Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Naomi L. Pollock"'
Autor:
José Edwin Neciosup Quesñay, Naomi L. Pollock, Raghavendra Sashi Krishna Nagampalli, Sarah C. Lee, Vijayakumar Balakrishnan, Sandra Martha Gomes Dias, Isabel Moraes, Tim R. Dafforn, Andre Luis Berteli Ambrosio
Publikováno v:
Biology, Vol 9, Iss 11, p 407 (2020)
The molecular identity of the mitochondrial pyruvate carrier (MPC) was presented in 2012, forty years after the active transport of cytosolic pyruvate into the mitochondrial matrix was first demonstrated. An impressive amount of in vivo and in vitro
Externí odkaz:
https://doaj.org/article/cc68b4aa6d6349f296de57bf236d933c
Publikováno v:
AIMS Molecular Science, Vol 1, Iss 4, Pp 141-161 (2014)
The cystic fibrosis transmembrane conductance regulator protein (CFTR) is a chloride channel highly expressed in the gills of Salmo salar, with a role in osmoregulation. It shares 60% identity with the human CFTR channel, mutations to which can cause
Externí odkaz:
https://doaj.org/article/44ae11f3c8c040fdae28099ca76a2f94
Publikováno v:
Biochemical Journal. 479:145-159
ATP-binding cassette (ABC) proteins play important roles in cells as importers and exporters but as membrane proteins they are subject to well-known challenges of isolating pure and stable samples for study. One solution to this problem is to use sty
Publikováno v:
The Biochemical journal. 479(15)
Human BK channels are large voltage and Ca2+-activated K+ channels, involved in several important functions within the body. The core channel is a tetramer of α subunits, and its function is modulated by the presence of β and γ accessory subunits.
Autor:
Vijayakumar Balakrishnan, José Edwin Neciosup Quesñay, Naomi L. Pollock, Isabel Moraes, Sandra Martha Gomes Dias, Timothy R. Dafforn, Raghavendra Sashi Krishna Nagampalli, Andre Luis Berteli Ambrosio, Sarah C. Lee
Publikováno v:
Biology, Vol 9, Iss 407, p 407 (2020)
Biology
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Biology
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Simple Summary The atomic structure of a biological macromolecule determines its function. Discovering how one or more amino acid chains fold and interact to form a protein complex is critical, from understanding the most fundamental cellular process
Autor:
Abigail Otchere, Daniel N. Wiseman, David R. Poyner, Romez Uddin, Cathy Slack, Alice Rothnie, Sarah J Routledge, Roslyn M. Bill, Jaimin H. Patel, Alan D. Goddard, Naomi L. Pollock
Publikováno v:
Protein Expression and Purification
Given their extensive role in cell signalling, GPCRs are significant drug targets; despite this, many of these receptors have limited or no available prophylaxis. Novel drug design and discovery significantly rely on structure determination, of which
Autor:
Sophie J. Hesketh, Zoe Stroud, Alvin C. K. Teo, Timothy R. Dafforn, Sarah C. Lee, Corinne J. Smith, David I. Roper, Timothy J. Knowles, Corinne M. Spickett, Megha Rai, Pooja Sridhar, J. Malcolm East, Mayuriben J. Parmar, Stephen P Muench, Kailene S. Simon, Richard Collins, Vincent L. G. Postis, Saskia E. Bakker, C. Howard Barton, Naomi L. Pollock, Gregory Hurlbut
Most membrane proteins function through interactions with other proteins in the phospholipid bilayer, the cytosol or the extracellular milieu. Understanding the molecular basis of these interactions is key to understanding membrane protein function a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4184bd5543023d4d506e72952b00801a
Autor:
Alvin C. K. Teo, David I. Roper, Corinne M. Spickett, Timothy R. Dafforn, Naomi L. Pollock, Andrew R. Pitt, Sarah C. Lee, Zoe Stroud, Alpesh Thakker, Stephen Hall
Publikováno v:
Teo, A C K, Lee, S C, Pollock, N L, Stroud, Z, Hall, S, Thakker, A, Pitt, A R, Dafforn, T R, Spickett, C M & Roper, D I 2019, ' Analysis of SMALP co-extracted phospholipids shows distinct membrane environments for three classes of bacterial membrane protein ', Scientific Reports, vol. 9, no. 1, 1813 . https://doi.org/10.1038/s41598-018-37962-0
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Scientific Reports
Biological characterisation of membrane proteins lags behind that of soluble proteins. This reflects issues with the traditional use of detergents for extraction, as the surrounding lipids are generally lost, with adverse structural and functional co
Autor:
Naomi L. Pollock, Sarah C. Lee
Publikováno v:
Biochemical Society Transactions. 44:1011-1018
The use of styrene maleic acid lipid particles (SMALPs) for the purification of membrane proteins (MPs) is a rapidly developing technology. The amphiphilic copolymer of styrene and maleic acid (SMA) disrupts biological membranes and can extract membr
New technologies for the purification of stable membrane proteins have emerged in recent years, in particular methods that allow the preparation of membrane proteins with their native lipid environment. Here, we look at the progress achieved with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d02a609c1ef4968158aba95e4d1bd39
https://publications.aston.ac.uk/id/eprint/31426/1/Membrane_proteins_encapsulated_in_a_polymer_bound_lipid_bilayer.pdf
https://publications.aston.ac.uk/id/eprint/31426/1/Membrane_proteins_encapsulated_in_a_polymer_bound_lipid_bilayer.pdf