Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Ramesh B. Bambal"'
Autor:
Tridib Chaira, Kunihiko Fujii, Tarani Kanta Barman, Vattan Joshi, Dilip J. Upadhyay, Ram Kumar, Lalima Sharma, Manoj Kumar, Mahadev Bandgar, Pradip Kumar Bhatnagar, Ramesh B. Bambal, Ashwani Kumar Verma, Tarun Mathur, Manisha Pandya, Nobuhisa Masuda, Balasaheb Gangadhar Jadhav
Publikováno v:
The Journal of antimicrobial chemotherapy. 76(11)
Objectives FtsZ is an essential bacterial protein and an unexplored target for the development of antibacterial drugs. The development of a novel inhibitor targeting FtsZ offers a potential opportunity to combat drug resistance. DS01750413, a new der
Autor:
Jitendra A. Sattigeri, Ramesh B. Bambal, Takahide Nishi, Ajay Soni, Pragya Bhateja, Tarun Jain, Dilip J. Upadhyay, Nidhi Alekar, Tridib Chaira, Abdul Rehman Abdul Rauf, Mahesh Subhashrao Deshmukh, Malvika Garg, Tarani Kanta Barman, Mahendrakumar Gupta, Paras Kumar Jha
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 28:2993-2997
FimH is a type I fimbrial lectin located at the tip of type-1 pili of Gram-negative uropathogenic Escherichia coli (UPEC) guiding its ability to adhere and infect urothelial cells. Accordingly, blocking FimH with small molecule inhibitor is considere
Autor:
Ramesh B. Bambal, Alka Khanna, Indu Pal Kaur, Mandeep Singh, Ruchi Sood, Pradip Kumar Bhatnagar, Tridib Chaira, Harinder Singh, Dilip J Upadhaya
Publikováno v:
Current drug delivery. 17(4)
Background: Rifampicin is known to degrade at the acidic pH of the stomach, especially in the presence of isoniazid. Although isoniazid also degrades partially, its degradation is reversible. Objective: Presently, we provide a proof of the fact that
Autor:
Nobuhisa Masuda, Amuliya Kashyap, Madhvi Rao, Ramesh B. Bambal, Manoj Kumar, Tarani Kanta Barman, Vattan Joshi, Tridib Chaira, Kedar Purnapatre, Dilip J. Upadhyay, Souhaila Al Khodor, Manisha Pandya
Publikováno v:
Antimicrobial Agents and Chemotherapy. 63
DS86760016 is a new leucyl-tRNA-synthetase inhibitor at the preclinical development stage. DS86760016 showed potent activity against extended-spectrum multidrug-resistant Pseudomonas aeruginosa isolated from clinical samples and in vitro biofilms. In
Autor:
Ramesh B. Bambal, Tridib Chaira, Kedar Purnapatre, Dilip J. Upadhyay, Madhvi Rao, Manisha Pandya, Alka Khanna, Nobuhisa Masuda
The emergence of multidrug-resistant (MDR) Gram-negative bacilli is a major concern in the treatment of nosocomial infections. Antibacterial agents with novel modes of action can be useful, as these pathogens have become resistant to almost all exist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f0b80f5d134267d9c62eb9fa0316fe1
https://europepmc.org/articles/PMC5913941/
https://europepmc.org/articles/PMC5913941/
Autor:
Stephen E. Clarke, Ramesh B. Bambal
Publikováno v:
Evaluation of Drug Candidates for Preclinical Development: Pharmacokinetics, Metabolism, Pharmaceutics, and Toxicology
Autor:
Lalita Guntuku, V.G.M. Naidu, Ramesh B. Bambal, Kahkashan Resham, Dinesh Thummuri, Prinesh N. Patel, Vanya Shah
Publikováno v:
Chemico-biological interactions. 240
There has been a search for new anticancer agents to treat cancer resistance throughout the globe. Salinomycin (SAL), a broad spectrum antibiotic and a coccidiostat has been found to counter tumour resistance and kill cancer stem cells with better ef
Publikováno v:
The Analyst. 138(20)
The aim of the present study is to develop and demonstrate the correlation between in vitro and in vivo Plasma Protein Binding (PPB) using the ultracentrifugation method for its validation by using marketed compounds like atenolol, theophylline and p
Autor:
Ramesh B. Bambal, Robert P. Hanzlik
Publikováno v:
Archives of Biochemistry and Biophysics. 334:59-66
The action of cytochrome P450 4A1 (CYP4A1) on fatty acid substrates is characterized by a pronounced regioselectivity for omega-hydroxylation. To elucidate the chemical basis of this specificity we probed the active site of a CYP4A1 fusion protein (f
Autor:
Ramesh B. Bambal, Robert P. Hanzlik
Publikováno v:
Biochemical and Biophysical Research Communications. 219:445-449
The active site of an engineered, expressed fusion protein containing the sequences of cytochrome P450 4A1 (lauric acid omega-hydroxylase) and NADPH-cytochrome P450 reductase, has been probed with olefinic, acetylenic, aromatic, and other analogs of