Martí Ninot‐Pedrosa

ORCID: 0000-0003-2851-9990
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About
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Research Areas
  • SARS-CoV-2 and COVID-19 Research
  • vaccines and immunoinformatics approaches
  • Alzheimer's disease research and treatments
  • Animal Virus Infections Studies
  • Supramolecular Self-Assembly in Materials
  • Virus-based gene therapy research
  • Computational Drug Discovery Methods
  • Advanced Biosensing Techniques and Applications
  • Advanced Proteomics Techniques and Applications
  • Drug Transport and Resistance Mechanisms
  • 14-3-3 protein interactions
  • Lipid Membrane Structure and Behavior

Université Claude Bernard Lyon 1
2021-2024

Centre National de la Recherche Scientifique
2021-2024

Institute for Research in Biomedicine
2016-2018

Significance Numerous reports indicate that amyloid-β peptide (Aβ) oligomers, considered the pathogenic molecular form of Aβ in Alzheimer´s disease (AD), exert their neurotoxicity within membrane. Therefore, it is critical to characterize them such an environment. Here, we worked with two major variants and handled as if they were membrane proteins. By doing so, found variant most strongly linked AD assembled into stable oligomers adopted a specific structure incorporated membranes pores,...

10.1073/pnas.1605104113 article EN Proceedings of the National Academy of Sciences 2016-09-12
Nadide Altincekic Sophie Marianne Korn Nusrat S. Qureshi Marie Dujardin Martí Ninot‐Pedrosa and 95 more Rupert Abele Marie Jose Abi Saad Caterina Alfano Fábio C. L. Almeida Islam Alshamleh Gisele Cardoso de Amorim Thomas K. Anderson Cristiane Dinis Anobom Chelsea Anorma Jasleen Kaur Bains Ad Bax Martin Blackledge Julius Blechar Anja Böckmann Louis Brigandat Anna L. Bula Matthias Bütikofer Aldo R. Camacho‐Zarco Teresa Carlomagno Ícaro Putinhon Caruso Betül Ceylan A. Chaikuad Feixia Chu Laura Cole Marquise G. Crosby Vanessa de Jesus Karthikeyan Dhamotharan Isabella C. Felli Jan Ferner Yanick Fleischmann Marie‐Laure Fogeron Nikolaos K. Fourkiotis Christin Fuks Boris Fürtig Angelo Gallo S.L. Gande Juan Gerez Dhiman Ghosh Francisco Gomes‐Neto Oksana Gorbatyuk Serafima Guseva Carolin Hacker Sabine Häfner Bing Hao Bruno Hargittay Katherine A. Henzler‐Wildman Jeffrey C. Hoch Katharina F. Hohmann Marie Hutchison Kristaps Jaudzems Katarina Jović Janina Kaderli G. Kalnins I. Kanepe Robert N. Kirchdoerfer John Kirkpatrick Stefan Knapp Robin Krishnathas Felicitas Kutz Susanne zur Lage Roderick Lambertz András Láng Douglas V. Laurents Lauriane Lecoq V.L. Linhard Frank Löhr Anas Malki Luiza M. Bessa Rachel W. Martin Tobias Matzel Damien Maurin Seth McNutt Nathane C. Mebus-Antunes Beat H. Meier Nathalie Meiser Miguel Mompeán Elisa Monaca Roland Montserret Laura Mariño Céline Moser Claudia Muhle‐Goll Thais C. Neves-Martins Xiamonin Ni Brenna Norton‐Baker Roberta Pierattelli Letizia Pontoriero Yulia Pustovalova Oliver Ohlenschläger Julien Orts Andrea T. Da Poian Dennis J. Pyper Christian Richter Roland Riek Chad M. Rienstra Angus J. Robertson

The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands redirection of scientific efforts criteria organized research projects. international COVID19-NMR consortium seeks provide such new approaches gathering expertise worldwide. In particular, making available viral proteins RNAs will pave way understanding molecular components in detail. resources provided through are fully disclosed accelerate access exploitation. NMR...

10.3389/fmolb.2021.653148 article EN cc-by Frontiers in Molecular Biosciences 2021-05-10

SARS-CoV-2 (SCoV2) and its variants of concern pose serious challenges to the public health. The increased vaccines, thus necessitating for development new intervention strategies including anti-virals. Within international Covid19-NMR consortium, we have identified binders targeting RNA genome SCoV2. We established protocols production NMR characterization more than 80 % all SCoV2 proteins. Here, performed an screening using a fragment library binding 25 proteins hits also against...

10.1002/anie.202205858 article EN cc-by Angewandte Chemie International Edition 2022-09-17

SARS-CoV-2, the virus responsible for COVID-19 pandemic, encodes several accessory proteins, among which ORF6, a potent interferon inhibitor, is recognized as one of most cytotoxic. Here, we investigated structure, oligomeric state, and membrane interactions ORF6 using NMR spectroscopy molecular dynamics simulations. Using chemical-shift-ROSETTA, show that in proteoliposomes adopts straight α-helical structure with an extended, rigid N-terminal part flexible C-terminal residues....

10.1021/jacs.4c17030 article EN Journal of the American Chemical Society 2025-05-15

Abstract ORF7b is an accessory protein of SARS-CoV-2, the virus behind COVID-19 pandemic. Using cell-free synthesized ORF7b, we experimentally show that assembles into stable multimers. The sequence shows a transmembrane segment, which multimerizes through leucine zipper. We hypothesize has potential to interfere with important cellular processes involve leucine-zipper formation, and present two particularly striking examples. First, zippers are central in heart rhythm regulation...

10.1101/2021.02.05.428650 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-02-05

Abstract SARS‐CoV‐2 (SCoV2) and its variants of concern pose serious challenges to the public health. The increased vaccines, thus necessitating for development new intervention strategies including anti‐virals. Within international Covid19‐NMR consortium, we have identified binders targeting RNA genome SCoV2. We established protocols production NMR characterization more than 80 % all SCoV2 proteins. Here, performed an screening using a fragment library binding 25 proteins hits also against...

10.1002/ange.202205858 article EN cc-by Angewandte Chemie 2022-09-17

SARS-CoV-2 carries a sizeable number of proteins that are accessory to replication but may be essential for virus–host interactions and modulation the host immune response. Here, we investigated structure largely unknown ORF7b, small membranous membrane protein SARS-CoV-2. We show structural predictions indicate transmembrane (TM) leucine zipper experimentally confirm predominantly α-helical secondary within phospholipid mimetic by solid-state NMR. also ORF7b forms heterogeneous higher-order...

10.1073/pnas.2407731121 article EN cc-by Proceedings of the National Academy of Sciences 2024-11-07

Background: The aggregation of the amyloid-beta peptide (Aβ) in brain is strongly associated with Alzheimer´s disease (AD). However, heterogeneous and transient nature this process has prevented identification exact molecular form Aβ responsible for neurotoxicity observed disease. Therefore, characterizing utmost importance field AD. Nuclear magnetic resonance spectroscopy (NMR) a technique that holds great potential to achieve goal. it requires use specific labels introduced through...

10.2174/2212796811666170206113722 article EN Current Chemical Biology 2017-04-27
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