Literature DB >> 723278

Spectrin binding and the control of membrane protein mobility.

S R Goodman, D Branton.   

Abstract

Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles.

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Year:  1978        PMID: 723278     DOI: 10.1002/jss.400080408

Source DB:  PubMed          Journal:  J Supramol Struct        ISSN: 0091-7419


  4 in total

1.  Abnormalities in the erythrocyte membrane in acute lymphoid leukaemia.

Authors:  M Kundu; J Basu; P Chakrabarti; M M Rakshit
Journal:  Biochem J       Date:  1989-03-15       Impact factor: 3.857

2.  Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.

Authors:  J Yu; S R Goodman
Journal:  Proc Natl Acad Sci U S A       Date:  1979-05       Impact factor: 11.205

3.  Identification of a spectrin-like protein in nonerythroid cells.

Authors:  S R Goodman; I S Zagon; R R Kulikowski
Journal:  Proc Natl Acad Sci U S A       Date:  1981-12       Impact factor: 11.205

4.  Characterization and localization of a flagellar-specific membrane glycoprotein in Euglena.

Authors:  A A Rogalski; G B Bouck
Journal:  J Cell Biol       Date:  1980-08       Impact factor: 10.539

  4 in total

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