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EXAFS study of the zinc-binding sites in the protein transcription factor IIIA.
Diakun GP, Fairall L, Klug A. Diakun GP, et al. Among authors: klug a. Nature. 1986 Dec 18-31;324(6098):698-9. doi: 10.1038/324698a0. Nature. 1986. PMID: 3796733
It can be isolated from Xenopus laevis oocytes as a 7S particle in which the protein is associated with 5S RNA. Recently it has been shown that the native particle contains 7-11 zinc atoms. ...
It can be isolated from Xenopus laevis oocytes as a 7S particle in which the protein is associated with 5S RNA. Recently it has been …
Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition.
Lu D, Searles MA, Klug A. Lu D, et al. Among authors: klug a. Nature. 2003 Nov 6;426(6962):96-100. doi: 10.1038/nature02088. Nature. 2003. PMID: 14603324
Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger binding, both of which differ from that in common use for …
Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete …
Zinc mining for protein domains.
Schwabe JW, Klug A. Schwabe JW, et al. Among authors: klug a. Nat Struct Biol. 1994 Jun;1(6):345-9. doi: 10.1038/nsb0694-345. Nat Struct Biol. 1994. PMID: 7664042 No abstract available.
Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes.
Miller J, McLachlan AD, Klug A. Miller J, et al. Among authors: klug a. EMBO J. 1985 Jun;4(6):1609-14. EMBO J. 1985. PMID: 4040853 Free PMC article.
The 7S particle of Xenopus laevis oocytes contains 5S RNA and a 40-K protein which is required for 5S RNA transcription in vitro. ...The linear arrangement of these repeated, independently folding domains, each centred on a zinc ion, comprises the major part of the …
The 7S particle of Xenopus laevis oocytes contains 5S RNA and a 40-K protein which is required for 5S RNA transcription in vitro. ... …
Mapping of the sites of protection on a 5 S RNA gene by the Xenopus transcription factor IIIA. A model for the interaction.
Fairall L, Rhodes D, Klug A. Fairall L, et al. Among authors: klug a. J Mol Biol. 1986 Dec 5;192(3):577-91. doi: 10.1016/0022-2836(86)90278-0. J Mol Biol. 1986. PMID: 3560227
The results of quantitative measurements, combined with those from earlier DNase I and DNase II protection studies, are consistent with a series of multiple contacts about five base-pairs apart, or half a double-helical turn, along the whole length of the internal c …
The results of quantitative measurements, combined with those from earlier DNase I and DNase II protection studies, are consistent with a
The role of the central zinc fingers of transcription factor IIIA in binding to 5 S RNA.
Searles MA, Lu D, Klug A. Searles MA, et al. Among authors: klug a. J Mol Biol. 2000 Aug 4;301(1):47-60. doi: 10.1006/jmbi.2000.3946. J Mol Biol. 2000. PMID: 10926492
High-resolution footprinting by RNases A and CV1 has been used to probe the binding to 5 S RNA of three TFIIIA peptides Tf(1-6), Tf(4-6) and Tf(4-7), consisting of fingers 1 to 6, 4 to 6, and 4 to 7, respectively, and of full-length TFIIIA. ...A comparison of the fo …
High-resolution footprinting by RNases A and CV1 has been used to probe the binding to 5 S RNA of three TFIIIA peptides Tf(1-6), Tf(4 …
A role in DNA binding for the linker sequences of the first three zinc fingers of TFIIIA.
Choo Y, Klug A. Choo Y, et al. Among authors: klug a. Nucleic Acids Res. 1993 Jul 25;21(15):3341-6. doi: 10.1093/nar/21.15.3341. Nucleic Acids Res. 1993. PMID: 8346014 Free PMC article.
Structural investigations by 2D NMR in solution and by X-ray crystallographic analyses of complexes with DNA point to a passive role for the linkers. We have therefore investigated the influence of the linker sequence on DNA binding using as a model the first three …
Structural investigations by 2D NMR in solution and by X-ray crystallographic analyses of complexes with DNA point to a passive role …
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus.
Churchill ME, Tullius TD, Klug A. Churchill ME, et al. Among authors: klug a. Proc Natl Acad Sci U S A. 1990 Jul;87(14):5528-32. doi: 10.1073/pnas.87.14.5528. Proc Natl Acad Sci U S A. 1990. PMID: 2164687 Free PMC article.
The zinc finger protein TFIIIA, a positive transcription factor of the 5S RNA gene, binds to an internal control region of 50 nucleotides. ...Since then, evidence has accumulated on the structures of individual components of the complex--for example, zinc finger polypeptid …
The zinc finger protein TFIIIA, a positive transcription factor of the 5S RNA gene, binds to an internal control region of 50 nucleot …
In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence.
Choo Y, Sánchez-García I, Klug A. Choo Y, et al. Among authors: klug a. Nature. 1994 Dec 15;372(6507):642-5. doi: 10.1038/372642a0. Nature. 1994. PMID: 7990954
A DNA-binding peptide comprising three zinc-fingers has been engineered to bind specifically to a unique nine-base-pair region of a BCR-ABL fusion oncogene in preference to the parent genomic sequences. ...Consequently, murine cells rendered independent of gr
A DNA-binding peptide comprising three zinc-fingers has been engineered to bind specifically to a unique nine-base-pair region
Structure of nucleosome core particles of chromatin.
Finch JT, Lutter LC, Rhodes D, Brown RS, Rushton B, Levitt M, Klug A. Finch JT, et al. Among authors: klug a. Nature. 1977 Sep 1;269(5623):29-36. doi: 10.1038/269029a0. Nature. 1977. PMID: 895884
The core is a flat particle of dimensions about 110 X 110 X 57 A, somewhat wedge shaped, and strongly divided into two 'layers', consistent with the DNA being wound into about 1 3/4 turns of a flat superhelix of a pitch about 28 A. ...A c …
The core is a flat particle of dimensions about 110 X 110 X 57 A, somewhat wedge shaped, and strongly divided into two 'layers …
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