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FEBS Letters
|
November 25, 2003
Membrane protein folding: beyond the two stage model
Donald M Engelman, Yang Chen, Chen-Ni Chin, et al.
Journal of the American Chemical Society
|
August 20, 2008
Using alpha-helical coiled-coils to design nanostructured metalloporphyrin arrays
Karen A McAllister, Hongling Zou, Frank V Cochran, et al.
The EMBO Journal
|
December 25, 2015
BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes
Zhi Zhang, Sabareesh Subramaniam, Justin Kale, et al.
The Journal of Biological Chemistry
|
December 14, 2017
The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions
Samson G F Condon, Deena-Al Mahbuba, Claire R Armstrong, et al.
Nature Communications
|
July 18, 2015
Inside-out Ca(2+) signalling prompted by STIM1 conformational switch
Guolin Ma, Ming Wei, Lian He, et al.
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Search research articles
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Showing results (31-40 of 35) with videos related to
Sort By:
Page
of 4
You have reached the last page of results.
This site can display upto 35 results.
FEBS Letters
|
November 25, 2003
Membrane protein folding: beyond the two stage model
Donald M Engelman, Yang Chen, Chen-Ni Chin, et al.
Journal of the American Chemical Society
|
August 20, 2008
Using alpha-helical coiled-coils to design nanostructured metalloporphyrin arrays
Karen A McAllister, Hongling Zou, Frank V Cochran, et al.
The EMBO Journal
|
December 25, 2015
BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes
Zhi Zhang, Sabareesh Subramaniam, Justin Kale, et al.
The Journal of Biological Chemistry
|
December 14, 2017
The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions
Samson G F Condon, Deena-Al Mahbuba, Claire R Armstrong, et al.
Nature Communications
|
July 18, 2015
Inside-out Ca(2+) signalling prompted by STIM1 conformational switch
Guolin Ma, Ming Wei, Lian He, et al.
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of 4