Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry-Reference-Cited by-同舟云学术

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Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry

Published:2005-04-21 Issue:5 Volume:2 Page:371-376
ISSN:1548-7091
Container-title:Nature Methods
language:en
Short-container-title:Nat Methods

Author:

van Duijn Esther,Bakkes Patrick J,Heeren Ron M A,van den Heuvel Robert H H,van Heerikhuizen Harm,van der Vies Saskia M,Heck Albert J R

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,Biochemistry,Biotechnology

Link

http://www.nature.com/articles/nmeth753.pdf

Reference38 articles.

1. Houry, W.A., Frishman, D., Eckerskorn, C., Lottspeich, F. & Hartl, F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147–154 (1999).

2. Hartl, F.U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852–1858 (2002).

3. Ellis, R.J. Molecular chaperones: inside and outside the Anfinsen cage. Curr. Biol. 11, R1038–R1040 (2001).

4. Sigler, P.B. et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581–608 (1998).

5. Walters, C., Errington, N., Rowe, A.J. & Harding, S.E. Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10. Biochem. J. 364, 849–855 (2002).

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