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Prem Singh Kaushal

Explore the profile of Prem Singh Kaushal including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 7
Citations 117
Followers 0
Related Specialties
Chemistry
Molecular Biology
Microbiology
Top 10 Co-Authors
M Vijayan
Md Faiz Ahmad
Qun Wan
Ramappa K Talawar
Sanath R Wijerathna
Umesh Varshney
Rajendra Kumar Agrawal
Carol Lyn Piazza
Alok Sharma
Chris G Dealwis
Published In
Acta Crystallogr D Biol Crystallogr
Acta Crystallogr Sect F Struct Biol Cryst Commun
Pharmaceuticals (Basel)
Nat Struct Mol Biol
J Mol Biol
Affiliations
Soon will be listed here.
Recent Articles
1.
Structure of a group II intron in complex with its reverse transcriptase
Qu G, Kaushal P, Wang J, Shigematsu H, Piazza C, Agrawal R, et al.
Nat Struct Mol Biol . 2016 May; 23(6):549-57. PMID: 27136327
Bacterial group II introns are large catalytic RNAs related to nuclear spliceosomal introns and eukaryotic retrotransposons. They self-splice, yielding mature RNA, and integrate into DNA as retroelements. A fully active...
2.
Targeting the Large Subunit of Human Ribonucleotide Reductase for Cancer Chemotherapy
Wijerathna S, Ahmad M, Xu H, Fairman J, Zhang A, Kaushal P, et al.
Pharmaceuticals (Basel) . 2012 Nov; 4(10):1328-1354. PMID: 23115527
Ribonucleotide reductase (RR) is a crucial enzyme in de novo DNA synthesis, where it catalyses the rate determining step of dNTP synthesis. RRs consist of a large subunit called RR1...
3.
Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase
Ahmad M, Kaushal P, Wan Q, Wijerathna S, An X, Huang M, et al.
J Mol Biol . 2012 Apr; 419(5):315-29. PMID: 22465672
Ribonucleotide reductases (RRs) catalyze the rate-limiting step of de novo deoxynucleotide (dNTP) synthesis. Eukaryotic RRs consist of two proteins, RR1 (α) that contains the catalytic site and RR2 (β) that...
4.
X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures
Kaushal P, Singh P, Sharma A, Muniyappa K, Vijayan M
Acta Crystallogr D Biol Crystallogr . 2010 Oct; 66(Pt 10):1048-58. PMID: 20944238
The crystal structures of two forms of Mycobacterium leprae single-stranded DNA-binding protein (SSB) have been determined at 2.05 and 2.8 Å resolution. Comparison of these structures with the structures of...
5.
Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis: insights into interactions with ligands
Kaushal P, Talawar R, Varshney U, Vijayan M
Acta Crystallogr Sect F Struct Biol Cryst Commun . 2010 Aug; 66(Pt 8):887-92. PMID: 20693660
Uracil N-glycosylase (Ung) is the most thoroughly studied of the group of uracil DNA-glycosylase (UDG) enzymes that catalyse the first step in the uracil excision-repair pathway. The overall structure of...
6.
Water-mediated variability in the structure of relaxed-state haemoglobin
Kaushal P, Sankaranarayanan R, Vijayan M
Acta Crystallogr Sect F Struct Biol Cryst Commun . 2008 Jun; 64(Pt 6):463-9. PMID: 18540052
The crystal structure of high-salt horse methaemoglobin has been determined at environmental relative humidities (r.h.) of 88, 79, 75 and 66%. The molecule is in the R state in the...
7.
Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources
Kaushal P, Talawar R, Krishna P, Varshney U, Vijayan M
Acta Crystallogr D Biol Crystallogr . 2008 May; 64(Pt 5):551-60. PMID: 18453691
Uracil-DNA glycosylase (UNG), a repair enzyme involved in the excision of uracil from DNA, from mycobacteria differs from UNGs from other sources, particularly in the sequence in the catalytically important...