Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Krishnaswamy S Kumar"'
Autor:
Tushar Vachharajani, Sanjiv Jasuja, Ali AlSahow, Saeed M G. Alghamdi, Ali H Al-Aradi, Issa Al Salmi, Bassam Bernieh, Yousif Bahbahani, Fadwa Alali, Raja Ramachandran, Suceena Alexander, Sandeep K Mandal, Rajeev K Malhotra, Manisha Sahay, Vinant Bhargava, Vivekanand Jha, Devendra Singh Rana, Gaurav Sagar, Anupam Bahl, Vijay Kher, Narayan Prasad, Krishnaswamy S Kumar, Mona Alrukhaimi, Gloria E Ashuntantang, Shalini Verma, Maurizio Gallieni
Publikováno v:
Saudi Journal of Kidney Diseases and Transplantation, Vol 32, Iss 4, Pp 1073-1088 (2021)
There is a paucity of data on epidemiology along with an incomplete registry of end-stage kidney disease (ESKD), nephrologist workforce, and variability among the countries of Gulf Cooperation Council (GCC). The study is an observation, descriptive s
Externí odkaz:
https://doaj.org/article/aef78ad207d14403824bcb1e71f1c74d
Autor:
Chin Yu, Thallampuranam Krishnaswamy S. Kumar, R. Bhaskaran, Gurunathan Jayaraman, Shui-Tein Chen, Hui-Ming Yu
Publikováno v:
International Journal of Peptide and Protein Research. 46:88-96
The solution conformation of a synthetic cyclic decapeptide [with sequence mimicking the third disulfide loop of rat transforming growth factor-alpha (rTGF-alpha)] in deuterated dimethyl sulfoxide was studied by 2D NMR. The determination of solution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb9b9f9ef91bc46649d09fcb6159ee7b
https://doi.org/10.1111/j.1399-3011.1995.tb00586.x
https://doi.org/10.1111/j.1399-3011.1995.tb00586.x
Autor:
Dharmaraj Samuel, Chin Yu, Gurunathan Jayaraman, Ding-Kwo Chang, Mei-Ming Chang, Pey-Wen Yang, Gopal Ganesh, Kuo Chu Hwang, Vishwa Deo Trivedi, Sue-Lein Wang, Thallampuranam Krishnaswamy S. Kumar
Publikováno v:
Protein Science. 9:344-352
The in vitro refolding of hen egg-white lysozyme is studied in the presence of various osmolytes. Proline is found to prevent aggregation during protein refolding. However, other osmolytes used in this study fail to exhibit a similar property. Experi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d2ff5803fa6346eabaa31c76ef80f11
https://doi.org/10.1110/ps.9.2.344
https://doi.org/10.1110/ps.9.2.344
Autor:
Chin Yu, Der-Hang Chin, Thallampuranam Krishnaswamy S. Kumar, Kandaswamy Jayachithra, Ta-Jung Lu
Publikováno v:
Biophysical Journal. 88(6):4252-4261
The conformational stability of aponeocarzinostatin, an all-β-sheet protein with 113 amino-acid residues, is investigated by thermal-induced equilibrium unfolding between pH 2.0 and 10.0 with and without urea. At room temperature, the protein is sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92003f39f15a2c30886ac197cca71e37
Autor:
Karuppanan Muthusamy Kathir, Hwo Shuenn Sheu, Pei Chi Chao, Chin Yu, Thallampuranam Krishnaswamy S. Kumar, Fuh-Jyh Jan, Dakshinamurthy Rajalingam, Sampath Srisailam
Publikováno v:
Journal of Biological Chemistry. 278:17701-17709
Acidic fibroblast growth factor from newt (Notopthalmus viridescens) is a ∼15-kDa, all β-sheet protein devoid of disulfide bonds. In the present study, we investigate the effects of 2,2,2-trifluoroethanol (TFE) on the structure of newt acidic fibr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e22fb2d5439db9c4768462ad619e0483
https://doi.org/10.1074/jbc.m300336200
https://doi.org/10.1074/jbc.m300336200
Autor:
Kellathur N. Srinivasan, Betty Cheng, Vaithiyalingam Sivaraja, Toru Sasaki, Thallampuranam Krishnaswamy S. Kumar, R. Manjunatha Kini, H. John Bowie, Chin Yu, Jan Tytgat, Ponnampalam Gopalakrishnakone, B. Chia Cheng San, Isabelle Huys, Kazuki Sato, Shoba Ranganathan
Publikováno v:
Journal of Biological Chemistry. 277:30040-30047
An important and exciting challenge in the postgenomic era is to understand the functions of newly discovered proteins based on their structures. The main thrust is to find the common structural motifs that contribute to specific functions. Using thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76f5915ef67604cd46328c65116a5c4d
https://doi.org/10.1074/jbc.m111258200
https://doi.org/10.1074/jbc.m111258200
Autor:
Yen-Chung Chang, ‡ Han-Min Wang, Chin Yu, Dakshinamurthy Rajalingam, Sampath Srisailam, Hwo Shuenn Sheu, Thallampuranam Krishnaswamy S. Kumar, Vaithiyalingam Sivaraja
Publikováno v:
Journal of Biological Chemistry. 277:19027-19036
In the present study, we demonstrate the thermal induced amyloid formation in a beta-barrel protein, such as the acidic fibroblast growth factor from Notopthalmus viridescens (nFGF-1). Fibril formation in nFGF-1 is observed to occur maximally at 65 d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8074e0a36b7ad0c46250b2dde1e68ca
https://doi.org/10.1074/jbc.m110762200
https://doi.org/10.1074/jbc.m110762200
Publikováno v:
Journal of the American Chemical Society. 124:1884-1888
Effect(s) of organic solvents on an all beta-sheet protein are investigated to understand the influence of backbone conformation on protein aggregation. Results obtained in the present study reveal that protein aggregation is accompanied by the forma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7894bfeddbda9efe8bb2b6afdb428ee
https://doi.org/10.1021/ja012070r
https://doi.org/10.1021/ja012070r
Autor:
Chin Yu, ‡ Han-Min Wang, Ya-Hui Chi, Meng-Chiao Ho, § and Ing-Ming Chiu, Thallampuranam Krishnaswamy S. Kumar
Publikováno v:
Biochemistry. 40:7746-7753
The thermodynamic parameters characterizing the conformational stability of the human acidic fibroblast growth factor (hFGF-1) have been determined by isothermal urea denaturation and thermal denaturation at fixed concentrations of urea using fluores
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ff2dcb209a3a50944e7429a1549bfc0
https://doi.org/10.1021/bi002364+
https://doi.org/10.1021/bi002364+
Autor:
Dharmaraj Samuel, Krishnaswamy Balamurugan, Wann-Yin Lin, Thallampuranam Krishnaswamy S. Kumar, Der-Hang Chin, Chin Yu
Publikováno v:
Journal of Biological Chemistry. 276:4134-4141
The refolding kinetics of the 140-residue, all beta-sheet, human fibroblast growth factor (hFGF-1) is studied using a variety of biophysical techniques such as stopped-flow fluorescence, stopped-flow circular dichroism, and quenched-flow hydrogen exc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f56ebe4228dbc89e97447bb9a718d156
https://doi.org/10.1074/jbc.m005921200
https://doi.org/10.1074/jbc.m005921200