Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Khondker R. Hossain"'
Autor:
Alvaro Garcia, Haipei Zou, Khondker R. Hossain, Qikui Henry Xu, Annabelle Buda, Ronald J. Clarke
Publikováno v:
ACS Omega, Vol 4, Iss 1, Pp 518-527 (2019)
Externí odkaz:
https://doaj.org/article/10ccbd8833ba4382a50da6682bcdc74b
Autor:
Muhammad Yasir, Debarun Dutta, Khondker R. Hossain, Renxun Chen, Kitty K. K. Ho, Rajesh Kuppusamy, Ronald J. Clarke, Naresh Kumar, Mark D. P. Willcox
Publikováno v:
Frontiers in Microbiology, Vol 10 (2020)
Bacterial colonization and biofilm development on medical devices can lead to infection. Antimicrobial peptide-coated surfaces may prevent such infections. Melimine and Mel4 are chimeric cationic peptides showing broad-spectrum antimicrobial activity
Externí odkaz:
https://doaj.org/article/203253a430274536a9660fbe2e9f4668
Publikováno v:
Membranes, Vol 6, Iss 4, p 51 (2016)
The Chloride Intracellular Ion Channel (CLIC) family consists of six conserved proteins in humans. These are a group of enigmatic proteins, which adopt both a soluble and membrane bound form. CLIC1 was found to be a metamorphic protein, where under s
Externí odkaz:
https://doaj.org/article/3a0dd246e6c8433086a7ea6d4692f1d7
Publikováno v:
Membranes, Vol 6, Iss 1, p 15 (2016)
CLIC1 is a Chloride Intracellular Ion Channel protein that exists either in a soluble state in the cytoplasm or as a membrane bound protein. Members of the CLIC family are largely soluble proteins that possess the intriguing property of spontaneous i
Externí odkaz:
https://doaj.org/article/8b746813ce294f878576b9c5fef1ecb5
Autor:
Khondker R. Hossain, Daniel R. Turkewitz, Stephen A. Holt, Anton P. Le Brun, Stella M. Valenzuela
Publikováno v:
Langmuir. 39:3286-3300
Autor:
Sophia C. Goodchild, Ronald J. Clarke, Flemming Cornelius, Alison Rodger, Richard J. Payne, Daniel Clayton, Khondker R. Hossain
Publikováno v:
Faraday Discussions
Membrane protein structure and function are modulated via interactions with their lipid environment. This is particularly true for integral membrane pumps, the P-type ATPases. These ATPases play vital roles in cell physiology, where they are associat
Autor:
Heba Al Khamici, Louise J Brown, Khondker R Hossain, Amanda L Hudson, Alxcia A Sinclair-Burton, Jane Phui Mun Ng, Elizabeth L Daniel, Joanna E Hare, Bruce A Cornell, Paul M G Curmi, Mary W Davey, Stella M Valenzuela
Publikováno v:
PLoS ONE, Vol 10, Iss 1, p e115699 (2015)
The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins where they function as
Externí odkaz:
https://doaj.org/article/b54dca6279c64ebfa0472ffbf7704d02
Autor:
Khondker R. Hossain, Preeti Jain, Murad Hossain, Hasan Mahmud Reza, Zarin Tasnim Gias, Tairin Islam
Plants belonging to Citrus sp. are rich in phenolics which are of great medicinal value. The present study focuses on antioxidant and antibacterial potential of various extracts of a locally grown variety of Citrus acida leaves and their correlation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d33323b81641277924b244dc7d293673
https://hdl.handle.net/10453/164788
https://hdl.handle.net/10453/164788
Autor:
Stella M. Valenzuela, Stephen A. Holt, Daniel R. Turkewitz, Paul M. G. Curmi, Khondker R. Hossain, Louise J. Brown, Bruce Cornell, Leonie Herson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1863:1243-1253
Background Sterols have been reported to modulate conformation and hence the function of several membrane proteins. One such group is the Chloride Intracellular Ion Channel (CLIC) family of proteins. The CLIC protein family consists of six evolutiona
Autor:
Bogdan Lev, Thi Hanh Nguyen Pham, Alvaro Garcia, Amy Gorman, Flemming Cornelius, Toby W. Allen, Dil Diaz, Khondker R. Hossain, Ronald J. Clarke
Publikováno v:
Garcia, A, Lev, B, Hossain, K R, Gorman, A, Diaz, D, Thi Hanh Nguyen Pham,, Cornelius, F, Allen, T W & Clarke, R J 2019, ' Cholesterol depletion inhibits Na+,K+-ATPase activity in a near-native membrane environment ', Journal of Biological Chemistry, vol. 294, no. 15, pp. 5956-5969 . https://doi.org/10.1074/jbc.RA118.006223
Cholesterol’s effects on Na+,K+-ATPase reconstituted in phospholipid vesicles have been extensively studied. However, previous studies have reported both cholesterol-mediated stimulation and inhibition of Na+,K+-ATPase activity. Here, using partial