Zobrazeno 1 - 10
of 13
pro vyhledávání: '"O. A. Bateman"'
Publikováno v:
BJOG: An International Journal of Obstetrics & Gynaecology. 116:49-59
The annual toll of losses resulting from poor pregnancy outcomes include half a million maternal deaths, more than three million stillbirths, of whom at least one million die during labour and 3.8 million neonatal deaths--up to half on the first day
Autor:
Eva-Maria Mayr, Rudi Glockshuber, O. A. Bateman, Christine Slingsby, H.P.C. Driessen, B.V. Norledge, Rainer Jaenicke
Publikováno v:
Nature Structural Biology. 3:267-274
We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal
Publikováno v:
Molecular Biology Reports. 17:185-195
Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs
Publikováno v:
BJOG : an international journal of obstetrics and gynaecology. 116
The annual toll of losses resulting from poor pregnancy outcomes include half a million maternal deaths, more than three million stillbirths, of whom at least one million die during labour and 3.8 million neonatal deaths--up to half on the first day
Publikováno v:
Biochemical Society Transactions. 19:853-858
Introduction The lens is a cellular structure formed from elongated fibre cells aligning into concentric layers that stack together with the organization of a uni-axial crystal 111. Within the fibre cells, where protein turnover is low, protein compo
Autor:
Karine Prat, O. A. Bateman, Annette Tardieu, Françoise Bonneté, Fériel Skouri-Panet, Nicolette H. Lubsen
Publikováno v:
Biophysical Chemistry
Biophysical Chemistry, Elsevier, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
Biophysical Chemistry, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
Biophysical Chemistry, Elsevier, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
Biophysical Chemistry, 2001, 89 (1), pp.65-76. ⟨10.1016/s0301-4622(00)00216-7⟩
International audience; Among lens crystallins, gamma -crystallins are particularly sensitive to oxidation, because of their high amount of Cys and Met residues. They have the reputation to induce, upon ageing, lens structural modifications leading t
Publikováno v:
Experimental eye research. 65(5)
gamma-Crystallins, although closely related in sequence, show intriguing differences in their temperature-dependent interactions: those that have a high or intermediate Tc for phase separation are cryoproteins whereas low Tc gamma-crystallins are not
Publikováno v:
European journal of clinical nutrition. 50(5)
To investigate the association between nutritional status, cell-mediated immune status and the incidence of acute lower respiratory infections (ALRI).Community-based longitudinal study.Three villages in rural Bangladesh at Matlab.696 children aged 0-
Autor:
Christine Slingsby, Benjamin D. Bax, Shabir Najmudin, R. Lapatto, Tom L. Blundell, David S. Moss, P.F. Lindley, O. A. Bateman, H.P.C. Driessen
Publikováno v:
Presbyopia Research ISBN: 9781441932174
The transparency of the lens depends on an even distribution of protein and water over distances comparable to the wavelength of light, while the degree of refraction is controlled partly by the ability of the lens to change shape. The core regions o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60ecb74dfaccf13c0e37823a311f17a2
https://doi.org/10.1007/978-1-4757-2131-7_5
https://doi.org/10.1007/978-1-4757-2131-7_5
Autor:
C. Slingsby, O. A. Bateman
Publikováno v:
Biochemistry. 29(28)
beta-Crystallins are complex eye lens proteins made up of several related basic and acidic subunits that combine to form differently sized oligomers each displaying extensive polydispersity. As the sequences are homologous to the X-ray-determined bil