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X-WR-CALDESC:Eventos para BIFI -  - Institute for Biocomputation and Physics of Complex Systems
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DTSTART;TZID=Europe/Madrid:20240926T123000
DTEND;TZID=Europe/Madrid:20240926T143000
DTSTAMP:20260422T022102
CREATED:20240912T081134Z
LAST-MODIFIED:20240912T081134Z
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SUMMARY:BIFI TALK: Sylvie Callegari\, del Eliza Hall Institute of Medical Research\, Australia
DESCRIPTION:BIFI TALKS: Sylvie Callegari\, del Eliza Hall Institute of Medical Research\, Australia \nTitle: Activating PINK1 to treat Parkinson’s disease \nAbstract \nPINK1\, a protein linked to Parkinson’s disease\, is a ubiquitin kinase that accumulates on the outer membrane of damaged mitochondria. Upon accumulation\, PINK1 becomes activated and phosphorylates ubiquitin\, generating a unique phospho-ubiquitin signal that triggers mitophagy to remove damaged mitochondria. Enhancing PINK1 activation is a promising strategy for boosting mitochondrial turnover in Parkinson’s patients. Using Cryo-EM\, we recently elucidated the activation mechanism of PINK1 and used our structural platform to study PINK1 activator compounds\, overturning previous assumptions about their mechanism of action. Another therapeutic approach to target PINK1 is to enhance it’s stabilisation on the outer mitochondrial membrane\, but despite decades of research into PINK1 function\, the mechanism of PINK1 stabilisation has remained elusive. Using single particle cryo-EM\, we determine the structure of stabilised human PINK1 on the Translocase of the Outer Membrane (TOM) to a resolution of 2.8 Å. This uncovers an unusual arrangement of the TOM complex and challenges previous models on the mode of ubiquitin phosphorylation by PINK1. Understanding the mechanisms of PINK1 stabilisation and activation opens up new therapeutic possibilities for using PINK1 to promote the turnover of damaged mitochondria in Parkinson’s disease patients. \nThursday\, 26th September 2024\, 12:30 h\nEdificio I+D (Conference room)
URL:https://bifi.es/es/schedule/bifi-talk-sylvie-callegari-del-eliza-hall-institute-of-medical-research-australia/
LOCATION:Edificio Institutos I+D\, Mariano Esquillor\, 50018 Zaragoza\, Zaragoza\, Zaragoza\, 50018\, España
CATEGORIES:Eventos
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DTSTART;TZID=Europe/Madrid:20240927T123000
DTEND;TZID=Europe/Madrid:20240927T143000
DTSTAMP:20260422T022102
CREATED:20240912T081614Z
LAST-MODIFIED:20240912T081647Z
UID:8296-1727440200-1727447400@bifi.es
SUMMARY:BIFI TALK: José Manuel Martín García\, Instituto Blas Cabrera\, CSIC\, Madrid
DESCRIPTION:BIFI TALK: José Manuel Martín García\, del Instituto Blas Cabrera\, CSIC\, Madrid \nTitle: Time-resolved structural studies with serial crystallography: A new frontier in biomedical research. \nAbstract \nStructural biology\, especially X-ray crystallography\, has significantly advanced our understanding of diseases by revealing the 3D structures of proteins. However\, traditional X-ray crystallography encounters challenges\, such as difficulties in obtaining suitable protein crystals and studying protein dynamics. X-ray free-electron lasers (XFELs) have transformed this field with their bright and brief X-ray pulses\, allowing for high-resolution structures of radiation-sensitive and hard-to-crystallize proteins. With XFELs\, structural biology is also shifting its focus from determining static structures to exploring the dynamic aspects of protein function. A key tool for investigating these dynamics is mix-and-inject time-resolved crystallography (MISC)\, which has emerged as a transformative approach in drug discovery\, offering unprecedented insights into the dynamic processes of protein function. Traditional X-ray crystallography provides static snapshots of protein structures\, which\, while valuable\, do not capture the full complexity of molecular interactions and conformational changes critical to drug efficacy. MISC\, leveraging the capabilities of XFELs and advanced synchrotron sources\, allows researchers to observe proteins in action at atomic resolution and in real-time. This technique employs ultra-fast\, intense X-ray pulses to trigger and capture transient states and intermediates in biochemical reactions\, providing a dynamic view of protein-ligand interactions\, enzyme mechanisms\, and conformational changes. These insights are crucial for the rational design of drugs with improved specificity and efficacy. In this seminar\, I will introduce MISC at XFEL and synchrotron facilities\, as well as present some of the most recent results we have obtained in my group by applying this powerful technology to several biomedical research projects. \nFRIDAY\, 27th September 2024\, 12:30 h\nEdificio I+D (Conference room) \n 
URL:https://bifi.es/es/schedule/bifi-talk-jose-manuel-martin-garcia-del-instituto-blas-cabrera-csic-madrid/
LOCATION:Edificio Institutos I+D\, Mariano Esquillor\, 50018 Zaragoza\, Zaragoza\, Zaragoza\, 50018\, España
CATEGORIES:Eventos
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