Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport.

No abstract is available for this paper.

• Publication year

  1996

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1996-09-03

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/PNAS.93.18.9606PMID 8790377PMCID PMC38475
• 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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  1996cited by this paper
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  1995cited by this paper
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  1995cited by this paper
• Inefficient Membrane Targeting, Translocation, and Proteolytic Processing by Signal Peptidase of a Mutant Preproparathyroid Hormone Protein (*)

  1995cited by this paper
• A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane.

  1995cited by this paper
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  1995cited by this paper
• Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

  1994cited by this paper
• Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences.

  1994cited by this paper
• Subcellular localization and targeting of cathepsin E.

  1994cited by this paper
• Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90).

  1994cited by this paper
• Retention of unassembled components of integral membrane proteins by calnexin.

  1994cited by this paper
• Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding

  1993cited by this paper
• Association of folding intermediates of glycoproteins with calnexin during protein maturation

  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1992cited by this paper
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  1990cited by this paper
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  1989cited by this paper
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