Crystal packing analysis of murine VDAC1 crystals in a lipidic environment reveals novel insights on oligomerization and orientation.

Channels (Austin, Tex.)

Volumn 3, Issue 3, 2009, Pages 167-170

  Ujwal, Rachna ^a   Cascio, Duilio ^b   Chaptal, Vincent ^b   Ping, Peipei ^b   Abramson, Jeff ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE LIPID; VDAC1 PROTEIN, MOUSE; VOLTAGE DEPENDENT ANION CHANNEL 1;

ANIMAL; ARTICLE; CHEMISTRY; METABOLISM; MOUSE; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; MEMBRANE LIPIDS; MICE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; VOLTAGE-DEPENDENT ANION CHANNEL 1;

EID: 72449124917     PISSN: None     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.3.3.9196     Document Type: Article

References (0)