Reconstitution of outer membrane protein assembly from purified components.
Reconstitution of outer membrane protein assembly from purified components.
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DOI：
10.1126/science.1188919
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发表时间：
2010-05-14
期刊：
影响因子：
--
通讯作者：
Kahne D
中科院分区：
文献类型：
--
作者：
Hagan CL;Kim S;Kahne D
β-barrel membrane proteins in Gram-negative bacteria, mitochondria, and chloroplasts are assembled by highly conserved multi-protein complexes. The mechanism by which these molecular machines fold and insert their substrates is poorly understood. It has not been possible to dissect the folding and insertion pathway because the process has not been reproduced in a biochemical system. We purified the components that fold and insert E. coli outer membrane proteins and reconstituted β-barrel protein assembly in proteoliposomes using the enzymatic activity of a protein substrate to report on its folding state. The assembly of this protein occurred without an energy source but required a soluble chaperone in addition to the multi-protein assembly complex.
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DOI：
10.1073/pnas.96.2.784
发表时间：
1999-01-19
影响因子：
11.1
作者：
Reumann, S;Davila-Aponte, J;Keegstra, K
通讯作者：
Keegstra, K
影响因子：
64.5
作者：
GORLICH, D;RAPOPORT, TA
通讯作者：
RAPOPORT, TA
影响因子：
56.9
作者：
Voulhoux, R;Bos, MP;Tommassen, J
通讯作者：
Tommassen, J
影响因子：
56.9
作者：
Kim, Seokhee;Malinverni, Juliana C.;Kahne, Daniel
通讯作者：
Kahne, Daniel
DOI：
10.1046/j.1432-1327.2000.01073.x
发表时间：
2000-02-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Kramer, RA;Zandwijken, D;Dekker, N
通讯作者：
Dekker, N