Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Orval A. Bateman"'
Autor:
J. Andrew Aquilina, Justin L. P. Benesch, Carol V. Robinson, Orval A. Bateman, Christine Slingsby
The quaternary structure of the polydisperse mammalian chaperone αB-crystallin, a member of the small heat-shock protein family, has been investigated by using electrospray mass spectrometry. The intact assemblies give rise to mass spectra that are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4afa6ea8d2c071c3bcb8a2af709fce
https://ora.ox.ac.uk/objects/uuid:c52ca492-3aa3-4527-8666-66a584656b2c
https://ora.ox.ac.uk/objects/uuid:c52ca492-3aa3-4527-8666-66a584656b2c
Autor:
Christine Slingsby, Orval A. Bateman, Sebastian M. Shimeld, Andrew G. Purkiss, Ron P. Dirks, Nicolette H. Lubsen
Publikováno v:
Current Biology, 15, 1684-1689
Current Biology, 15, 18, pp. 1684-1689
Current Biology, 15, 18, pp. 1684-1689
A refracting lens is a key component of our image-forming camera eye; however, its evolutionary origin is unknown because precursor structures appear absent in nonvertebrates. The vertebrate betagamma-crystallin genes encode abundant structural prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77d5a0dbda0bbc6526ce97c46007b165
https://doi.org/10.1016/j.cub.2005.08.046
https://doi.org/10.1016/j.cub.2005.08.046
A reference dataset for circular dichroism spectroscopy tailored for the βγ-crystallin lens proteins
Publikováno v:
Experimental Eye Research. 84:1001-1008
Circular dichroism (CD) spectroscopy is a powerful solution technique for the study of protein secondary structure. As hierarchical euclidean clustering analyses of high quality crystallin synchrotron radiation circular dichroism (SRCD) spectral data
Autor:
Graeme Wistow, Keith Wyatt, Christine Slingsby, Elena V. Orlova, Luchun Wang, Orval A. Bateman, Helen E. White
Publikováno v:
Structure. 14(12):1823-1834
Summary Lengsin is a major protein of the vertebrate eye lens. It belongs to the hitherto purely prokaryotic GS I branch of the glutamine synthetase (GS) superfamily, but has no enzyme activity. Like the taxon-specific crystallins, Lengsin is the res
Autor:
Steven L. Bernstein, Orval A. Bateman, Graeme Wistow, Chun Gao, Keith Wyatt, Stanislav I. Tomarev, Thomas S. Vihtelic, Larry L. David, Christine Slingsby, Lorenzo Segovia
Publikováno v:
FEBS Journal. 272:2276-2291
The β and γ crystallins are evolutionarily related families of proteins that make up a large part of the refractive structure of the vertebrate eye lens. Each family has a distinctive gene structure that reflects a history of successive gene duplic
Autor:
Keith Wyatt, Paul C. Evans, Graeme Wistow, Orval A. Bateman, Bonnie A. Wallace, Christine Slingsby
Publikováno v:
Journal of Molecular Biology. 343:435-444
Mutations in the human gammaD-crystallin gene have been linked to several types of congenital cataracts. In particular, the Pro23 to Thr (P23T) mutation of human gammaD crystallin has been linked to cerulean, lamellar, coralliform, and fasciculiform
Autor:
R. Sarra, Guido Kappé, Orval A. Bateman, Christine Slingsby, S.T. van Genesen, Nicolette H. Lubsen
Publikováno v:
Experimental Eye Research. 77:409-422
Crystallins are bulk structural proteins of the eye lens that have to last a life time. They gradually become modified with age, denature and form light scattering centres. High thermodynamic and kinetic stability of the crystallins enables them to r
Publikováno v:
Biochemistry. 42:4349-4356
Eta-crystallin is a retinal dehydrogenase that has acquired a role as a structural protein in the eye lens of elephant shrews, members of an ancient order of mammals. While it retains some activity toward retinal, which is oxidized to retinoic acid,
Autor:
Nicolette H. Lubsen, Julia M. Goodfellow, Christine Slingsby, Orval A. Bateman, Andrew G. Purkiss
Publikováno v:
Journal of Biological Chemistry. 277:4199-4205
gammaS-crystallin is a major human lens protein found in the outer region of the eye lens, where the refractive index is low. Because crystallins are not renewed they acquire post-translational modifications that may perturb stability and solubility.
Autor:
David S. Moss, A. Simpson, G. Wright, Orval A. Bateman, H.P.C. Driessen, P.F. Lindley, Benjamin D. Bax, B.V. Norledge, Christine Slingsby
Publikováno v:
Progress in Retinal and Eye Research. 16:3-29
The 3-dimensional organisation of crystallin polypeptides into globular proteins and their interactions into higher order structures are important factors governing optical functions related to refraction, accommodation and transparency. Single cryst