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Literature DB >> 19560414

The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner.

Abstract

In a recent issue of Molecular Cell, Feige et al. (2009) utilize the murine immunoglobulin system to shed light on a long-standing puzzle: how do cells coordinate folding of different polypeptides that ultimately form a complex?

Entities: Chemical Disease Gene Species

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Year: 2009 PMID： 19560414 PMCID： PMC2892106 DOI： 10.1016/j.molcel.2009.06.006

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

9 in total

1. Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization.

Authors: M J Thies; J Mayer; J G Augustine; C A Frederick; H Lilie; J Buchner
Journal: J Mol Biol Date: 1999-10-15 Impact factor: 5.469

Review 2. Function and structure of inherently disordered proteins.

Authors: A Keith Dunker; Israel Silman; Vladimir N Uversky; Joel L Sussman
Journal: Curr Opin Struct Biol Date: 2008-11-17 Impact factor: 6.809

Review 3. The Hsp70 and Hsp60 chaperone machines.

Authors: B Bukau; A L Horwich
Journal: Cell Date: 1998-02-06 Impact factor: 41.582

4. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

Authors: Laurent Meunier; Young-Kwang Usherwood; Kyung Tae Chung; Linda M Hendershot
Journal: Mol Biol Cell Date: 2002-12 Impact factor: 4.138

5. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein.

Authors: S Munro; H R Pelham
Journal: Cell Date: 1986-07-18 Impact factor: 41.582

1 in total

1. Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation.

Authors: Riccardo Bernasconi; Tatiana Soldà; Carmela Galli; Thomas Pertel; Jeremy Luban; Maurizio Molinari
Journal: PLoS One Date: 2010-09-28 Impact factor: 3.240

1 in total

The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner.

1. Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization.

Review 2. Function and structure of inherently disordered proteins.

Review 3. The Hsp70 and Hsp60 chaperone machines.

4. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

5. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein.

6. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

7. Immunoglobulin heavy chain binding protein.

8. Folding pathways of immunoglobulin domains. The folding kinetics of the Cgamma3 domain of human IgG1.

9. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.

1. Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation.