Zobrazeno 1 - 10
of 44
pro vyhledávání: '"J.M. Diprose"'
Autor:
Mark S.P. Sansom, Trevor G. Smart, Zhaoyang Sun, Els Pardon, Gianni Klesse, Sreenivas Chavali, Saad Hannan, J.M. Diprose, S. Masiulis, Luigi De Colibus, Abhay Kotecha, Shanlin Rao, Paul S. Miller, Brandon Frenz, Juha T. Huiskonen, Stephen J. Tucker, Frank DiMaio, Suzanne Scott, Tomas Malinauskas, Alistair Siebert, Robert Esnouf, Radu Aricescu, Sai Li, Jan Steyaert, M. Madan Babu
Type-A γ-aminobutyric acid (GABAA) receptors are pentameric ligand-gated ion channels (pLGICs), typically consisting of α/β/γ subunit combinations. They are the principal mediators of inhibitory neurotransmission throughout the central nervous sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3d5673ebc6cb19d77170ae851e68ebf
https://doi.org/10.1101/338343
https://doi.org/10.1101/338343
Autor:
Robert Esnouf, Chris Morris, Susan Daenke, Edward Daniel, Christian Siebold, J.M. Diprose, Keith S. Wilson, David I. Stuart, Richard Blake, Marc Savitsky, B Lin, B. Bishop, Susanne L. Griffiths
Publikováno v:
Journal of Structural Biology
The Protein Information Management System (PiMS) is a laboratory information management system (LIMS) designed for use with the production of proteins in a research environment. The software is distributed under the CCP4 licence, and so is available
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cf919597678413351bcb4197758846d
https://doi.org/10.1016/j.jsb.2011.05.009
https://doi.org/10.1016/j.jsb.2011.05.009
Autor:
Nicola G. A. Abrescia, Geoffrey C. Sutton, J.M. Diprose, David I. Stuart, George J. Thomas, Jonathan M. Grimes, Joseph J.B. Cockburn, James M. Benevides, Jaana K. H. Bamford, Dennis H. Bamford
Membranes are essential for selectively controlling the passage of molecules in and out of cells and mediating the response of cells to their environment. Biological membranes and their associated proteins present considerable difficulties for struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64dacfdae4b7f947941614b036914bbd
https://ora.ox.ac.uk/objects/uuid:db15eb93-12df-419f-8e43-bff704e71b84
https://ora.ox.ac.uk/objects/uuid:db15eb93-12df-419f-8e43-bff704e71b84
Autor:
David I. Stuart, Peter P. C. Mertens, Geoff Sutton, Jonathan M. Grimes, Karin Anduleit, J.M. Diprose
Many insect viruses survive for long periods by occlusion within robust crystalline polyhedra composed primarily of a single polyhedrin protein. We show that two different virus families form polyhedra which, despite lack of sequence similarity in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc9c6fa0420e77fa3fcc8d1ad85331d0
https://ora.ox.ac.uk/objects/uuid:7633f42f-fb85-4d3d-95ca-212536e9f28d
https://ora.ox.ac.uk/objects/uuid:7633f42f-fb85-4d3d-95ca-212536e9f28d
Autor:
Louise E. Bird, J.M. Diprose, Raymond J. Owens, Heather Rada, John G. Flanagan, Robert J.C. Gilbert
Publikováno v:
DNA Cloning and Assembly Methods ISBN: 9781627037631
In-Fusion™ cloning is a fl exible DNA ligase-independent cloning technology that has wide-ranging uses in molecular biology. In this chapter we describe the protocols used in the OPPF-UK to design and construct expression vectors using In-Fusion™
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0582a7cb8ef67f9cabe1de68757f015
https://doi.org/10.1007/978-1-62703-764-8_15
https://doi.org/10.1007/978-1-62703-764-8_15
Autor:
J.N. Burroughs, Peter P. C. Mertens, Stéphan Zientara, Jonathan M. Grimes, R. Malby, J.M. Diprose, Patrice Gouet, David I. Stuart
Publikováno v:
Cell
Cell, Elsevier, 1999, 97, pp.481-490
Cell, Elsevier, 1999, 97, pp.481-490
International audience; The concentration of double-stranded RNA within the bluetongue virus core renders the genome segments liquid crystalline. Powder diffraction rings confirm this local ordering with a 30 A separation between strands. Determinati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70d0c1b4d476bb6e243921068323a372
https://doi.org/10.1016/s0092-8674(00)80758-8
https://doi.org/10.1016/s0092-8674(00)80758-8
Autor:
Susanne L. Griffiths, Kim Henrick, A. Pajon, M. Savitsky, James H. Naismith, Colin Nave, K. Pilicheva, Neil W. Isaacs, Robert Esnouf, Richard Blake, Chris Morris, A. Wilter da Silva, Keith S. Wilson, J.M. Diprose, David I. Stuart, Peter V Troshin, J. van Niekerk, E J Daniel, B Lin
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
The Protein Information Management System (PiMS) is described together with a discussion of how its features make it well suited to laboratories of all sizes.
The techniques used in protein production and structural biology have been developing
The techniques used in protein production and structural biology have been developing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd13cbd4ffb9fecac8b5c8d616ab1c4b
https://ora.ox.ac.uk/objects/uuid:16ff2ae0-64e7-4bfc-abfa-1ee7d95149b5
https://ora.ox.ac.uk/objects/uuid:16ff2ae0-64e7-4bfc-abfa-1ee7d95149b5
Autor:
Jaana K. H. Bamford, Jonathan M. Grimes, David I. Stuart, Dennis H. Bamford, J.M. Diprose, Geoff Sutton, Joseph J.B. Cockburn
It has proved difficult to obtain well diffracting single crystals of macromolecular complexes rich in lipid. We report here the path that has led to crystals of the bacteriophage PRD1, a particle containing approximately 2000 protein subunits from 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c81142841237bacb37fb6a0154ed6e30
https://doi.org/10.1016/s1047-8477(02)00562-2
https://doi.org/10.1016/s1047-8477(02)00562-2
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
A fast and easy tool to locate unit-cell matches in the PDB is described.
When embarking upon X-ray diffraction data collection from a potentially novel macromolecular crystal form, it can be useful to ascertain whether the measured data reflect
When embarking upon X-ray diffraction data collection from a potentially novel macromolecular crystal form, it can be useful to ascertain whether the measured data reflect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73d83d669ce10fc5e05b23fa92379dcd
https://doi.org/10.1107/s0907444912040590
https://doi.org/10.1107/s0907444912040590
Autor:
N. Levy, Yoav Peleg, Christoph Scheich, Renaud Vincentelli, V. Lieu, Loubna Salim, Didier Busso, C. Pinaglia, Gert E. Folkers, Konrad Büssow, Nick S. Berrow, M. Ekberg, Bruno Coutard, J.M. Diprose, Sophie Quevillon-Cheruel, Raymond J. Owens
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2006, 62 (Pt 10), pp.1218-26. ⟨10.1107/S0907444906031337⟩
Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2006, 62 (Pt 10), pp.1218-26. ⟨10.1107/S0907444906031337⟩
Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
Producing soluble proteins in Escherichia coli is still a major bottleneck for structural proteomics. Therefore, screening for soluble expression on a small scale is an attractive way of identifying constructs that are likely to be amenable to struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b6095f5f49a5a0708d8aa7826051676
https://doi.org/10.1107/s0907444906031337
https://doi.org/10.1107/s0907444906031337