Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Antonio N. Calabrese"'
Autor:
Bob Schiffrin, Joel A. Crossley, Martin Walko, Jonathan M. Machin, G. Nasir Khan, Iain W. Manfield, Andrew J. Wilson, David J. Brockwell, Tomas Fessl, Antonio N. Calabrese, Sheena E. Radford, Anastasia Zhuravleva
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract The ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria, and delivers them to the β-barrel assembly machinery (BAM) for folding into the outer membrane
Externí odkaz:
https://doaj.org/article/b8ce23fd6b774989b970d0af57f9265e
Autor:
Katherine L. Fenn, Jim E. Horne, Joel A. Crossley, Nils Böhringer, Romany J. Horne, Till F. Schäberle, Antonio N. Calabrese, Sheena E. Radford, Neil A. Ranson
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel asse
Externí odkaz:
https://doaj.org/article/e2d6b62a22094d6bb6804c36a81d4e8a
Autor:
Christopher M. Jones, Arndt Rohwedder, Kin Man Suen, Safoura Zahed Mohajerani, Antonio N. Calabrese, Sabine Knipp, Mark T. Bedford, John E. Ladbury
Publikováno v:
Heliyon, Vol 10, Iss 15, Pp e35480- (2024)
Receptor tyrosine kinase (RTK) overexpression is linked to the development and progression of multiple cancers. RTKs are classically considered to initiate cytoplasmic signalling pathways via ligand-induced tyrosine phosphorylation, however recent ev
Externí odkaz:
https://doaj.org/article/756db033cc9a4969828da63cff6be9ba
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
Using Guanidium HCl denatured glyceraldehyde 3-phosphate dehydrogenase (GAPDH), the authors provide in vitro evidence for the active involvement of the trigger factor (TF) in promoting the native folding of pre-unfolded client proteins, by preventing
Externí odkaz:
https://doaj.org/article/c6fccd5e4bdc4f9e8591e0fdb1ec296d
Autor:
Bob Schiffrin, Jonathan M. Machin, Theodoros K. Karamanos, Anastasia Zhuravleva, David J. Brockwell, Sheena E. Radford, Antonio N. Calabrese
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-15 (2022)
Interaction of the outer membrane protein (OMP) chaperone SurA and the OMP folding catalyst BAM results in changes in the conformational ensembles of both species, suggesting a mechanism for delivery of OMPs to BAM in Gram-negative bacteria.
Externí odkaz:
https://doaj.org/article/49dc31e55c1c4e7abc6e6cd217e49c7b
Autor:
Benjamin J. Lane, Bolin Wang, Yue Ma, Antonio N. Calabrese, Hassane El Mkami, Christos Pliotas
Publikováno v:
STAR Protocols, Vol 3, Iss 3, Pp 101562- (2022)
Summary: Solvent accessibilities of and distances between protein residues measured by pulsed-EPR approaches provide high-resolution information on dynamic protein motions. We describe protocols for the purification and site-directed spin labeling of
Externí odkaz:
https://doaj.org/article/ad4467d6af924332936f59ebd54c7f43
Autor:
Paul White, Samuel F. Haysom, Matthew G. Iadanza, Anna J. Higgins, Jonathan M. Machin, James M. Whitehouse, Jim E. Horne, Bob Schiffrin, Charlotte Carpenter-Platt, Antonio N. Calabrese, Kelly M. Storek, Steven T. Rutherford, David J. Brockwell, Neil A. Ranson, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of
Externí odkaz:
https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d
Autor:
Matthew G. Iadanza, Bob Schiffrin, Paul White, Matthew A. Watson, Jim E. Horne, Anna J. Higgins, Antonio N. Calabrese, David J. Brockwell, Roman Tuma, Antreas C. Kalli, Sheena E. Radford, Neil A. Ranson
Publikováno v:
Communications Biology, Vol 3, Iss 1, Pp 1-14 (2020)
With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BA
Externí odkaz:
https://doaj.org/article/cc183779d41f4d5aabd191eaa4c934aa
Autor:
Antonio N. Calabrese, Bob Schiffrin, Matthew Watson, Theodoros K. Karamanos, Martin Walko, Julia R. Humes, Jim E. Horne, Paul White, Andrew J. Wilson, Antreas C. Kalli, Roman Tuma, Alison E. Ashcroft, David J. Brockwell, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show ho
Externí odkaz:
https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a
Publikováno v:
Frontiers in Chemistry, Vol 9 (2021)
Intrinsically disordered proteins (IDPs) and regions of intrinsic disorder (IDRs) are abundant in proteomes and are essential for many biological processes. Thus, they are often implicated in disease mechanisms, including neurodegeneration and cancer
Externí odkaz:
https://doaj.org/article/298bfb4ae898471284c2c29fd4a15489