Matches in SemOpenAlex for { <https://semopenalex.org/work/W4285602202> ?p ?o ?g. }
- W4285602202 endingPage "43" @default.
- W4285602202 startingPage "26" @default.
- W4285602202 abstract "Ribonucleotide reductase (RNR) is a multi-subunit enzyme responsible for catalyzing the rate-limiting step in the production of deoxyribonucleotides essential for DNA synthesis and repair. The active RNR complex is composed of multimeric R1 and R2 subunits. The RNR catalysis involves the formation of tyrosyl radicals in R2 subunits and thiyl radicals in R1 subunits. Despite the quaternary structure and cofactor diversity, all the three classes of RNR have a conserved cysteine residue at the active site which is converted into a thiyl radical that initiates the substrate turnover, suggesting that the catalytic mechanism is somewhat similar for all three classes of the RNR enzyme. Increased RNR activity has been associated with malignant transformation, cancer cell growth, and tumorigenesis. Efforts concerning the understanding of RNR inhibition in designing potent RNR inhibitors/drugs as well as developing novel approaches for antibacterial, antiviral treatments, and cancer therapeutics with improved radiosensitization have been made in clinical research. This review highlights the precise and potent roles of NO in RNR inhibition by targeting both the subunits. Under nitrosative stress, the thiols of the R1 subunits have been found to be modified by S-nitrosylation and the tyrosyl radicals of the R2 subunits have been modified by nitration. In view of the recent advances and progresses in the field of nitrosative modifications and its fundamental role in signaling with implications in health and diseases, the present article focuses on the regulations of RNR activity by S-nitrosylation of thiols (R1 subunits) and nitration of tyrosyl residues (R2 subunits) which will further help in designing new drugs and therapies." @default.
- W4285602202 created "2022-07-16" @default.
- W4285602202 creator A5005457550 @default.
- W4285602202 creator A5035336788 @default.
- W4285602202 creator A5088926379 @default.
- W4285602202 date "2022-10-01" @default.
- W4285602202 modified "2023-09-25" @default.
- W4285602202 title "Ribonucleotide reductase: Implications of thiol S-nitrosylation and tyrosine nitration for different subunits" @default.
- W4285602202 cites W1492951734 @default.
- W4285602202 cites W1497352222 @default.
- W4285602202 cites W1510505825 @default.
- W4285602202 cites W1559967612 @default.
- W4285602202 cites W1563948625 @default.
- W4285602202 cites W1565072410 @default.
- W4285602202 cites W1572756764 @default.
- W4285602202 cites W1575180462 @default.
- W4285602202 cites W1584870064 @default.
- W4285602202 cites W1589868601 @default.
- W4285602202 cites W169275994 @default.
- W4285602202 cites W1828441724 @default.
- W4285602202 cites W1832291055 @default.
- W4285602202 cites W1863202251 @default.
- W4285602202 cites W1889537242 @default.
- W4285602202 cites W1927227734 @default.
- W4285602202 cites W1940632416 @default.
- W4285602202 cites W1963483230 @default.
- W4285602202 cites W1963692497 @default.
- W4285602202 cites W1964634019 @default.
- W4285602202 cites W1964990390 @default.
- W4285602202 cites W1967252819 @default.
- W4285602202 cites W1968118415 @default.
- W4285602202 cites W1969366577 @default.
- W4285602202 cites W1970354788 @default.
- W4285602202 cites W1971765132 @default.
- W4285602202 cites W1972415066 @default.
- W4285602202 cites W1972624254 @default.
- W4285602202 cites W1973623137 @default.
- W4285602202 cites W1974616331 @default.
- W4285602202 cites W1976558321 @default.
- W4285602202 cites W1976685924 @default.
- W4285602202 cites W1978038466 @default.
- W4285602202 cites W1979404773 @default.
- W4285602202 cites W1981417880 @default.
- W4285602202 cites W1984858612 @default.
- W4285602202 cites W1986079719 @default.
- W4285602202 cites W1986204614 @default.
- W4285602202 cites W1986345122 @default.
- W4285602202 cites W1986386412 @default.
- W4285602202 cites W1987802758 @default.
- W4285602202 cites W1987821948 @default.
- W4285602202 cites W1988717330 @default.
- W4285602202 cites W1990980324 @default.
- W4285602202 cites W1991194699 @default.
- W4285602202 cites W1991454533 @default.
- W4285602202 cites W1993491727 @default.
- W4285602202 cites W1994166804 @default.
- W4285602202 cites W1994386857 @default.
- W4285602202 cites W1995592237 @default.
- W4285602202 cites W1995674872 @default.
- W4285602202 cites W1996295600 @default.
- W4285602202 cites W1997382890 @default.
- W4285602202 cites W1997692317 @default.
- W4285602202 cites W1998984215 @default.
- W4285602202 cites W2001707194 @default.
- W4285602202 cites W2002176182 @default.
- W4285602202 cites W2002192155 @default.
- W4285602202 cites W2003043809 @default.
- W4285602202 cites W2003108616 @default.
- W4285602202 cites W2004724154 @default.
- W4285602202 cites W2008734787 @default.
- W4285602202 cites W2008841158 @default.
- W4285602202 cites W2009410239 @default.
- W4285602202 cites W2011960809 @default.
- W4285602202 cites W2012219744 @default.
- W4285602202 cites W2013628401 @default.
- W4285602202 cites W2016455670 @default.
- W4285602202 cites W2017220997 @default.
- W4285602202 cites W2019227458 @default.
- W4285602202 cites W2020567919 @default.
- W4285602202 cites W2022313575 @default.
- W4285602202 cites W2022972602 @default.
- W4285602202 cites W2023379699 @default.
- W4285602202 cites W2024060193 @default.
- W4285602202 cites W2024610281 @default.
- W4285602202 cites W2024825275 @default.
- W4285602202 cites W2027103405 @default.
- W4285602202 cites W2028329897 @default.
- W4285602202 cites W2030495727 @default.
- W4285602202 cites W2030864821 @default.
- W4285602202 cites W2031615792 @default.
- W4285602202 cites W2031748708 @default.
- W4285602202 cites W2036776952 @default.
- W4285602202 cites W2037772209 @default.
- W4285602202 cites W2039050634 @default.
- W4285602202 cites W2039979152 @default.
- W4285602202 cites W2044429183 @default.
- W4285602202 cites W2044442079 @default.
- W4285602202 cites W2044813827 @default.