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January 1, 1992Journal of Biological ChemistryOpen Access

Soluble aggregates of the human PiZ alpha 1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis.

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Authors

ALA. LeMichael E. DeBakey VA Medical CenterGFG.A. FerrellBaylor College of MedicineDDD S DishonBaylor College of Medicine

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Cite This Study

Le et al. (1992) studied this question.

synapsesocial.com/papers/6a7c4b0508aec7c88ca160a1https://doi.org/10.1016/s0021-9258(18)48397-4
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP1990 · 125 citations
  2. 2Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases.1982 · 286 citations
  3. 3Tissue specific expression of the human alpha-1-antitrypsin gene in transgenic mice1987 · 120 citations
  4. 4Nonlysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor subunits: a TLCK- and TPCK-sensitive cleavage within the ER.1991 · 75 citations
  5. 5A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum.1988 · 216 citations