Výsledky vyhledávání - "S. J. Smerdon"

MRE11 stability is regulated by CK2-dependent interaction with R2TP complex

Autor: P, von Morgen, K, Burdova, T G, Flower, N J, O'Reilly, S J, Boulton, S J, Smerdon, L, Macurek, Z, Hořejší

Publikováno v: Oncogene

The MRN (MRE11–RAD50–NBS1) complex is essential for repair of DNA double-strand breaks and stalled replication forks. Mutations of the MRN complex subunit MRE11 cause the hereditary cancer-susceptibility disease ataxia-telangiectasia-like disorde

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f8f6e995c030e918902b543166318e33
https://pubmed.ncbi.nlm.nih.gov/28436950

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PhosphoSerine/threonine binding domains: you can't pSERious?

Autor: M B, Yaffe, S J, Smerdon

Publikováno v: Structure (London, England : 1993). 9(3)

The fundamental biological importance of protein phosphorylation is underlined by the existence of more than 500 protein kinase genes within the human genome. In many cases, phosphorylation on serine, threonine, and tyrosine residues creates binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::184cf0fc03d9cfec0ecbd7db750bbfb7
https://pubmed.ncbi.nlm.nih.gov/11286893

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The influence of DNA binding on the backbone dynamics of the yeast cell-cycle protein Mbp1

Autor: P B, McIntosh, I A, Taylor, T A, Frenkiel, S J, Smerdon, A N, Lane

Publikováno v: Journal of biomolecular NMR. 16(3)

Mbp1 is a transcription factor involved in the regulation of the cell cycle in yeast. The N-terminus of this protein contains a DNA binding domain that includes a winged helix-turn-helix motif. The C-terminal 24 residues of this domain (the 'tail') a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8992bd5eefc8c84d10318f6033bd8bfa
https://pubmed.ncbi.nlm.nih.gov/10805125

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1H, 15N and 13C assignments of the DNA binding domain of transcription factor Mbp1 from S. cerevisiae in both its free and the DNA bound forms, and 1H assignments of the free DNA

Autor: P B, McIntosh, I A, Taylor, S J, Smerdon, T A, Frenkiel, A N, Lane

Publikováno v: Journal of biomolecular NMR. 13(4)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4e50670eae076fd0501c768517f1f082
https://pubmed.ncbi.nlm.nih.gov/10353201

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X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications for Swi6 function

Autor: R, Foord, I A, Taylor, S G, Sedgwick, S J, Smerdon

Publikováno v: Nature structural biology. 6(2)

Swi6 is a 92,000 Mr protein common to two distinct transcriptional activation complexes (SBF and MBF) that coordinate gene expression at the G1-S boundary of the yeast cell cycle. The X-ray structure of a central 36,000 Mr fragment has been determine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a233d4b9d0f28ecb64dee1f6b63ef880
https://pubmed.ncbi.nlm.nih.gov/10048928

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Structural and functional architecture of the yeast cell-cycle transcription factor swi6

Autor: S G, Sedgwick, I A, Taylor, A C, Adam, A, Spanos, S, Howell, B A, Morgan, M K, Treiber, N, Kanuga, G R, Banks, R, Foord, S J, Smerdon

Publikováno v: Journal of molecular biology. 281(5)

The structural and functional organisation of Swi6, a transcriptional regulator of the budding yeast cell cycle has been analysed by a combination of biochemical, biophysical and genetic methods. Limited proteolysis indicates the presence of a approx

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4ead0745b5a3a03d9f10eb0464481c84
https://pubmed.ncbi.nlm.nih.gov/9719633

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The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution

Autor: I A, Taylor, M K, Treiber, L, Olivi, S J, Smerdon

Publikováno v: Journal of molecular biology. 272(1)

The structure of the DNA-binding domain of the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 has been solved using the multiwavelength anomalous diffraction (MAD) technique on crystals of selenomethionyl protein and refined at 2.1 A r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::54dc98ee5f186444ec65da49027bd80d
https://pubmed.ncbi.nlm.nih.gov/9299332

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Expression, purification, and crystallization of the DNA-binding domain from the Saccharomyces cerevisae cell-cycle transcription factor MBP-1

Autor: I A, Taylor, S J, Smerdon

Publikováno v: Proteins. 27(2)

A 124-residue N-terminal fragment corresponding to the DNA-binding domain of the Saccharomyces cerevisae cell-cycle transcription factor MBP-1 has been expressed with a hexahistidine affinity tag in E. coli and purified to apparent homogeneity. Cryst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cdf4842fb6035618dad86660c051db3c
https://pubmed.ncbi.nlm.nih.gov/9061798

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