# | Title | Journal | Year | Citations |
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1 | In vivo aspects of protein folding and quality control | Science | 2016 | 1,100 |
2 | Transient ribosomal attenuation coordinates protein synthesis and co-translational folding | Nature Structural and Molecular Biology | 2009 | 493 |
3 | Widespread Proteome Remodeling and Aggregation in Aging C. elegans | Cell | 2015 | 478 |
4 | Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry | Science | 2012 | 357 |
5 | The nucleolus functions as a phase-separated protein quality control compartment | Science | 2019 | 348 |
6 | Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s | EMBO Journal | 2006 | 310 |
7 | Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding | Cell | 2001 | 278 |
8 | Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding | Cell | 2008 | 235 |
9 | Regulation of Hsp70 Function by HspBP1 | Molecular Cell | 2005 | 185 |
10 | Coupled chaperone action in folding and assembly of hexadecameric Rubisco | Nature | 2010 | 165 |
11 | The Three-Dimensional Organization of Polyribosomes in Intact Human Cells | Molecular Cell | 2010 | 149 |
12 | Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis | Cell | 2017 | 140 |
13 | The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together | Proceedings of the National Academy of Sciences of the United States of America | 2012 | 136 |
14 | Functional Modules of the Proteostasis Network | Cold Spring Harbor Perspectives in Biology | 2020 | 133 |
15 | Identification of Nascent Chain Interaction Sites on Trigger Factor | Journal of Biological Chemistry | 2007 | 66 |
16 | GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones | Sub-Cellular Biochemistry | 2015 | 59 |
17 | Action of the Hsp70 chaperone system observed with single proteins | Nature Communications | 2015 | 58 |
18 | Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90 | Acta Crystallographica Section D: Biological Crystallography | 2011 | 57 |
19 | Chaperonin-mediated de novo generation of prion protein aggregates | Journal of Molecular Biology | 2001 | 55 |
20 | Crystal Structure of an Archaeal Actin Homolog | Journal of Molecular Biology | 2006 | 49 |
21 | Structural Basis for Subunit Assembly in UDP-glucose Pyrophosphorylase from Saccharomyces cerevisiae | Journal of Molecular Biology | 2006 | 49 |
22 | Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase | Molecular Cell | 2017 | 47 |
23 | Complex Chaperone Dependence of Rubisco Biogenesis | Biochemistry | 2018 | 43 |
24 | Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases | Photosynthesis Research | 2014 | 40 |
25 | Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein | Journal of Molecular Biology | 2010 | 38 |
26 | The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends | Nature Communications | 2021 | 37 |
27 | Rapid, Structure-Based Exploration of Pipecolic Acid Amides as Novel Selective Antagonists of the FK506-Binding Protein 51 | Journal of Medicinal Chemistry | 2016 | 31 |
28 | Functional Characterization of an Archaeal GroEL/GroES Chaperonin System | Journal of Biological Chemistry | 2004 | 28 |
29 | Sis1 potentiates the stress response to protein aggregation and elevated temperature | Nature Communications | 2020 | 28 |
30 | Sugarcoating ER Stress | Cell | 2014 | 22 |
31 | Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2 | Molecular Cell | 2019 | 18 |
32 | Chaperones and transcriptional regulation by nuclear receptors | Nature Structural Biology | 2002 | 17 |
33 | Crystal structure of phosphoribulokinase fromSynechococcussp. strain PCC 6301 | Acta Crystallographica Section F, Structural Biology Communications | 2019 | 15 |
34 | Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii | PLoS ONE | 2015 | 13 |
35 | Bacterial RF3 senses chaperone function in co-translational folding | Molecular Cell | 2021 | 9 |
36 | Structure and conformational cycle of a bacteriophage-encoded chaperonin | PLoS ONE | 2020 | 8 |
37 | Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins | Sub-Cellular Biochemistry | 2023 | 6 |
38 | Crystal structure of theThermoplasma acidophilumprotein Ta1207 | Acta Crystallographica Section F, Structural Biology Communications | 2017 | 0 |