Membrane proteins bind lipids selectively to modulate their structure and function

Nature

Volumn 510, Issue 7503, 2014, Pages 172-175

  Laganowsky, Arthur ^a   Reading, Eamonn ^a   Allison, Timothy M ^a   Ulmschneider, Martin B ^b   Degiacomi, Matteo T ^a   Baldwin, Andrew J ^a   Robinson, Carol V ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b Whiting School of Engineering   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; CARDIOLIPIN; MEMBRANE PROTEIN; PHOSPHATIDYLGLYCEROL;

EXPERIMENTAL STUDY; FUNCTIONAL ROLE; LIPID; MASS SPECTROMETRY; MEMBRANE; MICROBIAL ACTIVITY; PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; DRUG BINDING; ESCHERICHIA COLI; LIPID BILAYER; LIPID MEMBRANE; MASS SPECTROMETRY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMMONIA; APOPROTEINS; AQUAPORINS; BACTERIAL PROTEINS; CARDIOLIPINS; CATION TRANSPORT PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; ION CHANNELS; LIPID BILAYERS; MASS SPECTROMETRY; MEMBRANE LIPIDS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PHOSPHATIDYLGLYCEROLS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; SUBSTRATE SPECIFICITY;

EID: 84901936908     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13419     Document Type: Article

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