) (10)
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin (2018) (9)
Production of RNA for Transcriptomic Analysis from Mouse Spinal Cord Motor Neuron Cell Bodies by Laser Capture Microdissection (2014) (8)
Protein folding taking shape (2001) (8)
The processing peptidase of yeast mitochondria (1988) (8)
DNA analysis for ornithine transcarbamylase deficiency (1986) (6)
An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na+-Activated K+ Channels in Aplysia Neurons (2017) (5)
Precarious balance of nitrogen metabolism in women with a urea-cycle defect. (1990) (5)
THE 2.4 ANGSTROM CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL COMPLEXED WITH ATP-GAMMA-S (1996) (5)
Syntheses and stabilities of proteins related to the polyoma small T antigen in Escherichia coli (1982) (4)
Role of HSP60 in Folding/Assembly of Mitochondrial Proteins (1991) (4)
Working with Paul Sigler (2000) (4)
Protein folding taking shape Workshop on molecular chaperones (2001) (4)
ATP‐triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate‐limiting step of the GroEL/GroES reaction cycle (2010) (4)
Kinesis of polypeptide during GroEL-mediated folding. (1995) (3)
Structure and Action of Molecular Chaperones: Machines that Assist Protein Folding in the Cell (2016) (3)
Molecular chaperones in biology and medicine at Obernai. (1997) (3)
Structure and action of molecular chaperones (2016) (3)
Overwhelming sepsis in the adult variant of Wiskott-Aldrich syndrome. (1984) (3)
Protein folding in the cell (2002) (3)
Chapter 26 Chaperonin-mediated protein folding (1992) (3)
Chaperonin studies: faith, luck, and a little help from our friends (2017) (2)
820 ADDITIONAL RESTRICTION FRAGMENT LENGTH POLYMORPHISMS (RFLS)FOR DETECTION OF ORNITHINE TRANSCARBAMYLASE (OTC) DEFICIENCY (1985) (2)
STRATEGIES FOR THE MOLECULAR CLONING OF LOW ABUNDANCE MESSENGER RNAs (1984) (2)
Chemical Strike against a Dominant-Inherited MUC1-Frameshifted Protein Associated with Progressive Kidney Disease. (2019) (2)
Primary structure and function of a second essential member of the heterooligomeric TCP 1 chaperonin complex of yeast , TCP 1 fi (2)
Role of the g-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and (2003) (2)
Resurrection or destruction? Recent studies implicate Hspl 04/Clp family chaperones in both protein disaggregation and protein degradation. How do these homologous ring-shaped complexes function in such different ways? (1995) (2)
GENE DELETION AND RESTRICTION FRAGMENT LENGTH POLYMORPHISM (RFLP) AT THE HUMAN ORNITHINE TRANSCARBAMYLASE (OTC) LOCUS (1984) (2)
Molecular Machines in Biology: The GroEL/GroES Chaperonin Machine (2011) (2)
Isolation of Kirsten murine leukemia virus mutant temperature sensitive for particle production and env gene minus. (1982) (1)
Faculty of 1000 evaluation for Alcohol-abuse drug disulfiram targets cancer via p97 segregase adaptor NPL4. (2018) (1)
Motor nuclei innervating eye muscles spared in mouse model of SOD1-linked ALS (2018) (1)
ATP-triggered molecular mechanics of the chaperonin GroEL (2012) (1)
The Role of ATP in directing chaperonin-mediated polypeptide folding (2003) (1)
MOLECULAR STUDY OF ORNITHINE TRANSCARBAMYLASE: OTC DEFICIENCY AND ANALYSIS OF MITOCHONDRIAL TARGETING OF THE OTC PRECURSOR (1987) (1)
Stress-Induced Expression of Heat Shock Proteins and Action of the Heat Shock Protein Effectors (2006) (1)
Oncogenes and human cancer. (1984) (1)
Faculty Opinions recommendation of Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes. (2018) (1)
Structural Analysis of GroEL/GroES Chaperonin-Mediated Protein Folding (2016) (1)
Localization of DNA Sequences in Region Xp2 1 of the Human X Chromosome: Search for Molecular Markers (2006) (1)
Backbone 1H, 13C, and 15N Chemical Shift Assignments for GroES (2006) (0)
Crystal structure of groEL-groES (2003) (0)
ATP and the editing of protein folding (1997) (0)
Solution Structure of apo GroEL by Cryo-Electron microscopy (2002) (0)
SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM (2002) (0)
Faculty Opinions recommendation of Kinetic partitioning of protein folding and aggregation. (2002) (0)
Role of Chaperones in Neurodegeneration (2006) (0)
Isolation and characterisation of a new leukaemia virus mutant. (1981) (0)
SV 2 Expression and Synapse Distribution in Regenerating Spinal Cords of the Sea Lamprey , Petromyzon marinus (2013) (0)
Structural Analysis of Type II Chaperonins in Archaebacteria and the Eukaryotic Cytosol (2016) (0)
GroEL-GroES-ADP7 (2003) (0)
Structural insight into the function of GroEL/GroES/ADP complex (1996) (0)
Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes (1998) (0)
QnAs with Arthur L. Horwich. Interview by Prashant Nair. (2012) (0)
Faculty Opinions recommendation of Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. (2004) (0)
Faculty Opinions recommendation of Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. (2009) (0)
Faculty Opinions recommendation of p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. (2006) (0)
A father and son pulmonic stenosis with cholestasis and peripheral (1978) (0)
Faculty Opinions recommendation of Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. (2006) (0)
ATP-bound states of GroEL and GroEL-GroES captured by cryo-EM and single particle image processing (2002) (0)
Incomplete hepadnaviruses and cell line producing vaccines, as well as the treatment of liver diseases and disorders (1990) (0)
Contents, Vol. 32, 1977 (1977) (0)
October 6 Nonsense-Mediated mRNA Decay in Mammalian Cells: Pre-mRNA Splicing-Dependent mRNA Decay that Occurs 5'-to-3' and 3'-to-5' as a Consequence of a Pioneer Round of Translation (2005) (0)
Distinctactionsof cis and trans ATPwithin thedouble ring of thechaperoninGroEL (0)
Nucleic Acids Research A cDNA clone for the precursor of rat mitochondrial omithine transcarbamylase : comparison of rat and human leader sequences and conservation of catalytic sites (2004) (0)
The mitochondrial stress protein HSP60 as a catalyst of protein folding (1990) (0)
Chaperonin-mediated protein folding - part 2 of 2 (2012) (0)
ANALYSIS OF A CANDIDATE MOUSE IV (INVERSUS VISCERUM) GENE. • 123 (1996) (0)
Biological Bases and Clinical Implications of Tumor Radioresistance, Gilbert H. Fletcher, Carlo Nervi, H. Rodney Withers (Eds.). Masson Publishing, London (1983) (1984) (0)
Faculty Opinions recommendation of A naturally occurring variant of the human prion protein completely prevents prion disease. (2015) (0)
Crystal structure of GroEL14-GroES7-(ADP-AlFx)7 (2005) (0)
Direct NMR observation of a substrate protein bound to the chaperonin GroEL (2021) (0)
GroEL14-(ATPgammaS)14 (2005) (0)
Faculty Opinions recommendation of Small heat-shock proteins protect from heat-stroke-associated neurodegeneration. (2012) (0)
Abstracts of papers presented at the 2002 Meeting on Molecular Chaperones & the Heat Shock Response, May 1-May 5, 2002 (2002) (0)
Abstracts of papers presented at the 2000 Meeting on Molecular Chaperones & the Heat Shock Response, May 3-May 7, 2000 (2000) (0)
Theprocessing peptidase ofyeastmitochondria: the two co-operating componentsMPP andPEPare structurally related (1988) (0)
Solution Structure of GroEL(D398A)+ 250uM ATP by Cryo-Electron microscopy (2002) (0)
Table of Contents (1985) (0)
Chaperones and protein folding (2012) (0)
Faculty Opinions recommendation of Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. (2009) (0)
Deadly Conformations—Protein Review Misfolding in Prion Disease (1997) (0)
Searching for the Missing Link in the Pathogenic Pathway of Mutant SOD 1 in ALS (2013) (0)
Localization ofDNA Sequences inRegionXp21ofthe HumanX Chromosome: SearchforMolecular Markers ClosetotheDuchenneMuscular Dystrophy Locus (1985) (0)
Faculty Opinions recommendation of Vms1 and ANKZF1 peptidyl-tRNA hydrolases release nascent chains from stalled ribosomes. (2018) (0)
Fitted coordinates for GroEL-ADP7-GroES Cryo-EM complex (EMD-1181) (2006) (0)
3.10 Chaperones and Protein Folding (2012) (0)
Meiotic Expression ofHumanOrnithine Transcarbamylase intheTestes ofTransgenic Mice (1988) (0)
Faculty Opinions recommendation of Disulfide bond formation involves a quinhydrone-type charge-transfer complex. (2003) (0)
REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047) (2006) (0)

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