Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Sampath Srisailam"'
Autor:
Sampath Srisailam, 隋賽仁
90
The three dimensional solution structure of an acidic fibroblast growth factor (nFGF-1) from the newt (Notopthalmus Viridescens) is determined using multidimensional NMR techniques. Complete assignment of the all atoms (1H, 15N and 13C) has b
The three dimensional solution structure of an acidic fibroblast growth factor (nFGF-1) from the newt (Notopthalmus Viridescens) is determined using multidimensional NMR techniques. Complete assignment of the all atoms (1H, 15N and 13C) has b
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/95556377378219202307
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:
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:
King Wong Leung, Thallapuranam Krishnaswamy Suresh Kumar, Sampath Srisailam, A. I. Arunkumar, C. Yu, Hueih Min Chen
Publikováno v:
European Journal of Biochemistry. 268:4278-4284
The solution structure of a custom lytic peptide, cecropin B3 (CB3), having two identical hydrophobic segments on both the N- and C-termini, was investigated by two-dimensional NMR spectroscopy. The need to determine the structure of this peptide is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a4c025ea3dd16b30db2e5423cd3224df
https://doi.org/10.1046/j.1432-1327.2001.02345.x
https://doi.org/10.1046/j.1432-1327.2001.02345.x
Autor:
A.I Arunkumar, Thallampuranam Krishnaswamy S. Kumar, Thirunavukkarasu Sivaraman, Gopal Ganesh, Ho-Jen Peng, Chin Yu, Dharmaraj Samuel, Meng-Chiao Ho, Hui-Chu Hsieh, Sampath Srisailam, Kuo-Wei Hung
Publikováno v:
Journal of the Chinese Chemical Society. 47:1009-1042
The aim of this comprehensive review is to critically evaluate the progress in research in the area of protein folding. In the first section, we discuss the various models proposed to explain the protein folding paradox. In the succeeding section of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e1063dd422869a1fe9be4a65575cf5c
https://doi.org/10.1002/jccs.200000141
https://doi.org/10.1002/jccs.200000141
Publikováno v:
Proteins. 64(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6c7c49649fd3232e07f7c6c25b2b6114
https://pubmed.ncbi.nlm.nih.gov/16741959
https://pubmed.ncbi.nlm.nih.gov/16741959
Autor:
Chin Yu, Thallampuranam Krishnaswamy S. Kumar, Ing-Ming Chiu, Karuppanan Muthusamy Kathir, Ya-Hui Chi, Thiagarajan Srimathi, Sampath Srisailam, W.Y. Lin
Publikováno v:
Biophysical journal. 85(1)
Acidic fibroblast growth factors from human (hFGF-1) and newt (nFGF-1) (Notopthalamus viridescens) are 16-kDa, all beta-sheet proteins with nearly identical three-dimensional structures. Guanidine hydrochloride (GdnHCl)-induced unfolding of hFGF-1 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a0b675d356f3082fc1a827b1145b90a
https://pubmed.ncbi.nlm.nih.gov/12829501
https://pubmed.ncbi.nlm.nih.gov/12829501
Autor:
Chieh Hsi Wu, Ing-Ming Chiu, Han Min Wang, Karuppanan Muthusamy Kathir, Ya-Hui Chi, Gu-Gang Chang, Ho Chz Chen, Thallampuranam Krishnaswamy S. Kumar, Rong Tsun Wu, Sampath Srisailam, Chin Yu, Philominathan Sagaya Theresa Leena, A.I Arunkumar
Publikováno v:
Protein science : a publication of the Protein Society. 11(5)
Oligomerization of fibroblast growth factors (FGFs) induced on binding to heparin or heparan sulfate proteoglycan is considered to be crucial for receptor activation and initiation of biological responses. To gain insight into the mechanism of activa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5507bf83c02877c342b51aa6148115c
https://pubmed.ncbi.nlm.nih.gov/11967362
https://pubmed.ncbi.nlm.nih.gov/11967362
Autor:
Gurunathan Jayaraman, C. Yu, Sampath Srisailam, Thallapuranam Krishnaswamy Suresh Kumar, S H Chou, C L Ho, C C Tsai
Publikováno v:
Protein science : a publication of the Protein Society. 9(4)
The aim of the present study is to understand the structural features responsible for the lethal activity of snake venom cardiotoxins. Comparison of the lethal potency of the five cardiotoxin isoforms isolated from the venom of Taiwan cobra (Naja naj
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08b0742d0be2a75be68811383884ca72
https://pubmed.ncbi.nlm.nih.gov/10794406
https://pubmed.ncbi.nlm.nih.gov/10794406