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Rajendra Prasad

Researcher at Indian Institute of Technology (BHU) Varanasi

Publications -  1106
Citations -  33537

Rajendra Prasad is an academic researcher from Indian Institute of Technology (BHU) Varanasi. The author has contributed to research in topics: Candida albicans & Medicine. The author has an hindex of 86, co-authored 945 publications receiving 29526 citations. Previous affiliations of Rajendra Prasad include Jawaharlal Nehru University & University of the South Pacific.

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Prevention of pulmonary embolism and deep vein thrombosis with low dose aspirin: Pulmonary Embolism Prevention (PEP) trial

Jeremy L. O'Brien, +327 more
- 15 Apr 2000 - 
TL;DR: In this article, a meta-analysis of their results indicated reductions in the risks of deep-vein thrombosis and of pulmonary embolism in various high-risk groups.
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Requirement of mammalian DNA polymerase-beta in base-excision repair.

TL;DR: These studies demonstrate that β-polymerase functions specifically in base-excision repair in vivo, and establishes embryonic fibroblast cell lines homozygous for a deletion mutation in the gene encoding DNA polymerase-β.
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Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism.

TL;DR: Crystal structures suggest that pol beta may enhance fidelity by an induced fit mechanism in which correct base pairing between template and incoming dNTP induces alignment of catalytic groups for catalysis (via thumb closure), but incorrect base pairing will not.
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Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals.

TL;DR: By functional complementation of a PDR5 null mutant of Saccharomyces cervisiae, the multidrug-resistance gene CDR1 of Candida albicans is cloned and sequenced, revealing that it encodes a putative membrane pump belonging to the ABC (ATP-binding cassette) superfamily.
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AP endonuclease-independent DNA base excision repair in human cells

TL;DR: It is shown that in mammalian cells, removal of the 3' phosphate is dependent on polynucleotide kinase (PNK), and not APE, and that NEIL1/PNK could also repair the products of other DNA glycosylases, suggesting a broad role for this APE-independent BER pathway in mammals.