Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lauryn E. Sass"'
Publikováno v:
Biochemistry
MutS recognizes base-base mismatches and base insertions/deletions (IDLs) in newly replicated DNA. Specific interactions between MutS and these errors trigger a cascade of protein-protein interactions that ultimately lead to their repair. The inabili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::667278d183d31fb23e762b76e76246c9
https://doi.org/10.1021/bi401429b
https://doi.org/10.1021/bi401429b
Autor:
Aaron M. Leconte, Maha P. Patel, Lauryn E. Sass, Peter McInerney, Mirna Jarosz, Li Kung, Jayson L. Bowers, Philip R. Buzby, J. William Efcavitch, Floyd E. Romesberg
Publikováno v:
Angewandte Chemie. 122:6057-6060
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a40a7481540299573884ef4dbd24966b
https://doi.org/10.1002/ange.201001607
https://doi.org/10.1002/ange.201001607
Publikováno v:
Biochemistry. 49:3174-3190
The first step in DNA mismatch repair (MMR) is the recognition of DNA mismatches or nucleotide insertions/deletions (IDLs) by MutS and MutS homologs. To investigate the conformational properties of MutS-mismatch complexes, we used single-molecule flu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e729ab2092aa50e36d946522cd43e2d2
https://doi.org/10.1021/bi901871u
https://doi.org/10.1021/bi901871u
Publikováno v:
Nucleic Acids Research
Atomic force microscopy (AFM) is a powerful technique for examining the conformations of protein-DNA complexes and determining the stoichiometries and affinities of protein-protein complexes. We extend the capabilities of AFM to the determination of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::467947195d6c0118163195f417283c43
http://europepmc.org/articles/PMC1182163
http://europepmc.org/articles/PMC1182163
Autor:
Aaron M. Leconte, Maha P. Patel, Mirna Jarosz, Lauryn E. Sass, J. William Efcavitch, Peter McInerney, Floyd E. Romesberg, Li Kung, Philip R. Buzby, Jayson Bowers
Publikováno v:
Angewandte Chemie (International ed. in English). 49(34)
We present the application of an activity-based phage display method to identify DNA polymerases tailored for next generation sequencing applications. Using this approach, we identify a mutant of Taq DNA polymerase that incorporates the fluorophore-l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fa5b66fcba2f0221b42f66571f6d699
https://pubmed.ncbi.nlm.nih.gov/20629059
https://pubmed.ncbi.nlm.nih.gov/20629059
Autor:
Jeffrey G. Reifenberger, Adam R. Platt, Jayson Bowers, Lauryn E. Sass, Mirna Jarosz, Patrice M. Milos, Dan Jones, Fatih Ozsolak, John F. Thompson, Peter McInerney
Publikováno v:
Nature. 461(7265)
Our understanding of human biology and disease is ultimately dependent on a complete understanding of the genome and its functions. The recent application of microarray and sequencing technologies to transcriptomics has changed the simplistic view of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::987a6f8671581faa42bb7a5d3c196b9d
https://pubmed.ncbi.nlm.nih.gov/19776739
https://pubmed.ncbi.nlm.nih.gov/19776739
Publikováno v:
Frontiers in Optics 2009/Laser Science XXV/Fall 2009 OSA Optics & Photonics Technical Digest.
Crystal structures of mismatch repair proteins bound to mismatched DNA reveal kinked DNA. With single molecule FRET we observed dynamic switching among different bent states, which suggests the dynamics of bending may influence mismatch repair.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3683846d5826d53cdce5c224a5b01162
https://doi.org/10.1364/ls.2009.lsthd3
https://doi.org/10.1364/ls.2009.lsthd3