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词条 Helicase–primase complex
释义

  1. List of H-P by virus name

  2. List of H-P inhibitors

  3. References

A helicase–primase complex (also helicase-primase, Hel/Prim, H-P or H/P) is a complex of enzymes including DNA helicase and DNA primase. A helicase-primase associated factor protein may also be present.[1]

The complex is used by herpesviruses, in which it is responsible for lytic DNA virus replication.[2][3][4] In many dsDNA viruses, primase and helicase are fused into a single polypeptide chain, so that the primase and helicase domains correspond to the N-terminal and C-terminal parts of the protein, respectively.[5]

A helicase-primase inhibitor (HPI) is a drug that blocks this action through acting as an enzyme inhibitor.

List of H-P by virus name

  • EBV: helicase:BBLF4 primase: BSLF1 accessory protein:BBLF2/3[2]

List of H-P inhibitors

  • Amenamevir (ASP2151)[7]
  • Pritelivir (BAY 57-1293, AIC316)
  • BILS 22 BS[7]
  • T157602[6]

References

1. ^{{cite book | title = Encyclopedia of toxicology | edition = 2nd | editor-first1 = Philip | editor-last1 = Wexler | editor-first2 = Bruce D. | editor-last2 = Anderson | name-list-format = vanc | isbn = 978-0-08-054800-5 | date = 2005 | url = https://books.google.com/books?id=uQEkJw00eqcC&pg=PT1850&lpg=PT1850&dq=Encyclopedia+of+Toxicology+A+helicase-primase+associated+factor+protein&source=bl | page = 1850}}
2. ^{{cite journal | vauthors = Thierry E, Brennich M, Round A, Buisson M, Burmeister WP, Hutin S | title = Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3 | journal = Virus Genes | volume = 51 | issue = 2 | pages = 171–81 | date = October 2015 | pmid = 26292944 | doi = 10.1007/s11262-015-1233-6 }}
3. ^{{cite book | first1 = Hans-Georg | last1 = Kräusslich | first2 = Ralf | last2 = Bartenschlager | name-list-format = vanc | title = Antiviral Strategies | url=https://books.google.com/books?id=r_Dq0xIZ7d.HMC&pg=PA162|date=2 December 2008|publisher=Springer Science & Business Media|isbn=978-3-540-79086-0|pages=162–8}}
4. ^{{cite thesis | type = Ph.D. | last = Cavanaugh | first = Nisha Angele | name-list-format = vanc | publisher = University of Colorado at Boulder | title = Herpes DNA Synthesis: Initiation of New DNA Strands and Discrimination Between Right and Wrong Bases by the Polymerase|url=https://books.google.com/books?id=X_mfVkcaN20C&pg=PA2|year=2008 | isbn=978-0-549-67366-8|pages=2–12}}
5. ^{{cite journal | vauthors = Kazlauskas D, Krupovic M, Venclovas Č | title = The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomes | journal = Nucleic Acids Research | volume = 44 | issue = 10 | pages = 4551–64 | date = June 2016 | pmid = 27112572 | pmc = 4889955 | doi = 10.1093/nar/gkw322 }}
6. ^{{cite journal | vauthors = Weller SK, Kuchta RD | title = The DNA helicase-primase complex as a target for herpes viral infection | journal = Expert Opinion on Therapeutic Targets | volume = 17 | issue = 10 | pages = 1119–32 | date = October 2013 | pmid = 23930666 | pmc = 4098783 | doi = 10.1517/14728222.2013.827663 }}
{{DNA antivirals}}{{DEFAULTSORT:Helicase-primase complex}}{{virus-stub}}

3 : Viral proteins|Enzymes|DNA replication

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