Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Theodoros K. Karamanos"'
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
Publikováno v:
Frontiers in Neuroscience, Vol 16 (2022)
The early stages of protein misfolding and aggregation involve disordered and partially folded protein conformers that contain a high degree of dynamic disorder. These dynamic species may undergo large-scale intra-molecular motions of intrinsically d
Externí odkaz:
https://doaj.org/article/72df3476b89d4aeaab15ffa13b618827
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
Autor:
Matthew G. Iadanza, Robert Silvers, Joshua Boardman, Hugh I. Smith, Theodoros K. Karamanos, Galia T. Debelouchina, Yongchao Su, Robert G. Griffin, Neil A. Ranson, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Impaired kidney function can lead to an increase of β2-microglobulin (β2m) serum levels, which can cause β2m aggregation and amyloid fibril formation. Here the authors combine cryo-EM and magic angle spinning NMR measurements to determine the stru
Externí odkaz:
https://doaj.org/article/c2131f4762074ff88b7f948f11bb5fd7
Autor:
Vitali Tugarinov, Yusuke Okuno, Francesco Torricella, Theodoros K. Karamanos, G. Marius Clore
Publikováno v:
The Journal of Physical Chemistry Letters. 13:11271-11279
Autor:
Theodoros K Karamanos, Matthew P Jackson, Antonio N Calabrese, Sophia C Goodchild, Emma E Cawood, Gary S Thompson, Arnout P Kalverda, Eric W Hewitt, Sheena E Radford
Publikováno v:
eLife, Vol 8 (2019)
Transient oligomers are commonly formed in the early stages of amyloid assembly. Determining the structure(s) of these species and defining their role(s) in assembly is key to devising new routes to control disease. Here, using a combination of chemi
Externí odkaz:
https://doaj.org/article/ae5e6a17dff3440081ba46090b9199cc
Autor:
Roberto, Maya-Martinez, Yong, Xu, Nicolas, Guthertz, Martin, Walko, Theodoros K, Karamanos, Frank, Sobott, Alexander L, Breeze, Sheena E, Radford
Publikováno v:
The Journal of biological chemistry. 298(12)
Self-association of WT β
Publikováno v:
Angewandte Chemie International Edition. 61
DNAJB6 is a prime example of an anti-aggregation chaperone that functions as an oligomer. DNAJB6 oligomers are dynamic and subunit exchange is critical for inhibiting client protein aggregation. The T193A mutation in the C-terminal domain (CTD) of DN
Publikováno v:
Journal of Biomolecular NMR. 74:673-680
Optimized selection of the slow-relaxing components of single-quantum 13C magnetization in 13CH3 methyl groups of proteins using acute (
Publikováno v:
ChemPhysChem. 21:1087-1091
Dynamics of protein side chains is one of the principal determinants of conformational entropy in protein structures and molecular recognition events. We describe NMR experiments that rely on the use of magic-angle pulses for efficient isolation of d