Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Rakesh K. Dhiman"'
Autor:
Rakesh K. Dhiman, Mark C. Schulbach, Sebabrata Mahapatra, Alain R. Baulard, Varalakshmi Vissa, Patrick J. Brennan, Dean C. Crick
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 6, Pp 1140-1147 (2004)
We have identified an ω,E,E-farnesyl diphosphate (ω,E,E-FPP) synthase, encoded by the open reading frame Rv3398c, from Mycobacterium tuberculosis that is unique among reported FPP synthases in that it does not contain the type I (eukaryotic) or the
Externí odkaz:
https://doaj.org/article/206f8398d11c41a891f794692d28a480
Publikováno v:
ACS infectious diseases. 8(12)
Menaquinone (MK) is an essential component of the electron transport chain (ETC) in the gram-variable
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c177367dde63813cb7b39113ecad2197
https://pubmed.ncbi.nlm.nih.gov/36417754
https://pubmed.ncbi.nlm.nih.gov/36417754
Autor:
Melanie Ikeh, Dean C. Crick, Rakesh K. Dhiman, Venugopal Pujari, James M. Kincaid, Tanya Parish
Publikováno v:
PLoS ONE, Vol 14, Iss 4, p e0214958 (2019)
The menaquinone biosynthetic pathway presents a promising drug target against Mycobacterium tuberculosis and potentially other Gram-positive pathogens. In the present study, the essentiality, steady state kinetics of MenA from M. tuberculosis and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf5913d4c3ca85209c793edf97e4e314
https://doaj.org/article/d1e32ccd874444b0ba75e87523fc9b1d
https://doaj.org/article/d1e32ccd874444b0ba75e87523fc9b1d
Autor:
Dean C. Crick, Gavin J. Ryan, Premkumar Dinadayala, Alan R. Schenkel, Rakesh K. Dhiman, Anne J. Lenaerts
Publikováno v:
Journal of Bacteriology. 193:5802-5809
Lipoarabinomannan (LAM) is a structurally heterogeneous amphipathic lipoglycan present in Mycobacterium spp. and other actinomycetes, which constitutes a major component of the cell wall and exhibits a wide spectrum of immunomodulatory effects. Analy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a6a62e0891b39b7d2d97614575ea419
https://doi.org/10.1128/jb.05299-11
https://doi.org/10.1128/jb.05299-11
Autor:
Dean C. Crick, Kallolmay Biswas, Delphi Chatterjee, Anne J. Lenaerts, Richard A. Slayden, Jerald C. Hinshaw, Shiva K. Angala, Rakesh K. Dhiman, Melissa E. Boyne, Prabagaran Narayanasamy, Michio Kurosu, Sebabrata Mahapatra
Publikováno v:
Molecular Microbiology. 72:85-97
Understanding the basis of bacterial persistence in latent infections is critical for eradication of tuberculosis. Analysis of Mycobacterium tuberculosis mRNA expression in an in vitro model of non-replicating persistence indicated that the bacilli r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da848436c8404e3848ecd3e802f2b11c
https://doi.org/10.1111/j.1365-2958.2009.06625.x
https://doi.org/10.1111/j.1365-2958.2009.06625.x
Autor:
Varalakshmi D. Vissa, Rakesh K. Dhiman, Mark C. Schulbach, Dean C. Crick, Alain R. Baulard, Patrick J. Brennan, Sebabrata Mahapatra
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 6, Pp 1140-1147 (2004)
We have identified an omega,E,E-farnesyl diphosphate (omega,E,E-FPP) synthase, encoded by the open reading frame Rv3398c, from Mycobacterium tuberculosis that is unique among reported FPP synthases in that it does not contain the type I (eukaryotic)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adfb6d111c2c8db559be7ddc34242880
http://www.sciencedirect.com/science/article/pii/S0022227520318125
http://www.sciencedirect.com/science/article/pii/S0022227520318125
Autor:
Christopher M. Sassetti, Andrew Zukauskas, Jennifer E. Griffin, Christine L. Gee, Sloane R. Blair, Tom Alber, Rakesh K. Dhiman, Jun-Rong Wei, K. G. Papavinasasundaram, Eric J. Rubin, Harene Venghatakrishnan, Dean C. Crick, Arnold M. Falick, David S. King, Christina E. Baer
Publikováno v:
Science Signaling. 5
Prokaryotic cell wall biosynthesis is coordinated with cell growth and division, but the mechanisms regulating this dynamic process remain obscure. Here, we describe a phosphorylation-dependent regulatory complex that controls peptidoglycan (PG) bios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fefc69fd103819983c7510d60338a9ec
https://doi.org/10.1126/scisignal.2002525
https://doi.org/10.1126/scisignal.2002525
Publikováno v:
Journal of bacteriology. 192(24)
The DosR regulon in Mycobacterium tuberculosis is involved in respiration-limiting conditions, its induction is controlled by two histidine kinases, DosS and DosT, and recent experimental evidence indicates DosS senses either molecular oxygen or a re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5084fd5f842a8125200474f80419cbdf
https://pubmed.ncbi.nlm.nih.gov/20952575
https://pubmed.ncbi.nlm.nih.gov/20952575
Autor:
Rakesh K, Dhiman, Sebabrata, Mahapatra, Richard A, Slayden, Melissa E, Boyne, Anne, Lenaerts, Jerald C, Hinshaw, Shiva K, Angala, Delphi, Chatterjee, Kallolmay, Biswas, Prabagaran, Narayanasamy, Michio, Kurosu, Dean C, Crick
Publikováno v:
Molecular microbiology. 72(1)
Understanding the basis of bacterial persistence in latent infections is critical for eradication of tuberculosis. Analysis of Mycobacterium tuberculosis mRNA expression in an in vitro model of non-replicating persistence indicated that the bacilli r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7c1412caaffb5c3993315c2caa1bcda
https://pubmed.ncbi.nlm.nih.gov/19220750
https://pubmed.ncbi.nlm.nih.gov/19220750
Publikováno v:
Journal of medicinal chemistry. 50(17)
Since utilization of menaquinone in the electron transport system is a characteristic of Gram-positive organisms, the 1,4-dihydroxy-2-naphthoate prenyltransferase (MenA) inhibitors 1a and 2a act as selective antibacterial agents against organisms suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca616abb6a3e39ef216ef6c51f52fdf4
https://pubmed.ncbi.nlm.nih.gov/17658779
https://pubmed.ncbi.nlm.nih.gov/17658779