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Methods in Enzymology
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March 12, 2002
Protein disulfide isomerase as an enzyme and a chaperone in protein folding
Chih-Chen Wang
Trends in Biochemical Sciences
|
July 23, 2022
Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum
Lei Wang, Chih-Chen Wang
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|
August 9, 2002
Post-genome Study----Proteomics
Chih-Chen Wang, Chen-Lu Tsou
Cell Stress & Chaperones
|
December 5, 2009
Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation
Han Cheng, Lei Wang, Chih-chen Wang
The Biochemical Journal
|
November 25, 2010
The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation
Lei Wang, Li Zhu, Chih-chen Wang
Free Radical Biology & Medicine
|
February 21, 2015
Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone
Lei Wang, Xi Wang, Chih-chen Wang
Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|
November 6, 2020
Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions
Lei Wang, Jiaojiao Yu, Chih-Chen Wang
Protein Expression and Purification
|
June 9, 2005
A new method for purification of recombinant human alpha-synuclein in Escherichia coli
Chunjuan Huang, Guoping Ren, Hui Zhou, et al.
The Journal of Biological Chemistry
|
April 26, 2005
The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity: a small angle X-ray scattering study in solution
Yuan-yuan Shi, Xin-guo Hong, Chih-chen Wang
Journal of Protein Chemistry
|
December 24, 2003
Effects of macromolecular crowding on the unfolding and the refolding of D-glyceraldehyde-3-phosophospate dehydrogenase
Guoping Ren, Zong Lin, Chen-lu Tsou, et al.
Page
of 6
Search research articles
Search
Showing results (1-10 of 56) with videos related to
Sort By:
Page
of 6
Methods in Enzymology
|
March 12, 2002
Protein disulfide isomerase as an enzyme and a chaperone in protein folding
Chih-Chen Wang
Trends in Biochemical Sciences
|
July 23, 2022
Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum
Lei Wang, Chih-Chen Wang
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|
August 9, 2002
Post-genome Study----Proteomics
Chih-Chen Wang, Chen-Lu Tsou
Cell Stress & Chaperones
|
December 5, 2009
Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation
Han Cheng, Lei Wang, Chih-chen Wang
The Biochemical Journal
|
November 25, 2010
The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation
Lei Wang, Li Zhu, Chih-chen Wang
Free Radical Biology & Medicine
|
February 21, 2015
Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone
Lei Wang, Xi Wang, Chih-chen Wang
Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|
November 6, 2020
Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions
Lei Wang, Jiaojiao Yu, Chih-Chen Wang
Protein Expression and Purification
|
June 9, 2005
A new method for purification of recombinant human alpha-synuclein in Escherichia coli
Chunjuan Huang, Guoping Ren, Hui Zhou, et al.
The Journal of Biological Chemistry
|
April 26, 2005
The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity: a small angle X-ray scattering study in solution
Yuan-yuan Shi, Xin-guo Hong, Chih-chen Wang
Journal of Protein Chemistry
|
December 24, 2003
Effects of macromolecular crowding on the unfolding and the refolding of D-glyceraldehyde-3-phosophospate dehydrogenase
Guoping Ren, Zong Lin, Chen-lu Tsou, et al.
Page
of 6