MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS - Journal - MOST Wiedzy

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MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS

ISSN:

0027-5107

eISSN:

1873-135X

Disciplines
(Field of Science):

  • Biomedical engineering (Engineering and Technology)
  • Pharmacology and pharmacy (Medical and Health Sciences )
  • Medical sciences (Medical and Health Sciences )
  • Health sciences (Medical and Health Sciences )
  • Nutrition and food technology (Agricultural sciences)
  • Agriculture and horticulture (Agricultural sciences)
  • Veterinary science (Agricultural sciences)
  • Chemical sciences (Natural sciences)
  • Biological sciences (Natural sciences)

Ministry points: Help

Ministry points - current year
Year Points List
Year 2021 70 Ministry Scored Journals List 2019
Ministry points - previous years
Year Points List
2021 70 Ministry Scored Journals List 2019
2020 70 Ministry Scored Journals List 2019
2019 70 Ministry Scored Journals List 2019
2018 35 A
2017 35 A
2016 35 A
2015 35 A
2014 35 A
2013 35 A
2012 35 A
2011 35 A
2010 32 A
2009 32 A
2008 32 A

Points CiteScore:

Points CiteScore - current year
Year Points
Year 2019 5
Points CiteScore - previous years
Year Points
2019 5
2018 5.5
2016 5.7
2015 4.1
2014 1.6
2013 1
2012 1.8
2011 0.5

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Catalog Journals

Year 2014
  • Conserved motifs of MutL proteins

    tThe MutL protein is best known for its function in DNA mismatch repair (MMR). However, there isevidence to suggest that MutL is not only the linker connecting the functions of MutS and MutH in MMR,but that it also participates in other repair systems, such as Very Short Patch (VSP), Base Excision (BER)and Nucleotide Excision Repair (NER). This study set out to identify the most highly conserved aminoacid sequence motifs in MutL...

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Year 2011
Year 2010
  • Conservation and diversity of MutS proteins

    The homologues of MutS, mismatch repair protein, exist in all prokaryotes, with the exception of Actinobacteria, Mollicutes and part of the Archaea. Multiple alignments of 316 MutS amino acid sequences from 169 species revealed conserved residues and sequence motifs distinguishing MutS homologues. All MutS homologues show high conservation within the ATPase domain. MutS1, the homologue responsible for DNA mismatch recognition,...

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Year 2008
Year 2005
Year 2003

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