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Literature DB >> 23062952

You got to know when to hold (or unfold) 'em….

Daniel N Hebert¹, Kshama D Chandrasekhar, Lila M Gierasch.

Abstract

In this issue of Molecular Cell, Hoffmann et al. (2012) demonstrate that the ribosome-associated bacterial chaperone Trigger Factor assists in the maturation of ribosome-attached nascent chains by acting as both a holdase and an unfoldase.

Entities: Chemical Species

Year: 2012 PMID： 23062952 PMCID： PMC3491977 DOI： 10.1016/j.molcel.2012.09.022

Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970

9 in total

1. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.

Authors: Lars Ferbitz; Timm Maier; Holger Patzelt; Bernd Bukau; Elke Deuerling; Nenad Ban
Journal: Nature Date: 2004-08-29 Impact factor: 49.962

2. Trigger factor forms a protective shield for nascent polypeptides at the ribosome.

Authors: Anja Hoffmann; Frieder Merz; Anna Rutkowska; Beate Zachmann-Brand; Elke Deuerling; Bernd Bukau
Journal: J Biol Chem Date: 2006-01-05 Impact factor: 5.157

3. Folding zones inside the ribosomal exit tunnel.

Authors: Jianli Lu; Carol Deutsch
Journal: Nat Struct Mol Biol Date: 2005-11-20 Impact factor: 15.369

Review 4. Structure and function of the molecular chaperone Trigger Factor.

Authors: Anja Hoffmann; Bernd Bukau; Günter Kramer
Journal: Biochim Biophys Acta Date: 2010-02-02

5. The ribosome modulates nascent protein folding.

Authors: Christian M Kaiser; Daniel H Goldman; John D Chodera; Ignacio Tinoco; Carlos Bustamante
Journal: Science Date: 2011-12-23 Impact factor: 47.728

6. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.

Authors: E Crooke; W Wickner
Journal: Proc Natl Acad Sci U S A Date: 1987-08 Impact factor: 11.205

7. Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo.

Authors: Eugene Oh; Annemarie H Becker; Arzu Sandikci; Damon Huber; Rachna Chaba; Felix Gloge; Robert J Nichols; Athanasios Typas; Carol A Gross; Günter Kramer; Jonathan S Weissman; Bernd Bukau
Journal: Cell Date: 2011-12-09 Impact factor: 41.582

8. Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.

Authors: Marta del Alamo; Daniel J Hogan; Sebastian Pechmann; Veronique Albanese; Patrick O Brown; Judith Frydman
Journal: PLoS Biol Date: 2011-07-12 Impact factor: 8.029

9. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

Authors: G Stoller; K P Rücknagel; K H Nierhaus; F X Schmid; G Fischer; J U Rahfeld
Journal: EMBO J Date: 1995-10-16 Impact factor: 11.598

9 in total

2 in total

Review 1. Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.

Authors: Rayees U H Mattoo; Pierre Goloubinoff
Journal: Cell Mol Life Sci Date: 2014-04-24 Impact factor: 9.261

Review 2. Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?

Authors: Irina Sorokina; Arcady R Mushegian; Eugene V Koonin
Journal: Int J Mol Sci Date: 2022-01-04 Impact factor: 5.923

2 in total