A citation-based method for searching scientific literature

David Balchin, Manajit Hayer-Hartl, F Ulrich Hartl. Science 2016
Times Cited: 677







List of co-cited articles
687 articles co-cited >1



Times Cited
  Times     Co-cited
Similarity


Molecular chaperones in protein folding and proteostasis.
F Ulrich Hartl, Andreas Bracher, Manajit Hayer-Hartl. Nature 2011
18

Adapting proteostasis for disease intervention.
William E Balch, Richard I Morimoto, Andrew Dillin, Jeffery W Kelly. Science 2008
15

Molecular chaperone functions in protein folding and proteostasis.
Yujin E Kim, Mark S Hipp, Andreas Bracher, Manajit Hayer-Hartl, F Ulrich Hartl. Annu Rev Biochem 2013
861
11

The Hsp70 chaperone network.
Rina Rosenzweig, Nadinath B Nillegoda, Matthias P Mayer, Bernd Bukau. Nat Rev Mol Cell Biol 2019
328
11


Pathways of cellular proteostasis in aging and disease.
Courtney L Klaips, Gopal Gunanathan Jayaraj, F Ulrich Hartl. J Cell Biol 2018
324
9

The biology of proteostasis in aging and disease.
Johnathan Labbadia, Richard I Morimoto. Annu Rev Biochem 2015
673
9

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Harm H Kampinga, Elizabeth A Craig. Nat Rev Mol Cell Biol 2010
9

The proteostasis network and its decline in ageing.
Mark S Hipp, Prasad Kasturi, F Ulrich Hartl. Nat Rev Mol Cell Biol 2019
373
8


The heat shock response: life on the verge of death.
Klaus Richter, Martin Haslbeck, Johannes Buchner. Mol Cell 2010
7

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.
Daniel Mateju, Titus M Franzmann, Avinash Patel, Andrii Kopach, Edgar E Boczek, Shovamayee Maharana, Hyun O Lee, Serena Carra, Anthony A Hyman, Simon Alberti. EMBO J 2017
234
7

Converging concepts of protein folding in vitro and in vivo.
F Ulrich Hartl, Manajit Hayer-Hartl. Nat Struct Mol Biol 2009
721
7


Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.
Jack M Webster, April L Darling, Vladimir N Uversky, Laura J Blair. Front Pharmacol 2019
56
12

DnaK functions as a central hub in the E. coli chaperone network.
Giulia Calloni, Taotao Chen, Sonya M Schermann, Hung-Chun Chang, Pierre Genevaux, Federico Agostini, Gian Gaetano Tartaglia, Manajit Hayer-Hartl, F Ulrich Hartl. Cell Rep 2012
220
6

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease.
Marc Brehme, Cindy Voisine, Thomas Rolland, Shinichiro Wachi, James H Soper, Yitan Zhu, Kai Orton, Adriana Villella, Dan Garza, Marc Vidal,[...]. Cell Rep 2014
291
6

A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.
Massimo Ganassi, Daniel Mateju, Ilaria Bigi, Laura Mediani, Ina Poser, Hyun O Lee, Samuel J Seguin, Federica F Morelli, Jonathan Vinet, Giuseppina Leo,[...]. Mol Cell 2016
167
6

Recent advances in understanding catalysis of protein folding by molecular chaperones.
David Balchin, Manajit Hayer-Hartl, F Ulrich Hartl. FEBS Lett 2020
36
16

The hallmarks of aging.
Carlos López-Otín, Maria A Blasco, Linda Partridge, Manuel Serrano, Guido Kroemer. Cell 2013
6

Protein misfolding, functional amyloid, and human disease.
Fabrizio Chiti, Christopher M Dobson. Annu Rev Biochem 2006
6


Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging.
Anat Ben-Zvi, Elizabeth A Miller, Richard I Morimoto. Proc Natl Acad Sci U S A 2009
446
6

Highly accurate protein structure prediction with AlphaFold.
John Jumper, Richard Evans, Alexander Pritzel, Tim Green, Michael Figurnov, Olaf Ronneberger, Kathryn Tunyasuvunakool, Russ Bates, Augustin Žídek, Anna Potapenko,[...]. Nature 2021
6

HSP90 at the hub of protein homeostasis: emerging mechanistic insights.
Mikko Taipale, Daniel F Jarosz, Susan Lindquist. Nat Rev Mol Cell Biol 2010
5


The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.
Manajit Hayer-Hartl, Andreas Bracher, F Ulrich Hartl. Trends Biochem Sci 2016
182
5

Proteasomal and Autophagic Degradation Systems.
Ivan Dikic. Annu Rev Biochem 2017
497
5


Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
Roman Kityk, Jürgen Kopp, Irmgard Sinning, Matthias P Mayer. Mol Cell 2012
269
5


Structural analysis of substrate binding by the molecular chaperone DnaK.
X Zhu, X Zhao, W F Burkholder, A Gragerov, C M Ogata, M E Gottesman, W A Hendrickson. Science 1996
960
5

Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.
Nitika, Corey M Porter, Andrew W Truman, Matthias C Truttmann. J Biol Chem 2020
62
8

Protein Misfolding Diseases.
F Ulrich Hartl. Annu Rev Biochem 2017
200
5


Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
Prajwal Ciryam, Gian Gaetano Tartaglia, Richard I Morimoto, Christopher M Dobson, Michele Vendruscolo. Cell Rep 2013
170
5

Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling.
Olivier Genest, Joel R Hoskins, Jodi L Camberg, Shannon M Doyle, Sue Wickner. Proc Natl Acad Sci U S A 2011
83
4

The chaperone network connected to human ribosome-associated complex.
Himjyot Jaiswal, Charlotte Conz, Hendrik Otto, Tina Wölfle, Edith Fitzke, Matthias P Mayer, Sabine Rospert. Mol Cell Biol 2011
60
6

Heat shock factors: integrators of cell stress, development and lifespan.
Malin Akerfelt, Richard I Morimoto, Lea Sistonen. Nat Rev Mol Cell Biol 2010
842
4

Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation.
Zhenying Liu, Shengnan Zhang, Jinge Gu, Yilun Tong, Yichen Li, Xinrui Gui, Houfang Long, Chuchu Wang, Chunyu Zhao, Jinxia Lu,[...]. Nat Struct Mol Biol 2020
49
8

The ribosome modulates nascent protein folding.
Christian M Kaiser, Daniel H Goldman, John D Chodera, Ignacio Tinoco, Carlos Bustamante. Science 2011
190
4

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.
Pierre Goloubinoff, Alberto S Sassi, Bruno Fauvet, Alessandro Barducci, Paolo De Los Rios. Nat Chem Biol 2018
45
8

Mechanisms and Functions of Spatial Protein Quality Control.
Emily Mitchell Sontag, Rahul S Samant, Judith Frydman. Annu Rev Biochem 2017
134
4

Biological and chemical approaches to diseases of proteostasis deficiency.
Evan T Powers, Richard I Morimoto, Andrew Dillin, Jeffery W Kelly, William E Balch. Annu Rev Biochem 2009
772
4

Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.
Rishika Kundra, Prajwal Ciryam, Richard I Morimoto, Christopher M Dobson, Michele Vendruscolo. Proc Natl Acad Sci U S A 2017
48
8

Progressive disruption of cellular protein folding in models of polyglutamine diseases.
Tali Gidalevitz, Anat Ben-Zvi, Kim H Ho, Heather R Brignull, Richard I Morimoto. Science 2006
471
4

Aging as an event of proteostasis collapse.
Rebecca C Taylor, Andrew Dillin. Cold Spring Harb Perspect Biol 2011
302
4

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.
Eric B Bertelsen, Lyra Chang, Jason E Gestwicki, Erik R P Zuiderweg. Proc Natl Acad Sci U S A 2009
317
4

Differential scales of protein quality control.
Suzanne Wolff, Jonathan S Weissman, Andrew Dillin. Cell 2014
166
4

The integrated stress response: From mechanism to disease.
Mauro Costa-Mattioli, Peter Walter. Science 2020
259
4


Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.