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Conferences and Training Events

The Biochemical Society provides an extensive range of events, including scientific conferences, outreach activities, medal lectures and policy and education events.  

 

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Future Events > Biennial International LRRK2 Meeting

Biennial International LRRK2 Meeting

2-4 September 2018

TBC, Italy



A Biochemical Society Focused Meeting

 

Leucine Rich Repeat Kinase 2 has emerged as a major genetic determinant of Parkinson's disease, placing this multidomain enzyme at the core of research efforts for the development of both disease modifying therapies as well as disease related biomarkers. Given the success of the previous LRRK2 focused meetings, we launch a third edition of this event where the latest biochemical, cellular and translational LRRK2 research will be discussed in the frame of future clinical applications.

Topics include:

- LRRK2 genetics

- LRRK2 structural biology

- LRRK2 animal models

- LRRK2 in immune function

- LRRK2 intracellular pathways

- LRRK2/alpha-synuclein interaction in Parkinson's disease pathogenesis

- LRRK2 in neuronal function

- LRRK2 substrate and effectors

- LRRK2 pathways to clinic

- LRRK2 in other diseases

 

Abstract deadline: 2 July 2018

 

Earlybird registration deadline: 2 July 2018

 

Oral communication slots are available at this meeting. All attendees, particularly researchers in the early stages of their career, are invited to submit a poster abstract for consideration as an oral communication.

 

Student Bursaries are available for this meeting.

Not a member of the Biochemical Society? Join today and save up to £100 on your registration fee.

 

Image 


Molecular structures depicted in the logo have been reporduced from the following references:

- Guaitoli G, Raimondi F, Gilsbach B, Gómez-Llorente Y, Deyaert E, Renzi F, Li X, Schaffner A, Jagtap P, Boldt K, von Zweydorf F, Gotthardt K, Lorimer D, Yue Z, Burgin A, Janjic N, Sattler M, Versées W, Ueffing M, Ubarretxena-Belandia I, Kortholt A, Gloeckner C (2016) Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. PNAS, 113(30):E4357-66. http://www.pnas.org/content/113/30/E4357.long

- Sejwal K, Chami M, Rémigy H, Vancraenenbroeck R, Sibran W, Sütterlin R, Baumgartner P, McLeod R, Chartier-Harlin MC, Baekelandt V, Stahlberg H, Taymans J-M (2017) Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes. Scientific Reports, 7(1):8667. 

https://www.nature.com/articles/s41598-017-09126-z