Md Faiz Ahmad
Overview
Explore the profile of Md Faiz Ahmad including associated specialties, affiliations and a list of published articles.
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Articles
18
Citations
351
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0
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Recent Articles
1.
Ahsan S, Mohan Rao C, Ahmad M
Adv Exp Med Biol
. 2018 Feb;
1048:175-198.
PMID: 29453539
The physico-chemical properties of nanoparticles, as characterized under idealized laboratory conditions, have been suggested to differ significantly when studied under complex physiological environments. A major reason for this variation has...
2.
Knappenberger A, Grandhi S, Sheth R, Ahmad M, Viswanathan R, Harris M
J Biol Chem
. 2017 Aug;
292(40):16463-16476.
PMID: 28808063
Eukaryotic class I ribonucleotide reductases (RRs) generate deoxyribonucleotides for DNA synthesis. Binding of dNTP effectors is coupled to the formation of active dimers and induces conformational changes in a short...
3.
Ahmad M, Alam I, Huff S, Pink J, Flanagan S, Shewach D, et al.
Proc Natl Acad Sci U S A
. 2017 Jul;
114(31):8241-8246.
PMID: 28716944
Human ribonucleotide reductase (hRR) is crucial for DNA replication and maintenance of a balanced dNTP pool, and is an established cancer target. Nucleoside analogs such as gemcitabine diphosphate and clofarabine...
4.
Knappenberger A, Ahmad M, Viswanathan R, Dealwis C, Harris M
Biochemistry
. 2016 Sep;
55(41):5884-5896.
PMID: 27634056
Class I ribonucleotide reductase (RR) maintains balanced pools of deoxyribonucleotide substrates for DNA replication by converting ribonucleoside diphosphates (NDPs) to 2'-deoxyribonucleoside diphosphates (dNDPs). Binding of deoxynucleoside triphosphate (dNTP) effectors (ATP/dATP,...
5.
Misko T, Wijerathna S, Radivoyevitch T, Berdis A, Ahmad M, Harris M, et al.
FEBS Lett
. 2016 May;
590(12):1704-12.
PMID: 27155231
Sml1 is an intrinsically disordered protein inhibitor of Saccharomyces cerevisiae ribonucleotide reductase (ScRR1), but its inhibition mechanism is poorly understood. RR reduces ribonucleoside diphosphates to their deoxy forms, and balances...
6.
Ahmad M, Huff S, Pink J, Alam I, Zhang A, Perry K, et al.
J Med Chem
. 2015 Oct;
58(24):9498-509.
PMID: 26488902
Ribonucleotide reductase (RR) catalyzes the rate-limiting step of dNTP synthesis and is an established cancer target. Drugs targeting RR are mainly nucleoside in nature. In this study, we sought to...
7.
Ahmad M, Dealwis C
Prog Mol Biol Transl Sci
. 2013 May;
117:389-410.
PMID: 23663976
Ribonucleotide reductases (RRs) catalyze a crucial step of de novo DNA synthesis by converting ribonucleoside diphosphates to deoxyribonucleoside diphosphates. Tight control of the dNTP pool is essential for cellular homeostasis....
8.
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...
9.
Ahmad M, Wan Q, Jha S, Motea E, Berdis A, Dealwis C
Mol Cancer Ther
. 2012 Aug;
11(10):2077-86.
PMID: 22933704
Human ribonucleotide reductase (hRR) is the key enzyme involved in de novo dNTP synthesis and thus represents an important therapeutic target against hyperproliferative diseases, most notably cancer. The purpose of...
10.
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...