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1998
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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
1994 Nature
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1998
High-resolution single-particle orientation refinement based on spectrally self-adapting common lines
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Decision-making in structure solution using Bayesian estimates of map quality: thePHENIX AutoSolwizard
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Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone
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Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites
2001 Nobel
Residues in chaperonin GroEL required for polypeptide binding and release
1994 Nature
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
1997 Nature
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
1997
The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
1995
Thermophilic Adaptation of Proteins
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Channel opening and gating mechanism in AMPA-subtype glutamate receptors
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High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome
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Automated segmentation of molecular subunits in electron cryomicroscopy density maps
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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
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Unidirectional molecular motor on a gold surface
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Cryo-EM Structure of a Group II Chaperonin in the Prehydrolysis ATP-Bound State Leading to Lid Closure
2011 StandoutNobel
A dynamic model for the allosteric mechanism of GroEL 1 1Edited by A. Fersht
2000
The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
1996
Release of both native and non-native proteins from a cis-only GroEL ternary complex
1996 Nature
Closing the Folding Chamber of the Eukaryotic Chaperonin Requires the Transition State of ATP Hydrolysis
2003
Specificity in chaperonin-mediated protein folding
1995 Nature
How GroES Regulates Binding of Nonnative Protein to GroEL
1997
Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin
1995
GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine
1998
Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit
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GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices 1 1Edited by J. Karn
1999
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
1996 NatureNobel
Identification of GroEL as a constituent of an mRNA‐protection complex in Escherichia coli
1995
The Hsp70 and Hsp60 Chaperone Machines
1998 Standout
GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated
2001
Crystal Structures of the Group II Chaperonin from Thermococcus strain KS-1: Steric Hindrance by the Substituted Amino Acid, and Inter-subunit Rearrangement between Two Crystal Forms
2003
Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations
2000
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
1995
Towards automated crystallographic structure refinement with phenix.refine
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Evolution of a designed protein assembly encapsulating its own RNA genome
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Rational design of α-helical tandem repeat proteins with closed architectures
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Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm‐cpn
2003
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
1997
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
1994 Nature
The Crystal Structure of a GroEL/Peptide Complex
1999
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
1995
Design of biologically active binary protein 2D materials
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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
1994
Nested allosteric interactions in the cytoplasmic chaperonin containing TCP‐1
2001
FindEM—a fast, efficient program for automatic selection of particles from electron micrographs
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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
1993 Nature
Not your average density
1997
GroEL-Mediated Protein Folding: Making the Impossible, Possible
2006
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
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Structure of mammalian eIF3 in the context of the 43S preinitiation complex
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Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70
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Structure of the mechanically activated ion channel Piezo1
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Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction
1997
GroEL‐Mediated protein folding
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An Expanded Conformation of Single-Ring GroEL-GroES Complex Encapsulates an 86 kDa Substrate
2006
The Disordered Mobile Loop of GroES Folds into a Defined β-Hairpin upon Binding GroEL
2001
NMR analysis of a 900K GroEL–GroES complex
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Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle
2010
De novo design of a fluorescence-activating β-barrel
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Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
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MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
1999
Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7
1999
Flexible Fitting of Atomic Structures into Electron Microscopy Maps Using Molecular Dynamics
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Automated molecular microscopy: The new Leginon system
2005 Standout
Structure of the Molecular Chaperone Prefoldin
2000
Revisiting the Anfinsen cage
1996
The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure Topology
1995
Molecular chaperones in cellular protein folding
1996 StandoutNature
The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin
2001
Kinetic Analysis of Interactions between GroEL and Reduced α-Lactalbumin
1995
Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
1994
Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT
1998
Structural Adaptations in the Specialized Bacteriophage T4 Co-Chaperonin Gp31 Expand the Size of the Anfinsen Cage
1997 Nobel
3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin.
1999
Mechanism of folding chamber closure in a group II chaperonin
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GroEL Binds to and Unfolds Rhodanese Posttranslationally
1996
Gene Duplication and the Evolution of Group II Chaperonins: Implications for Structure and Function
2001
Folding of malate dehydrogenase inside the GroEL-GroES cavity.
2001
Transient Kinetic Analysis of ATP-induced Allosteric Transitions in the Eukaryotic Chaperonin containing TCP-1
2003
Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin
1998
Primary Structure of the Thermosome fromThermoplasma acidophilum
1995
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
2002 StandoutNatureNobel
Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin
1997
A 11.5 Å single particle reconstruction of GroEL using EMAN
2001
Protein folding in the central cavity of the GroEL–GroES chaperonin complex
1996 Nature
A surprising simplicity to protein folding
2000 StandoutNatureNobel
The rotary mechanism of the ATP synthase
2008
Molecular Mechanism of Protein Folding in the Cell
2011 StandoutNobel
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
2000
[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
1998
Protein folding and molecular chaperones in Archaea
2001
ATP-Induced Structural Change of the Thermosome Is Temperature-Dependent
2001
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
1996
Location and Flexibility of the Unique C-Terminal Tail of Aquifex aeolicus Co-Chaperonin Protein 10 as Derived by Cryo-Electron Microscopy and Biophysical Techniques
2008
Characterization of a functionally important mobile domain of GroES
1993 Nature
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding
2001
De Novo Backbone Trace of GroEL from Single Particle Electron Cryomicroscopy
2008
Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin
2010
Conformational rearrangements of an archaeal chaperonin upon ATPase cycling
2000
A Reversible, Unidirectional Molecular Rotary Motor Driven by Chemical Energy
2005 StandoutScienceNobel
beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.
1996
Elucidation of AMPA receptor–stargazin complexes by cryo–electron microscopy
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A Cas9–guide RNA complex preorganized for target DNA recognition
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Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.
1994
Architecture of an RNA Polymerase II Transcription Pre-Initiation Complex
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Structural Insight into Nascent Polypeptide Chain–Mediated Translational Stalling
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3V: cavity, channel and cleft volume calculator and extractor
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Structure of the STRA6 receptor for retinol uptake
2016 StandoutScienceNobel
Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.
1996
A structural model for GroEL–polypeptide recognition
1997
Protein folding in the cell: competing models of chaperonin function
1996
Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein Folding
1995 Science
Structures of the CRISPR-Cmr complex reveal mode of RNA target positioning
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The Hydrophobic Nature of GroEL-Substrate Binding
1995
Chaperonin Function: Folding by Forced Unfolding
1999 Science
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
2000 StandoutScienceNobel
Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
1997
Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB
1996 Science
Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling
1996
Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution
2011 StandoutNobel
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNA Ile and Mupirocin
1999 StandoutScienceNobel
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
1998 StandoutScienceNobel
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
2002 StandoutScience
Interplay of structure and disorder in cochaperonin mobile loops.
1996
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.
1996
Molecular dynamics and protein function
2005
Linear Artificial Molecular Muscles
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Toward Intelligent Molecular Machines: Directed Motions of Biological and Artificial Molecules and Assemblies
2005
Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis
2003
Characterization of a Functional GroEL 14 (GroES 7 ) 2 Chaperonin Hetero-Oligomer
1994 Science
Single-particle selection and alignment with heavy atom cluster-antibody conjugates
1998 StandoutNobel
A thermodynamic coupling mechanism for GroEL-mediated unfolding.
1996
How chaperones tell wrong from right
1994
Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
1994 Science
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
1997
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
1998
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
2001
Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase
2003 StandoutNobel
Chaperone rings in protein folding and degradation
1999
Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle
1994 Science
Functional Significance of Symmetrical Versus Asymmetrical GroEL-GroES Chaperonin Complexes
1995 Science
The effect of macromolecular crowding on chaperonin-mediated protein folding
1997
Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae
1996 Science
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.
1994
Structure of Hexameric DnaB Helicase and Its Complex with a Domain of DnaG Primase
2007 StandoutScienceNobel
Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry
1994 Nature
The missing link between thermodynamics and structure in F 1 -ATPase
2003
Protein Assembly by Design
2021
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
2011 StandoutNobel
Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding.
1995
Works of K. Braig being referenced
Chaperonins
1998
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
1994 Nature
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
1995
Structure of bovine mitochondrial F1-ATPase inhibited by Mg2+ADP and aluminium fluoride
2000 Nobel
The structure of bovine F1‐ATPase inhibited by ADP and beryllium fluoride
2004 Nobel
The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
1996
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
1995
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
1993
The structure of bovine mitochondrial F1-ATPase: an example of rotary catalysis
1999 Nobel