A consensus structure for membrane transport

P. C. Maloney

doi:10.1016/0923-2508(90)90015-I

A consensus structure for membrane transport

P. C. Maloney

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

Abstract

Combined information from biochemical and molecular biological experiments reveals a consistent structural rhythm that underlies the construction of all membrane carriers and perhaps all transport systems. Biochemical work shows that while some carrier proteins function as monomers, others operate as dimers. But despite this variation, all examples can be modelled as having a pair of membrane-embedded domains, each of.

Original language	English (US)
Pages (from-to)	374-395
Number of pages	22
Journal	Research in Microbiology
Volume	141
Issue number	3
DOIs	https://doi.org/10.1016/0923-2508(90)90015-I
State	Published - 1990
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Molecular Biology

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10.1016/0923-2508(90)90015-I

Cite this

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title = "A consensus structure for membrane transport",

abstract = "Combined information from biochemical and molecular biological experiments reveals a consistent structural rhythm that underlies the construction of all membrane carriers and perhaps all transport systems. Biochemical work shows that while some carrier proteins function as monomers, others operate as dimers. But despite this variation, all examples can be modelled as having a pair of membrane-embedded domains, each of.",

author = "Maloney, {P. C.}",

note = "Funding Information: We thank Lyn Alkan and Mary Beth Hiller for valuablea ssistance in the preparationo f this manuscript. Work in the authors' laboratories was supported by US Public Health ServiceG rants 5-ROI-AI21702 and 2-ROI-A114176f rom the National Institute of Allergya nd Infectious Diseases (to MHS) and by the Deutsche Forschungsgemeinschaftt hrough grants Ra276/3-6 and SFB31 (to BR).",

year = "1990",

doi = "10.1016/0923-2508(90)90015-I",

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N1 - Funding Information: We thank Lyn Alkan and Mary Beth Hiller for valuablea ssistance in the preparationo f this manuscript. Work in the authors' laboratories was supported by US Public Health ServiceG rants 5-ROI-AI21702 and 2-ROI-A114176f rom the National Institute of Allergya nd Infectious Diseases (to MHS) and by the Deutsche Forschungsgemeinschaftt hrough grants Ra276/3-6 and SFB31 (to BR).

PY - 1990

Y1 - 1990

N2 - Combined information from biochemical and molecular biological experiments reveals a consistent structural rhythm that underlies the construction of all membrane carriers and perhaps all transport systems. Biochemical work shows that while some carrier proteins function as monomers, others operate as dimers. But despite this variation, all examples can be modelled as having a pair of membrane-embedded domains, each of.

AB - Combined information from biochemical and molecular biological experiments reveals a consistent structural rhythm that underlies the construction of all membrane carriers and perhaps all transport systems. Biochemical work shows that while some carrier proteins function as monomers, others operate as dimers. But despite this variation, all examples can be modelled as having a pair of membrane-embedded domains, each of.

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A consensus structure for membrane transport

Abstract

ASJC Scopus subject areas

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