PMID- 10526214
OWN - NLM
STAT- MEDLINE
DCOM- 19991102
LR  - 20190702
IS  - 0027-5107 (Print)
IS  - 0027-5107 (Linking)
VI  - 435
IP  - 1
DP  - 1999 Sep 13
TI  - Protein complexes in nucleotide excision repair.
PG  - 23-33
AB  - The main pathway by which mammalian cells remove DNA damage caused by UV light
      and some other mutagens is nucleotide excision repair (NER). The best
      characterised components of the human NER process are those proteins defective in
      the inherited disorder xeroderma pigmentosum (XP). The proteins known to be
      involved in the first steps of the NER reaction (damage recognition and
      incision-excision) are heterotrimeric RPA, XPA, the 6 to 9 subunit TFIIH,
      XPC-hHR23B, XPG, and ERCC1-XPF. Many interactions between these proteins have
      been found in recent years using different methods both in mammalian cells and
      for the homologous proteins in yeast. There are virtually no quantitative
      measurements of the relative strengths of these interactions. Higher order
      associations between these proteins in solution and even the existence of a
      complete "repairosome" complex have been reported, which would have implications 
      both for the mechanism of repair and for the interplay between NER and other
      cellular processes. Nevertheless, evidence for a completely pre-assembled
      functional repairosome in solution is inconclusive and the order of action of
      repair factors on damaged DNA is uncertain.
FAU - Araujo, S J
AU  - Araujo SJ
AD  - Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms,
      Hertfordshire, UK.
FAU - Wood, R D
AU  - Wood RD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Netherlands
TA  - Mutat Res
JT  - Mutation research
JID - 0400763
RN  - 0 (Proteins)
SB  - IM
EIN - Mutat Res 2000 Mar 20;459(2):171-2
MH  - DNA Repair/*physiology
MH  - Humans
MH  - Proteins/metabolism/*physiology
MH  - Saccharomyces cerevisiae/*genetics
RF  - 83
EDAT- 1999/10/20 09:00
MHDA- 2000/05/20 09:00
CRDT- 1999/10/20 09:00
PHST- 1999/10/20 09:00 [pubmed]
PHST- 2000/05/20 09:00 [medline]
PHST- 1999/10/20 09:00 [entrez]
AID - S0921877799000427 [pii]
AID - 10.1016/s0921-8777(99)00042-7 [doi]
PST - ppublish
SO  - Mutat Res. 1999 Sep 13;435(1):23-33. doi: 10.1016/s0921-8777(99)00042-7.