Catalysis, commitment and encapsulation during GroE-mediated folding.

No abstract is available for this paper.

• Publication year

  1999

• Venue

  Journal of Molecular Biology

• Publication date

  1999-06-18

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1006/JMBI.1999.2780PMID 10369783
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1998cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1997influential reference
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  1997cited by this paper
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  1997cited by this paper
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  1996influential reference
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  1995influential reference
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  1995cited by this paper
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  1995influential reference
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  1994influential reference
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  1994cited by this paper
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  1994influential reference
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  1994influential reference
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  1989cited by this paper
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  1984cited by this paper
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  1983influential reference
• Correspondence analysis of aligned images of biological particles.

  1982cited by this paper
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  1976cited by this paper
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  1976cited by this paper
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  1973cited by this paper

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  2004cites this paper
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