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377 results on '"Barford D"'

14. Structure of the human CCAN bound to alpha satellite DNA

Author

Yatskevich, S., primary, Muir, K.W., additional, Bellini, D., additional, Zhang, Z., additional, Yang, J., additional, Tischer, T., additional, Predin, M., additional, Dendooven, T., additional, McLaughlin, S.H., additional, and Barford, D., additional

Published
2022
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22. Nsp7-Nsp8-Nsp12 SARS-CoV2 RNA-dependent RNA polymerase in complex with template:primer dsRNA and favipiravir-RTP

Author

Naydenova, K., primary, Muir, K.W., additional, Wu, L.F., additional, Zhang, Z., additional, Coscia, F., additional, Peet, M., additional, Castro-Hartman, P., additional, Qian, P., additional, Sader, K., additional, Dent, K., additional, Kimanius, D., additional, Sutherland, J.D., additional, Loewe, J., additional, Barford, D., additional, and Russo, C.J., additional

Published
2020
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24. CryoEM structure of the ternary DOCK2-ELMO1-RAC1 complex

Author

Chang, L., primary, Yang, J., additional, Chang, J.H., additional, Zhang, Z., additional, Boland, A., additional, McLaughlin, S.H., additional, Abu-Thuraia, A., additional, Killoran, R.C., additional, Smith, M.J., additional, Cote, J.F., additional, and Barford, D., additional

Published
2020
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25. CryoEM structure of the binary DOCK2-ELMO1 complex

Author

Chang, L., primary, Yang, J., additional, Chang, J.H., additional, Zhang, Z., additional, Boland, A., additional, McLaughlin, S.H., additional, Abu-Thuraia, A., additional, Killoran, R.C., additional, Smith, M.J., additional, Cote, J.F., additional, and Barford, D., additional

Published
2020
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42. Protein-Oligosaccharide Interactions: Lysozyme, Phosphorylase, Amylases

Author

Johnson, L. N., Cheetham, J., McLaughlin, P. J., Acharya, K. R., Barford, D., Phillips, D. C., Clarke, A., editor, Compans, R. W., editor, Cooper, M., editor, Eisen, H., editor, Goebel, W., editor, Koprowski, H., editor, Melchers, F., editor, Oldstone, M., editor, Vogt, P. K., editor, Wagner, H., editor, Wilson, I., editor, Clarke, Adrienne E., editor, and Wilson, Ian A., editor

Published
1988
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45. Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors

Author

Oikonomakos, N, Johnson, L, Acharya, K, Stuart, D, Barford, D, Hajdu, J, Varvill, K, Melpidou, A, Papageorgiou, T, and Graves, D

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, Phosphorylases, Protein Conformation, Stereochemistry, Biochemistry, Cofactor, Structure-Activity Relationship, chemistry.chemical_compound, Glycogen phosphorylase, X-Ray Diffraction, Phosphite anion, Animals, Organic chemistry, Phosphorylase b, Pyridoxal phosphate, Pyridoxal, Binding Sites, biology, Muscles, Phosphate, Phosphonate, Kinetics, A-site, chemistry, Pyridoxal Phosphate, biology.protein, Rabbits, Protein Binding
Abstract

The detailed environment of the essential cofactor pyridoxal 5'-phosphate in glycogen phosphorylase b, resulting from crystallographic refinement at 1.9-A resolution, is described. The pyridoxal ring is buried in a nonpolar site containing three aromatic rings while the 5'-phosphate group is highly solvated and makes only three direct contacts to the protein. The pyridine nitrogen interacts via a water with protein atoms. The crystal structures of three active derivatives of phosphorylase reconstituted with 5'-deoxypyridoxal 5'-methylenephosphonate (PDMP), 6-fluoropyridoxal 5'-phosphate (6-FPLP), and pyridoxal (PL) in place of the natural cofactor have been determined at 2.5-A resolution. The results for PDMP-phosphorylase show a closer proximity of the phosphonate group to the NZ atom of a lysine (Lys-574) than that observed in the native enzyme, consistent with /sup 31/P NMR studies that have shown a change in ionization state of the phosphonate group compared to the native cofactor phosphate. The replacement of the polar 5'-ester linkage by a CH/sub 2/ group results in a small shift of a water and its hydrogen-bonded tyrosine (Tyr-648). In 6-FPLP-phosphorylase the fluorine is accommodated with no significant change in structure. In PL-phosphorylase co-crystallized with 6.5 mM phosphite and 50 mM glucose, the phosphite anion binds to a site thatmore » is close to but distinguishable from the 5'-phosphate site of the coenzyme. In the presence of glucose, phosphite binding provides significant stability to the crystal structure of PL-phosphorylase (T state) through a number of polar interactions. The implications of these results on the role of PLP in phosphorylase are discussed.« less

Published
2016

47. KSR2 mutations are associated with obesity, insulin resistance, and impaired cellular fuel oxidation

Author

Pearce LR, Atanassova N, Banton MC, Bottomley B, van der Klaauw AA, Revelli JP, Hendricks A, Keogh JM, Henning E, Doree D, Jeter-Jones S, Garg S, Bochukova EG, Bounds R, Ashford S, Gayton E, Hindmarsh PC, Shield JP, Crowne E, Barford D, Wareham NJ, UK10K consortium, O'Rahilly S, Murphy MP, Powell DR, Barroso I, Farooqi IS, Pearce LR, Atanassova N, Banton MC, Bottomley B, van der Klaauw AA, Revelli JP, Hendricks A, Keogh JM, Henning E, Doree D, Jeter-Jones S, Garg S, Bochukova EG, Bounds R, Ashford S, Gayton E, Hindmarsh PC, Shield JP, Crowne E, Barford D, Wareham NJ, UK10K consortium, O'Rahilly S, Murphy MP, Powell DR, Barroso I, and Farooqi IS

Published
2013

48. Geology of the Cenozoic Indus Basin sedimentary rocks : paleoenvironmental interpretation of sedimentation from the western Himalaya during the early phases of India-Eurasia collision

Author

Henderson, A. L., Najman, Y., Parrish, R., BouDagher-Fadel, M., Barford, D., Garzanti, E., Ando, S., Henderson, A, Najman, Y, Parrish, R, BouDagher Fadel, M, Barford, D, Garzanti, E, and Ando', S

Subjects
paleoenvironment, continental collision, sedimentary rock, Himalayas, Cenozoic, Eurasian plate, suture zone, Tsangpo suture zone, Fore-arc basin, Ladakh-Himalaya, NW Himalaya, Tectonic evolution, U-Pb, Asia collision, Northwestern Himalaya, Continental-margin, Pakistan Himalaya, GEO/02 - GEOLOGIA STRATIGRAFICA E SEDIMENTOLOGICA, sedimentation, Indian plate, tectonic setting
Abstract

This study reassesses the stratigraphy, sedimentology, and provenance of the Indus Basin sedimentary rocks, deposited within the Indus Tsangpo Suture Zone (ITSZ) during the early phases of India-Eurasia collision. Using field observations, biostratigraphy, and petrographic and isotopic analyses we create a paleodepositional reconstruction within the paleotectonic setting of the early phases of India-Eurasia collision. We then re-examine existing constraints to the timing of India-Eurasia collision previously interpreted from the earliest occurrence of mixed Indian-and Eurasian-derived detritus in the succession. From mid-Cretaceous to early Paleocene times the Jurutze and Sumda Formations were deposited within an arc-bounded marine basin between the Dras and Kohistan-Ladakh Island arcs. The

Published
2010

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