Molecular Playground/Tic40
From Proteopedia
(Difference between revisions)
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| - | <Structure load='2LNM' size='500' frame='true' align='right' caption=' | + | <Structure load='2LNM' size='500' frame='true' align='right' caption='C-terminal NP-repeat domain of Tic40(2)' <scene name='User:Mine_Canakci/Sandbox_1/Tic40-np_domain/1'> |
<scene name='User:Mine_Canakci/Sandbox_1/Tic40-np_domain/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene> | <scene name='User:Mine_Canakci/Sandbox_1/Tic40-np_domain/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene> | ||
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References: | References: | ||
| - | 1- Schleiff, E. and Becker, T. (2011) Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat. Rev. Mol. Cell Biol. 12, | + | |
| + | 1- Schleiff, E. and Becker, T. (2011) Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat. Rev. Mol. Cell Biol. 12, 48-59 | ||
2- Yi-Fen Kao,Yuan-Chao Lou,Yi-Hung Yeh,Chwan-Deng Hsiao,and Chinpan Chen. (2012) Solution structure of the C-terminal NP-repeat domain of Tic40, a co-chaperone during protein import into chloroplasts. J Biochem 152(5): 443-451 | 2- Yi-Fen Kao,Yuan-Chao Lou,Yi-Hung Yeh,Chwan-Deng Hsiao,and Chinpan Chen. (2012) Solution structure of the C-terminal NP-repeat domain of Tic40, a co-chaperone during protein import into chloroplasts. J Biochem 152(5): 443-451 | ||
Revision as of 07:18, 12 December 2012
C-terminal NP-repeat domain of Tic40
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