Zobrazeno 1 - 10
of 452
pro vyhledávání: '"Beat H Meier"'
Autor:
Ricardo Guerrero-Ferreira, Nicholas MI Taylor, Ana-Andreea Arteni, Pratibha Kumari, Daniel Mona, Philippe Ringler, Markus Britschgi, Matthias E Lauer, Ali Makky, Joeri Verasdonck, Roland Riek, Ronald Melki, Beat H Meier, Anja Böckmann, Luc Bousset, Henning Stahlberg
Publikováno v:
eLife, Vol 8 (2019)
Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibr
Externí odkaz:
https://doaj.org/article/5511896652574ffdab1b13b67a01332c
A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein
Autor:
Lukas Frey, Jiangtao Zhou, Gea Cereghetti, Marco E. Weber, David Rhyner, Aditya Pokharna, Luca Wenchel, Harindranath Kadavath, Yiping Cao, Beat H. Meier, Matthias Peter, Jason Greenwald, Roland Riek, Raffaele Mezzenga
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Reversible and irreversible amyloids are two diverging cases of protein (mis)folding associated with the cross-β motif in the protein folding and aggregation energy landscape. Yet, the molecular origins responsible for the formation of reve
Externí odkaz:
https://doaj.org/article/8b5b5edb4fa34aebba0ca7e2954be041
Autor:
Daniel Stöppler, Alex Macpherson, Susanne Smith-Penzel, Nicolas Basse, Fabien Lecomte, Hervé Deboves, Richard D Taylor, Tim Norman, John Porter, Lorna C Waters, Marta Westwood, Ben Cossins, Katharine Cain, James White, Robert Griffin, Christine Prosser, Sebastian Kelm, Amy H Sullivan, David Fox, Mark D Carr, Alistair Henry, Richard Taylor, Beat H Meier, Hartmut Oschkinat, Alastair D Lawson
Publikováno v:
PLoS Biology, Vol 16, Iss 5, p e2006192 (2018)
Aiming at the design of an allosteric modulator of the neonatal Fc receptor (FcRn)-Immunoglobulin G (IgG) interaction, we developed a new methodology including NMR fragment screening, X-ray crystallography, and magic-angle-spinning (MAS) NMR at 100 k
Externí odkaz:
https://doaj.org/article/8aa07cda1edf4eacba469577557c2556
The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili
Autor:
Dawid S. Zyla, Thomas Wiegand, Paul Bachmann, Rafal Zdanowicz, Christoph Giese, Beat H. Meier, Gabriel Waksman, Manuela K. Hospenthal, Rudi Glockshuber
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA a
Externí odkaz:
https://doaj.org/article/884d08eb71b24e7aa30ce532b269e3b7
Publikováno v:
Frontiers in Molecular Biosciences, Vol 2 (2015)
Recently the 3D structure of the Osaka mutant form (E22Δ) of Amyloid-β1-40 has been determined. We here compare the NMR chemical-shift with the published shifts of a brain-seeded form of wild-type Aβ and suggest that the determined mutant fold is
Externí odkaz:
https://doaj.org/article/f1d5e879081c4cb8b4168056daf666a1
Autor:
Britta eKunert, Carole eGardiennet, Denis eLacabanne, Daniel eCalles-Garcia, Pierre eFalson, Jean-Michel eJault, Beat H Meier, Penin eFrancois, Anja eBöckmann
Publikováno v:
Frontiers in Molecular Biosciences, Vol 1 (2014)
We present solid-state NMR sample preparation and first 2D spectra of the Bacillus subtilis ATP-binding cassette transporter BmrA, a membrane protein involved in multidrug resistance. The homodimeric 130-kDa protein is a challenge for structural char
Externí odkaz:
https://doaj.org/article/af001a35af1f44a498e9b09af67f9f0c
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e90659 (2014)
We structurally compare, using solid-state NMR, two different polymorphs of α-synuclein which, as established recently, display contrasting biochemical properties, toxicity, and tropism for cells. We show that both forms, which can each be produced
Externí odkaz:
https://doaj.org/article/1f8e8b5f4b604242897b2a53b763e1d7
Autor:
Carolin Seuring, Jason Greenwald, Christian Wasmer, Roger Wepf, Sven J Saupe, Beat H Meier, Roland Riek
Publikováno v:
PLoS Biology, Vol 10, Iss 12, p e1001451 (2012)
The HET-s protein from the filamentous fungus Podospora anserina is a prion involved in a cell death reaction termed heterokaryon incompatibility. This reaction is observed at the point of contact between two genetically distinct strains when one har
Externí odkaz:
https://doaj.org/article/4d95b330bb97425cb7b5d1d55a63b52a
Autor:
Malgorzata Tokarska-Schlattner, Raquel F Epand, Flurina Meiler, Giorgia Zandomeneghi, Dietbert Neumann, Hans R Widmer, Beat H Meier, Richard M Epand, Valdur Saks, Theo Wallimann, Uwe Schlattner
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43178 (2012)
A broad spectrum of beneficial effects has been ascribed to creatine (Cr), phosphocreatine (PCr) and their cyclic analogues cyclo-(cCr) and phospho-cyclocreatine (PcCr). Cr is widely used as nutritional supplement in sports and increasingly also as a
Externí odkaz:
https://doaj.org/article/86b6e333407b4687a2bed2971b73ff3c
Autor:
Elodie Teissier, Giorgia Zandomeneghi, Antoine Loquet, Dimitri Lavillette, Jean-Pierre Lavergne, Roland Montserret, François-Loïc Cosset, Anja Böckmann, Beat H Meier, François Penin, Eve-Isabelle Pécheur
Publikováno v:
PLoS ONE, Vol 6, Iss 1, p e15874 (2011)
The broad-spectrum antiviral arbidol (Arb) inhibits cell entry of enveloped viruses by blocking viral fusion with host cell membrane. To better understand Arb mechanism of action, we investigated its interactions with phospholipids and membrane pepti
Externí odkaz:
https://doaj.org/article/b5018ec167664ed6b836c2e03b8ff3e2