Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta

Autor: A K Downing, Joanne M. O'Leary, Daniel B. Rifkin, Xuemei Yuan, J. Lack, Knott, Penny A. Handford

Almost all TGF-beta is secreted as part of a large latent complex. This complex is formed from three molecules, a latent transforming growth factor-beta binding protein (LTBP), which plays roles in targeting and activation, a latency associated pepti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee4da76a63c2c1308021b4257e07a4ac
https://doi.org/10.1016/j.jmb.2003.09.053

Identification and removal of O-linked and non-covalently linked sugars from recombinant protein produced using Pichia pastoris

Autor: Catherine M. Radcliffe, A. Kristina Downing, Antony C. Willis, Joanne M. O'Leary, Pauline M. Rudd, Raymond A. Dwek

Publikováno v: Protein Expression and Purification. 38:217-227

The use of the methylotrophic yeast Pichia pastoris for large-scale recombinant production of proteins for therapeutic uses and/or biophysical characterisation has been gaining popularity. Here we describe the use of this organism for the production

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41a00ed3f2973a6050983157421647fb
https://doi.org/10.1016/j.pep.2004.08.010

Isotopic labeling of recombinant proteins from the methylotrophic yeast Pichia pastoris

Autor: Andrew R, Pickford, Joanne M, O'Leary

Publikováno v: Methods in molecular biology (Clifton, N.J.). 278

The methylotrophic yeast Pichia pastoris is now an established expression system for the production of recombinant protein for nuclear magnetic resonance (NMR) studies. It is capable of expressing high levels of heterologous proteins and possesses th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fab263fa9b6bb5d521c1d5ebf42e636a
https://pubmed.ncbi.nlm.nih.gov/15317988

Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces

Autor: Paul N. Barlow, X. Wang, Christian Schmitz, J.P. Atkinson, Joanne M. O'Leary, Gordon M. Black, M. Krych, Krystyna Bromek, Dušan Uhrín, Stanislava Uhrínová

Publikováno v: O'Leary, JM, Bromek, K, Black, GM, Uhrinova, S, Schmitz, C, Wang, XF, Krych, M, Atkinson, JP, Uhrin, D & Barlow, PN 2004, ' Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces ', Protein Science, vol. 13, no. 5, pp. 1238-1250 . https://doi.org/10.1110/ps.03582704

The regulators of complement activation (RCA) are critical to health and disease because their role is to ensure that a complement-mediated immune response to infection is proportionate and targeted. Each protein contains an uninterrupted array of fr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cac8846c038461eeb5ce5a7a3eb421f
https://www.pure.ed.ac.uk/ws/files/7555483/PS_2004_Barlow.pdf