Folding of newly translated proteins in vivo: the role of molecular chaperones.

By Judith Frydman. Annual Review of Biochemistry, 2001

1,218 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/99ed6bfd378b6063523c1c56adc589efb3b26efc

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

In Molecular Biology

Citations in the corpus

Molecular chaperones in protein folding and proteostasis (2011, background): “Among these are several essential proteins, such as actins and tubulin”
The roles of conditional disorder in redox proteins (2013, background): “However, one of the hallmarks of many chaperone client proteins is that they have hydrophobic surfaces, which are transiently exposed, prone to aggregation, and in need of protection [31].”
Converging concepts of protein folding in vitro and in vivo (2009, background): “Principles of chaperone pathways in de novo folding The chaperone pathways and networks acting in protein folding in the cytosol follow general organizational rule”
Heat shock protein 70 regulates the abscisic acid-induced antioxidant response of maize to combined drought and heat stress (2010, background): “HSP70 is one of the major classes of chaperone molecules and is involved in a variety of tasks in eukaryotic cells (Frydman 2001; Hartl and Hayer-Hartl 2002; Neupert and Brunner 2002; Mayer 2005; Bukau et al. 2006; Voellmy and Boellmann 2007).”
Protein degradation and protection against misfolded or damaged proteins (2003, background): “Degradation of newly synthesized proteins The folding of newly synthesized proteins to their proper conformations involves the sequential actions of multiple molecular chaperone”
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “The Hsp70 chaperone system: The Hsp70 chaperone is the “workhorse” chaperone of eukaryotic cells [bacterial cells rely to a greater extent on the Hsp60/chaperonin family (GroEL/ES)], that interacts with proteins at all stages in Heat and Oxidant Resistance 1163 their lifetimes (Frydman 2001).”
Properties, Potentials, and Prospects of Antifreeze Proteins (2008, methodology): “…have also been made to solubilize heterologous proteins expressed as inclusion bodies by the use of in vitro folding methods after denaturation of inclusion bodies (for a review, see Frydman, 2001; Schlieker et al., 2002; Baneyx and Mujacic, 2004; Tan and Bardwell, 2004; Young et al., 2004).”
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. (2005, background): “Molecular chaperones protect newly synthesized or stressdenatured polypeptides from misfolding and aggregating in the highly crowded cellular environment, often in an ATP-driven process (Frydman, 2001; Hartl and Hayer-Hartl, 2002).”
Molecular Simulations of Cotranslational Protein Folding: Fragment Stabilities, Folding Cooperativity, and Trapping in the Ribosome (2006, neutral): “]. First, a variety of chaperonins play prominent roles in preventing or reversing misfolding and aggregation [”
Some like it hot, some like it cold: the heat shock response is found in New Zealand but not Antarctic notothenioid fishes (2005, background): “These chaperones are significant because, given that most new proteins require some chaperone assistance to fold properly (Frydman, 2001), Antarctic fish still require cognate members of the HSP gene families in order to perform protein biosynthesis.”