"Leucine Zippers" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). The DNA-binding residues are located in the bifurcated region of the Y.
- Leucine Zippers
- Leucine Zipper
- Zipper, Leucine
- Zippers, Leucine
Below are MeSH descriptors whose meaning is more general than "Leucine Zippers".
Below are MeSH descriptors whose meaning is more specific than "Leucine Zippers".
This graph shows the total number of publications written about "Leucine Zippers" by people in this website by year, and whether "Leucine Zippers" was a major or minor topic of these publications.
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Below are the most recent publications written about "Leucine Zippers" by people in Profiles.
Pryciak PM. Systems biology. Customized signaling circuits. Science. 2008 Mar 14; 319(5869):1489-90.
Litman R, Peng M, Jin Z, Zhang F, Zhang J, Powell S, Andreassen PR, Cantor SB. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell. 2005 Sep; 8(3):255-65.
Wang H, San Agustin JT, Witman GB, Kilpatrick DL. Novel role for a sterol response element binding protein in directing spermatogenic cell-specific gene expression. Mol Cell Biol. 2004 Dec; 24(24):10681-8.
Friedman JS, Khanna H, Swain PK, Denicola R, Cheng H, Mitton KP, Weber CH, Hicks D, Swaroop A. The minimal transactivation domain of the basic motif-leucine zipper transcription factor NRL interacts with TATA-binding protein. J Biol Chem. 2004 Nov 05; 279(45):47233-41.
Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc Natl Acad Sci U S A. 2004 Feb 24; 101(8):2357-62.
Kaufmann WK, Heffernan TP, Beaulieu LM, Doherty S, Frank AR, Zhou Y, Bryant MF, Zhou T, Luche DD, Nikolaishvili-Feinberg N, Simpson DA, Cordeiro-Stone M. Caffeine and human DNA metabolism: the magic and the mystery. Mutat Res. 2003 Nov 27; 532(1-2):85-102.
Wolfe SA, Grant RA, Pabo CO. Structure of a designed dimeric zinc finger protein bound to DNA. Biochemistry. 2003 Nov 25; 42(46):13401-9.
Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR. A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. J Mol Biol. 2002 Aug 02; 321(1):1-6.
Persengiev SP, Devireddy LR, Green MR. Inhibition of apoptosis by ATFx: a novel role for a member of the ATF/CREB family of mammalian bZIP transcription factors. Genes Dev. 2002 Jul 15; 16(14):1806-14.
Zitzewitz JA, Ibarra-Molero B, Fishel DR, Terry KL, Matthews CR. Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. J Mol Biol. 2000 Mar 03; 296(4):1105-16.