Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Renee D, Jiji"'
Publikováno v:
Journal of Raman Spectroscopy. 53:58-68
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e31decb791ecb94281bc138b3299fcdc
https://doi.org/10.1002/jrs.6252
https://doi.org/10.1002/jrs.6252
Autor:
Jian Xiong, Renee D. JiJi
Publikováno v:
Biophysical Chemistry. 220:42-48
The hydrophobic fragment of the Alzheimer's related β-amyloid (Aβ) peptide, Aβ(25-40), aggregates and forms insoluble amyloid fibrils at a rate similar to the full-length peptide. In order to gain insight into the fibrillization of Aβ(25-40) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2460cfae5b6f229a02aa07703481bce1
https://doi.org/10.1016/j.bpc.2016.11.003
https://doi.org/10.1016/j.bpc.2016.11.003
Autor:
Haolin Liu, Jing Wang, Gongyi Zhang, Yang Wang, Xiaoxue Yan, Xia Hong, Jian Xiong, Shaodong Dai, Chengyu Jiang, Zhangguo Chen, Schuyler Lee, Michal Hammel, Renee D. JiJi, Chao Wang
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The yield of protein refolding is reciprocal to the number of proline residues in the target protein. Hydrogen bonds are the primary driving force for de novo protein folding
The protein-folding mechanism remains a major puzzle in life science.
The protein-folding mechanism remains a major puzzle in life science.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d690a36eea51451ccca2365469d3b98
https://pubmed.ncbi.nlm.nih.gov/29199976
https://pubmed.ncbi.nlm.nih.gov/29199976
Autor:
Renee D. JiJi, Olayinka O. Oshokoya
Publikováno v:
Analytica Chimica Acta. 892:59-68
Protein secondary structural analysis is important for understanding the relationship between protein structure and function, or more importantly how changes in structure relate to loss of function. The structurally sensitive protein vibrational mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd399fdbb8ebaea88b2a801961ebb427
https://doi.org/10.1016/j.aca.2015.08.035
https://doi.org/10.1016/j.aca.2015.08.035
Autor:
Haolin Liu, Chengyu Jiang, Shaodong Dai, Michal Hammel, Schuyler Lee, Yang Wang, Xia Hong, Jian Xiong, Jing Wang, Gongyi Zhang, Chao Wang, Xiaoxue Yan, Renee D. JiJi, Zhangguo Chen
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The protein-folding mechanism remains a major puzzle in life science. Purified soluble activation-induced cytidine deaminase (AID) is one of the most difficult proteins to obtain. Starting from inclusion bodies containing a C-terminally truncated ver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e9369cadddf9690fe99a81ae80cd769
https://pubmed.ncbi.nlm.nih.gov/29652265
https://pubmed.ncbi.nlm.nih.gov/29652265
Autor:
Renee D. JiJi, Alaa Abdine, Adam Schaffner, José L. Chávez, Jason W. Cooley, Roman Osman, Mia Brown, Iban Ubarretxena-Belandia, Brian Lada, Celia Torres-Arancivia
Publikováno v:
Biophysical journal. 114(7)
Intramembrane-cleaving proteases (I-CLiPs) activate pools of single-pass helical membrane protein signaling precursors that are key in the physiology of prokaryotic and eukaryotic cells. Proteases typically cleave peptide bonds within extended or fle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5e6d6d5721855a6a263c5c3afa59ebe
https://pubmed.ncbi.nlm.nih.gov/29642028
https://pubmed.ncbi.nlm.nih.gov/29642028
Autor:
Renee D. JiJi, Alaa Abdine, Iban Ubarretxena-Belandia, José L. Chávez, Bryan M. Lada, Mia Brown, Jason W. Cooley
We present a new method based on deep-UV resonance Raman spectroscopy to determine the backbone conformation of intramembrane protease substrates. The classical amide vibrational modes reporting on the conformation of just the transmembrane region of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74b2f3c160987251d387d8152d595343
https://doi.org/10.1016/bs.mie.2016.10.030
https://doi.org/10.1016/bs.mie.2016.10.030
Publikováno v:
Anal. Methods. 6:1691-1699
Determination of protein secondary structure (α-helical, β-sheet, and disordered motifs) has become an area of great importance in biochemistry and biophysics as protein secondary structure is directly related to protein function and protein relate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f964e7395f9699b8050a843aa6f8e18
https://doi.org/10.1039/c3ay42032a
https://doi.org/10.1039/c3ay42032a
Publikováno v:
Journal of Raman Spectroscopy. 44:957-962
The molten globule state can aide in the folding of a protein to a functional structure and is loosely defined as an increase in structural disorder with conservation of the ensemble secondary structure content. Simultaneous observation of persistent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::71d28ab7823b06eb201701cfa2b2c2b8
https://doi.org/10.1002/jrs.4316
https://doi.org/10.1002/jrs.4316
Autor:
Barry K. Lavine, Steven D. Brown, Karl S. Booksh, Svante Wold, William S. Rayens, Peter D. Wentzell, L. Scott Ramos, Jon Nuwer, Gregory L. Glass, Amrita Malik, Anna de Juan, Roma Tauler, Philip K. Hopke, Liyuan Chen, Collin White, Matthew Allen, Ayuba Fasasi, Jonathan Palmer, John H. Kalivas, Joshua Ottaway, Joseph P. Smith, Jerome J. Workman, Jeffrey A. Cramer, Olayinka O. Oshokoya, Renee D. JiJi, Frank Vogt