@article{
 title = {A structural analysis of DNA binding by myelin transcription factor 1 double zinc fingers},
 type = {article},
 year = {2013},
 pages = {35180-35191},
 volume = {288},
 id = {87086ec5-3591-3e63-826a-b7a3fde32906},
 created = {2023-01-10T01:44:47.925Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:44:47.925Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {Background: Myelin transcription factor 1 (MyT1) contains seven similar zinc finger domains that bind DNA specifically. Results: A three-dimensional structural model explains how a double zinc finger unit is able to recognize DNA. Conclusion: DNA-binding residues are conserved among all MyT1 zinc fingers, suggesting an identical DNA binding mode. Significance: Determination of the molecular details of DNA interaction will be crucial in understanding MyT1 function. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.},
 bibtype = {article},
 author = {Gamsjaeger, R. and O'Connell, M.R. and Cubeddu, L. and Shepherd, N.E. and Lowry, J.A. and Kwan, A.H. and Vandevenne, M. and Swanton, M.K. and Matthews, J.M. and Mackay, J.P.},
 doi = {10.1074/jbc.M113.482075},
 journal = {Journal of Biological Chemistry},
 number = {49}
}

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