Molecular insights into lipid-assisted Ca 2+ regulation of the TRP channel Polycystin-2

Nature Structural and Molecular Biology

Volumn 24, Issue 2, 2017, Pages 123-130

  Wilkes, Martin ^a   Madej, M Gregor ^b   Kreuter, Lydia ^b,e   Rhinow, Daniel ^a   Heinz, Veronika ^b   De Sanctis, Silvia ^b   Ruppel, Sabine ^b   Richter, Rebecca M ^b   Joos, Friederike ^a   Grieben, Marina ^c   Pike, Ashley C W ^c   Huiskonen, Juha T ^d   Carpenter, Elisabeth P ^c   Kühlbrandt, Werner ^a   Witzgall, Ralph ^b   Ziegler, Christine ^b  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b Faculty of Biology and Preclinical Medicine   (Germany)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

^e UNIVERSITY OF MARYLAND CENTER FOR ENVIRONMENTAL SCIENCE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CALCIUM; CALCIUM ION; DISULFIDE; LIPID; POLYCYSTIN 2; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; POLYCYSTIC KIDNEY DISEASE 2 PROTEIN; POLYCYSTIN; PROTEIN BINDING;

AFFINITY CHROMATOGRAPHY; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CALCIUM CONDUCTANCE; CALCIUM METABOLISM; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; CRYSTALLOID; HUMAN; IMMUNOGOLD LABELING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN GLYCOSYLATION; PROTEIN LIPID INTERACTION; PROTEIN PURIFICATION; REGULATORY MECHANISM; SCANNING ELECTRON MICROSCOPY; WESTERN BLOTTING; ALPHA HELIX; CALCIUM SIGNALING; CHEMISTRY; GLYCOSYLATION; HEK293 CELL LINE; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN QUATERNARY STRUCTURE;

BINDING SITES; CALCIUM; CALCIUM SIGNALING; CRYOELECTRON MICROSCOPY; GLYCOSYLATION; HEK293 CELLS; HUMANS; MODELS, MOLECULAR; PHOSPHATIDIC ACIDS; PHOSPHATIDYLCHOLINES; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN DOMAINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; TRPP CATION CHANNELS;

EID: 85009831976     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3357     Document Type: Article

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