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Article

alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.

The Journal of biological chemistry - 14 Jul 1995

Lomas D A, Elliott P R, Sidhar S K, Foreman R C, Finch J T, Cox D W, Whisstock J C, Carrell R W

Abstract excerpt

The Z (Glu342-->Lys) and Siiyama (Ser53-->Phe) deficiency variants of alpha 1-antitrypsin result in the retention of protein in the endoplasmic reticulum of the hepatocyte by loop-sheet polymerization in which the reactive center loop of one molecule is inserted into a beta-pleated sheet of a second. We show here that antitrypsin Mmalton (Phe52-deleted), which is associated with the same liver inclusions, is also...

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PMID: 7622502
DOI: 10.1074/jbc.270.28.16864

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.PMID 7622502Read ↗

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Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.Semantic proximity Read ↗

Alpha 1-antitrypsin Siiyama (Ser53-->Phe). Further evidence for intracellular loop-sheet polymerization.Semantic proximity Read ↗

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