Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rui-Ai Chu"'
Publikováno v:
Cancer Biology & Therapy. 8:161-166
RP215 monoclonal antibody was originally generated against OC-3-VGH ovarian cancer cells. It was shown to recognize specifically a carbohydrate-associated epitope(s) of cancer cell-expressed immunoglobulin heavy chains designated as CA215. Previous s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73b52e5ecefd60861717918b85a85f7f
https://doi.org/10.4161/cbt.8.2.7117
https://doi.org/10.4161/cbt.8.2.7117
Autor:
Rui-Ai Chu, Yawen Bai
Publikováno v:
Journal of Molecular Biology. 315:759-770
It has been shown that the burst-phase (submillisecond) intermediate of barnase, if it exists, can be only marginally more stable than the fully unfolded state at pH 6.3 and 25 °C. In the study reported here, no stable burst-phase intermediate could
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a5b52b9f89aa5b7a6d592fbc03a73aa8
https://doi.org/10.1006/jmbi.2001.5240
https://doi.org/10.1006/jmbi.2001.5240
Publikováno v:
Journal of Molecular Biology. 293:991-995
Folding of equine cytochrome c at a low protein concentration (26 μM) eliminated a slow kinetic phase (time constant three seconds) that was observed in the previous hydrogen exchange pulse-labeling experiments at pH 6.2 and 10 °C. It was demonstra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bfb3228adedcb64723038c312ee0cea
https://doi.org/10.1006/jmbi.1999.3226
https://doi.org/10.1006/jmbi.1999.3226
Autor:
Michelle Andrykovitch, J. Randolph Knowlton, Jiro Takei, Xinhua Ji, Andrey V. Kajava, Wuhong Pei, Rui-Ai Chu, Yawen Bai, Peter J. Steinbach
Publikováno v:
Journal of molecular biology. 323(2)
To test whether it is practical to use phage display coupled with proteolysis for protein design, we used this approach to convert a partially unfolded four-helix bundle protein, apocytochrome b562, to a stably folded four-helix bundle protein. Four
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::392aa641a86604cbeb9f89d7ef6f740d
https://pubmed.ncbi.nlm.nih.gov/12381319
https://pubmed.ncbi.nlm.nih.gov/12381319
Publikováno v:
Biochemistry. 41(25)
The hydrogen exchange behavior of a four-helix bundle protein in low concentrations of denaturant reveals some partially unfolded forms that are significantly more stable than the fully unfolded state. Kinetic folding of the protein, however, is appa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94c0b8b1fad15c2c3d26b3f96f0d734f
https://pubmed.ncbi.nlm.nih.gov/12069590
https://pubmed.ncbi.nlm.nih.gov/12069590
Barnase is one of the few protein models that has been studied extensively for protein folding. Previous studies led to the conclusion that barnase folds through a very stable submillisecond intermediate (≈3 kcal/mol). The structure of this interme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9139a1dc19ca0a93d479a807fe0e97aa
https://europepmc.org/articles/PMC27103/
https://europepmc.org/articles/PMC27103/
Publikováno v:
Biochemistry. 38(43)
The previous native-state hydrogen exchange experiment with barnase failed to detect any partially unfolded intermediate state which was contrary to the experimental results from kinetic deuterium hydrogen exchange pulse labeling and protein engineer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3054e91765029bad9271f36e31dc3992
https://pubmed.ncbi.nlm.nih.gov/10571984
https://pubmed.ncbi.nlm.nih.gov/10571984
Autor:
Takei, Jiro, Rui-Ai Chu
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 09/26/2000, Vol. 97 Issue 20, p10796, 6p, 2 Charts, 7 Graphs