Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Dale A. Shepherd"'
Autor:
Lieke Lamont, Darya Hadavi, Andrew P. Bowman, Bryn Flinders, Dale Cooper‐Shepherd, Martin Palmer, Jan Jordens, Ynze Mengerink, Maarten Honing, James Langridge, Tiffany Porta Siegel, Rob J. Vreeken, Ron M. A. Heeren
Publikováno v:
Rapid Communications in Mass Spectrometry, 37(5):e9439. Wiley
RATIONALE: Isomeric separation of prostanoids is often a challenge and requires chromatography and time-consuming sample preparation. Multiple prostanoid isomers have distinct in vivo functions crucial to understand the inflammation process, includin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e451ae0bc9ff8f47267b260fc70b251
https://doi.org/10.1002/rcm.9439
https://doi.org/10.1002/rcm.9439
Autor:
Elsa Wagner-Rousset, Olivier Colas, Kevin Giles, Sarah Cianférani, Thomas Botzanowski, Evolène Deslignière, Oscar Hernandez-Alba, Alain Beck, Dale Cooper-Shepherd, Hélène Diemer, Guillaume Béchade
Publikováno v:
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press, ⟨10.1021/jasms.1c00151⟩
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press, ⟨10.1021/jasms.1c00151⟩
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press
International audience; Monoclonal antibodies (mAbs) have taken on an increasing importance for the treatment of various diseases, including cancers and immunological disorders. Disulfide bonds play a pivotal role in therapeutic antibody structure an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d8d2127da7e4623cbd97d46b87317e4
https://doi.org/10.1021/jasms.1c00151
https://doi.org/10.1021/jasms.1c00151
Autor:
Dale Cooper-Shepherd, Konstantinos Thalassinos, Rehana Akter, Kevin Giles, Aisha Ben-Younis, Michael Morris, Daniel P. Raleigh, Jakub Ujma, Charles Eldrid, Hannah M. Britt, Symeon Kalfas, Tristan Cragnolini, Nick Tomczyk
Publikováno v:
Journal of the American Society for Mass Spectrometry
Ion mobility coupled to mass spectrometry (IM-MS) is widely used to study protein dynamics and structure in the gas phase. Increasing the energy with which the protein ions are introduced to the IM cell can induce them to unfold, providing informatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbb5654ad0020d0a9d8f0dd3f7bb543d
http://europepmc.org/articles/PMC8172447
http://europepmc.org/articles/PMC8172447
Autor:
Jason Wildgoose, Darren Hewitt, Jeffery Mark Brown, Yu-Fu Lin, Dale Cooper-Shepherd, Dalton T. Snyder, Vicki H. Wysocki, James I. Langridge, Benjamin J. Jones
Publikováno v:
The Analyst
We describe the implementation of a simple three-electrode surface-induced dissociation (SID) cell on a cyclic ion mobility spectrometer (cIMS) and demonstrate the utility of multipass mobility separations for resolving multiple conformations of prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d758fa1b8c91c02a2e67670112dc8cc6
https://pubmed.ncbi.nlm.nih.gov/34632987
https://pubmed.ncbi.nlm.nih.gov/34632987
Autor:
Sophie Laurent, Patrick Flammang, Guillaume Caulier, Julien De Winter, Pascal Gerbaux, Dale Cooper-Shepherd, Emmanuel Colson, Jan Claereboudt, Corentin Decroo, Martin Palmer, Céline Henoumont
Publikováno v:
Journal of the American Society for Mass Spectrometry. 30:2228-2237
Modern mass spectrometry methods provide a huge benefit to saponin structural characterization, especially when combined with collision-induced dissociation experiments to obtain a partial description of the saponin (ion) structure. However, the comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::419d20fb681a7b9b5df595195a89d12e
https://doi.org/10.1007/s13361-019-02310-7
https://doi.org/10.1007/s13361-019-02310-7
Autor:
Hannah M. Britt, Tristan Cragnolini, Jakub Ujma, Daniel P. Raleigh, Symeon Kalfas, Rehana Akter, Konstantinos Thalassinos, Charles Eldrid, Nick Tomczyk, Dale Cooper-Shepherd, Michael A. Morris, Kevin Giles
Elucidating the properties of intrinsically disordered proteins (IDPs) and unfolded and partially folded states of globular proteins is challenging owing to their heterogeneous and dynamic nature. Protein unfolding and misfolding is a key feature of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e9f3029f6afb8b5b3d6c2c4cd70468f
https://doi.org/10.26434/chemrxiv.11687100.v1
https://doi.org/10.26434/chemrxiv.11687100.v1
Autor:
Justin L. P. Benesch, Georg K. A. Hochberg, Matteo T. Degiacomi, Indu Santhanagopalan, Elizabeth Vierling, Dale A. Shepherd
Publikováno v:
J Biol Chem
Journal of biological chemistry, 2018, Vol.293(51), pp.19511-19521 [Peer Reviewed Journal]
Journal of biological chemistry, 2018, Vol.293(51), pp.19511-19521 [Peer Reviewed Journal]
Small heat-shock proteins (sHsps) are ubiquitous molecular chaperones, and sHsp mutations or altered expression are linked to multiple human disease states. sHsp monomers assemble into large oligomers with dimeric substructure, and the dynamics of sH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::691cae40ea10f0934a210bd8718da55c
http://ora.ox.ac.uk/objects/uuid:
http://ora.ox.ac.uk/objects/uuid:
Autor:
Georg K. A. Hochberg, Erik G. Marklund, Weston B. Struwe, Eman Basha, Dale A. Shepherd, Martin R. Galpin, Timothy M. Allison, Elizabeth Vierling, Matteo T. Degiacomi, Andrew Baldwin, Michael T. Marty, Indu Santhanagoplan, Justin L. P. Benesch, Arthur Laganowsky
Publikováno v:
Science
Science, 2018, Vol.359(6378), pp.930-935 [Peer Reviewed Journal]
Science, 2018, Vol.359(6378), pp.930-935 [Peer Reviewed Journal]
Putting distance between protein relatives Many proteins form complexes to function. When the gene for a self-assembling protein duplicates, it might be expected that the related proteins (paralogs) would retain interfaces that would allow coassembly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15f82a9b77bd6be47e6d9d5f25bdf2ca
https://doi.org/10.1126/science.aam7229
https://doi.org/10.1126/science.aam7229
Publikováno v:
International Journal of Mass Spectrometry. 377:663-671
Polydispersity presents a considerable challenge for the detailed molecular characterisation of many proteins. This is because in most biophysical and structural biology approaches the molecules in solution are ensemble-averaged, obscuring difference
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10e636ed649a74ae3965dc1242ee50b2
https://doi.org/10.1016/j.ijms.2014.09.007
https://doi.org/10.1016/j.ijms.2014.09.007
Autor:
Dale A. Shepherd, Alison E. Ashcroft, Stefan M.V. Freund, Gilles J. P. Rautureau, Christopher M. Johnson, Valerie E. Pye, Jimmy Muldoon, Judit Vörös, Maike C. Jürgens, Neil M. Ferguson
Publikováno v:
Nature Chemical Biology. 9:540-547
Hepatitis B virus (HBV) is an infectious, potentially lethal human pathogen. However, there are no effective therapies for chronic HBV infections. Antiviral development is hampered by the lack of high-resolution structures for essential HBV protein-p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4faa9d61ff02a223d96c582c42604d5e
https://doi.org/10.1038/nchembio.1294
https://doi.org/10.1038/nchembio.1294