ArticleImmunogenetics1991
Variations in the cytoplasmic region account for the heterogeneity of the chicken MHC class I (B-F) molecules.
Article in Immunogenetics, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Surveillance Imaging following Endovascular Aneurysm Repair: State of the Art.Seminars in interventional radiology · 2020Review
- Peptide motifs of the single dominantly expressed class I molecule explain the striking MHC-determined response to Rous sarcoma virus in chickens.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- The relocalization of v-Rel from the nucleus to the cytoplasm coincides with induction of expression of Ikba and nfkb1 and stabilization of I kappa B-alpha.Journal of virology · 1995Article
- In vivo evolution of c-rel oncogenic potential.Journal of virology · 1994Article
- Molecular analysis reveals MHC class I intra-locus recombination in the chicken.Immunogenetics · 1994Article
- v-rel induces expression of three avian immunoregulatory surface receptors more efficiently than c-rel.Journal of virology · 1994Article
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
Molecular variation among major histocompatibility complex (MHC) class I (B-F) proteins from B-homozygous chickens is apparently caused by C-terminal variation. Analysis of the total B-F protein pool revealed substantial heterogeneity with two or three molecular mass constituents, each being comprised by several isoelectric focusing variants. This heterogeneity could not be reduced by enzymatic deglycosylation. By contrast, proteolytic removal of a small (Mr 1000-4000) fragment from the alpha chain resulted in the generation of a Mr 36,000 fragment, common to all the molecular mass variants. Unlike the parent proteins, the Mr 36,000 fragment derived from isolated variants yielded identical, simple patterns in two-dimensional gel electrophoresis and identical finger prints in peptide mapping. This, together with N-terminal amino acid sequencing, as well as comparison of hydrophobicity properties of fragments obtained by gradual proteolytic digestion, indicated that the small peptide responsible for the major B-F heterogeneity was situated in the intracellular, C-terminal part.
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