Výsledky vyhledávání - "Thorsten B. Blum"

Akademický článek

Abstract OR-8: High-Resolution Structures of Microtubule-Drug Complexes Revealed by Cryo-EM

Autor: Kushal Sejwal, Thorsten B. Blum, Joseph Atherton, Ashwani Sharma, Natacha Olieric, Andrea E. Prota, Carolyn A. Moores, Michel O. Steinmetz

Publikováno v: International Journal of Biomedicine, Vol 9, Iss Suppl_1, Pp S9-S9 (2019)

Background: Microtubules are dynamic protein filaments that are crucial for cell division and constitute key elements of the cytoskeleton. They are assembled from αβ-tubulin heterodimers that form hollow cylindrical structures. There is a large num

Externí odkaz: https://doaj.org/article/a1867fbadfe041bc8abc03f9441aa9c9

Zobrazit plný text záznamu

Cryo‐electron Microscopy Imaging of Alzheimer's Amyloid‐beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold

Autor: Daniel P. Farrell, Thorsten B. Blum, Frank DiMaio, Jinming Wu, Jan Pieter Abrahams, Jinghui Luo

Publikováno v: Angewandte Chemie (International Ed. in English)

Amyloid‐β peptide (Aβ) oligomers are pathogenic species of amyloid aggregates in Alzheimer's disease. Like certain protein toxins, Aβ oligomers permeabilize cellular membranes, presumably through a pore formation mechanism. Owing to their struct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d2d1b98ad20d599d0b372e482a06a5c
http://europepmc.org/articles/PMC8457241

Zobrazit plný text záznamu

VASH1-SVBP and VASH2-SVBP generate different detyrosination profiles on microtubules

Autor: Sacnicte Ramirez-Rios, Sung Ryul Choi, Chadni Sanyal, Thorsten B. Blum, Christophe Bosc, Fatma Krichen, Eric Denarier, Jean-Marc Soleilhac, Béatrice Blot, Carsten Janke, Virginie Stoppin-Mellet, Maria M. Magiera, Isabelle Arnal, Michel O. Steinmetz, Marie-Jo Moutin

Publikováno v: The Journal of cell biology. 222(2)

The detyrosination/tyrosination cycle of α-tubulin is critical for proper cell functioning. VASH1-SVBP and VASH2-SVBP are ubiquitous enzyme complexes involved in microtubule detyrosination. However, little is known about their mode of action. Here,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4965e10aa01e8f59f70566810218b744
https://pubmed.ncbi.nlm.nih.gov/36512346

Zobrazit plný text záznamu

Rational Design of a Novel Tubulin Inhibitor with a Unique Mechanism of Action

Autor: Tobias Mühlethaler, Lampros Milanos, Jose Antonio Ortega, Thorsten B. Blum, Dario Gioia, Bibhas Roy, Andrea E. Prota, Andrea Cavalli, Michel O. Steinmetz

Publikováno v: Angewandte Chemie. 134

In this study, we capitalized on our previously performed crystallographic fragment screen and developed the antitubulin small molecule Todalam with only two rounds of straightforward chemical synthesis. Todalam binds to a novel tubulin site, disrupt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be20c20dcf6329e2f1ea656f9d1964d0
https://doi.org/10.1002/ange.202204052

Zobrazit plný text záznamu

Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core–Shell Nanostructures

Autor: Andrea D. Merg, Jan Pieter Abrahams, Eric van Genderen, Gavin Touponse, Vincent P. Conticello, Khalid Salaita, Xiaobing Zuo, Hanquan Su, Thorsten B. Blum, Alisina Bazrafshan

Publikováno v: Journal of the American Chemical Society. 141:20107-20117

Engineering free-standing 2D nanomaterials with compositional, spatial, and functional control across size regimes from the nano- to mesoscale represents a significant challenge. Herein, we demonstrate a straightforward strategy for the thermodynamic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0657ad5b8a4779f45dc2f291af756f5
https://doi.org/10.1021/jacs.9b09335

Zobrazit plný text záznamu

The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo

Autor: Thorsten B. Blum, Mathilda Fatton, Pilar Junier, Jan Pieter Abrahams, Sevasti Filippidou

Publikováno v: Scientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
Scientific Reports, 9:14948. NATURE PORTFOLIO
Scientific Reports

Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament’s supercoil. So far, all studied functional fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6267e05815b19eef9b763fceb9f8c431
http://link.springer.com/article/10.1038/s41598-019-51440-1

Zobrazit plný text záznamu

Plný text ve formátu HTML

Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals

Autor: Dominique Housset, Wai Li Ling, Thorsten B. Blum, Andrew A. McCarthy, Max T. B. Clabbers, Ulrich Zander, Maria Bacia-Verloop, Jan Pieter Abrahams, Eric van Genderen, Guy Schoehn

Publikováno v: Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2021, 77 (1), pp.75-85. ⟨10.1107/S2059798320014540⟩
Acta Crystallographica. Section D, Structural Biology
Acta crystallographica. Section D, Structural biology
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2021, 77 (1), pp.75-85. ⟨10.1107/S2059798320014540⟩
'Acta Crystallographica D ', vol: 77, pages: 75-85 (2021)

A likelihood-based method is improved to correct for dynamical scattering in weakly diffracting protein nanocrystals. The method has been tested on three protein crystals and yielded better refinement statistics and structure interpretations, includi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d097123e17ecde388744cb746f4cb949
https://hal.univ-grenoble-alpes.fr/hal-03119765

Zobrazit plný text záznamu

Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets

Autor: Vincent P. Conticello, Khalid Salaita, Xiaobing Zuo, Thorsten B. Blum, Hew Ming Helen Siaw, Arthur L. McCanna, Alisina Bazrafshan, Andrea D. Merg, Eric van Genderen, Gavin Touponse, R. Brian Dyer, Jan Pieter Abrahams

Publikováno v: Journal of the American Chemical Society. 142(47)

The fabrication of dynamic, transformable biomaterials that respond to environmental cues represents a significant step forward in the development of synthetic materials that rival their highly functional, natural counterparts. Here, we describe the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20124184699509ddf18cc63436e8125d
https://pubmed.ncbi.nlm.nih.gov/33170675

Zobrazit plný text záznamu

A lipocalin mediates unidirectional heme biomineralization in malaria parasites

Autor: Michael J. Blackman, Benjamin Drepper, Thomas Stach, Joachim M. Matz, Thorsten B. Blum, Kai Matuschewski, Lucy M. Collinson, Eric van Genderen, Peer Martin, Jan Pieter Abrahams, Alana Burrell

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences, 117(28), 16546-16556. NATL ACAD SCIENCES

Significance During blood-stage development, the malaria parasite replicates inside erythrocytes of the vertebrate host, where it engulfs and digests most of the available hemoglobin. This results in release of the oxygen-binding prosthetic group hem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cd99a457aa95ef38d87418bc7772d8e
https://hdl.handle.net/1887/3620604

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání