4.4 Review

Chaperone discovery

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Mario Kraft et al.

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Ario de Marco et al.

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Franck Tarendeau et al.

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Chaperone-like features of bovine serum albumin:: a comparison with α-crystallin

I Marini et al.

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A cradle for new proteins: trigger factor at the ribosorne

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Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein

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FRET-based in vivo screening for protein folding and increased protein stability

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Genetic screens and directed evolution for protein solubility

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Directed evolution of substrate-optimized GroEL/S chaperonins

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DL Tucker et al.

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Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures

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Engineering soluble proteins for structural genomics

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Gene expression response to misfolded protein as a screen for soluble recombinant protein

SA Lesley et al.

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Libraries of hybrid proteins from distantly related sequences

V Sieber et al.

NATURE BIOTECHNOLOGY (2001)

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Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein

WC Wigley et al.

NATURE BIOTECHNOLOGY (2001)

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Random PCR-based screening for soluble domains using green fluorescent protein

M Kawasaki et al.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2001)

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Structure of Hsp15 reveals a novel RNA-binding motif

BL Staker et al.

EMBO JOURNAL (2000)

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Hsp 15: a ribosome-associated heat shock protein

P Korber et al.

EMBO JOURNAL (2000)