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BIAL Foundation
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DE:"Protein-lipid interactions"
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Type Title Begin End
DocumentSpecific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins2014

Reference code: PT/FB
Entity holding: BIAL Foundation
Location: S. Mamede do Coronado
Title:
BIAL Foundation Archive
Start date: 1994
History:
The BIAL Foundation was created in 1994 by Laboratórios BIAL in conjunction with the Council of Rectors of Portuguese Universities. BIAL’s Foundation mission is to foster the scientific study of Man from both the physical and spiritual perspectives.
Along the years the BIAL Foundation has developed an important relationship with the scientific community, first in Portugal and after worldwide. Today it is an institution of reference which aims to stimulate new researches that may help people, promote more health and contribute to new milestones to gain access to knowledge.
Among its activities the BIAL Foundation manages the BIAL Award, created in 1984, one of the most important awards in the Health field in Europe. The BIAL Award rewards both the basic and the clinical research distinguishing works of major impact in medical research.
The BIAL Foundation also assigns Scientific Research Scholarships for the study of neurophysiological and mental health in people, arousing the interest of researchers in the areas of Psychophysiology and Parapsychology.
To date the BIAL Foundation has supported 461 projects, more than 1000 researchers, with research groups in twenty-seven countries, resulting, until April 2013, in about 600 full papers, out of which 172 published in indexed international journals with an average impact factor of 3.6 and a substantial number of citations (1665).
Since 1996 the BIAL Foundation organizes the Symposia entitled "Behind and Beyond the Brain", a Forum that gathers well renowned neurosciences speakers and the BIAL Foundation Fellows which are spread around the world.
Classified as an institution of public utility, the BIAL Foundation includes among its patrons the Portuguese President, the Portuguese Universities Rectors' Council and the Portuguese Medical Association.
URL: http://www.bial.com/pt/
Accessibility: By permission

Reference code: PT/FB/BL
Entity holding: BIAL Foundation
Title: BIAL Grants
Start date: 1994
History:
In 1994 the BIAL Foundation launched a programme of science research grants with the aim of encouraging the research into Man’s physical and mental processes, namely in fields still largely unexplored but which warrant further scientific analysis, as Psychophysiology and Parapsychology.
Since its launch, applications to the BIAL grants have been increasing. Up to now 461 projects have been supported, involving more than 1000 researchers from 27 countries.
The approved applications have benefited from grants in amounts comprised between €5,000 and €50, 000. The amount to be granted is fixed by the Scientific board according to the needs of each project.
The supported projects have originated, until April 2013, in about 600 full papers, 172 out of which were published in indexed international journals with an average impact factor of 3.6 and a substantial number of citations (1665).
Among the BIAL Foundation fellows is worth highlighting the presence of scientists from prestigious universities from the United States, United Kingdom, Australia, Russia, Germany, Japan, France, Canada, and many others.
The BIAL grants are promoted biannually.

Reference code: PT/FB/BL-2004
Location: Arquivo PCA - Pastas 1 a 25/2004
Title:
2004 Grants
Start date: 2005-01 - 2012-09
Dimension/support:
25 caixas de arquivo

Reference code: PT/FB/BL-2004-009
Location: Arquivo PCA - Pasta 8/2004
Title:
009 - Structural biology of human brain CNP, a protein essential for axonal survival
Duration: 2005-02 - 2007-04
Researcher(s):
Andreas Hofmann
Institution(s): Institute of Cell & Molecular Biology, The University of Edinburgh (UK)
Contents: Contents:
Bursary agreement
Application form
Correspondence
Financial report and expenditure documents
Progress report
Final report
Language: eng
Author:
Hofmann, A.
Number of reproductions:
1
Keywords:
Psychophysiology / Brain structure and function / Assessment tools

Reference code: PT/FB/BL-2004-009.08
Location: Arquivo PCA - Pasta 8/2004
Title:
Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins
Publication year: 2014
URL:
https://www.sciencedirect.com/science/article/pii/S0005273614002442?via%3Dihub
Abstract/Results: ABSTRACT:
VIsinin-LIke Proteins (VILIPs) are a subfamily of the Neuronal Calcium Sensor (NCS) proteins, which possess both N-myristoylation and EF-hand motifs allowing for a putative 'calcium-myristoyl switch' regulation mechanism. It has previously been established that myristoyl conjugation increases the affinity of proteins for membranes, but, in many cases, a second feature such as a cluster of positively-charged residues is needed for stable membrane binding. The interaction of two members of this family, VILIP-1 and VILIP-3, with Langmuir monolayers as membrane models has been investigated in order to study the effects of both myristoylation and the highly basic region containing conserved poly-lysine residues on membrane association kinetics and binding properties. Results show that in the presence of calcium, N-myristoylation significantly increases the kinetic rate of VILIP adsorption to the membrane. Additionally, the proteins bind to negatively charged phospholipids independently of the conjugated myristate moiety. Besides the regulatory effect of calcium on the rate of binding presumably due to exposure of the myristoyl moiety ascribed to their putative 'calcium-myristoyl switch', VILIP-1 and -3 also engage specific interactions with biomimetic membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2). The presence of PIP2 increases the membrane association rates of both VILIPs. Taken together, these results show the major kinetic role of N-myristoylation for membrane binding, and highlight the critical role of specific phosphoinositide interactions for membrane association of members of the VILIP family.
Accessibility: Document exists in file
Language:
eng
Author:
Rebaud, S.
Secondary author(s):
Wang, C. K., Sarkis, J., Mason, L., Simon, A., Blum, L. J., Hofmann, A., Girard-Egrot, A. P.
Document type:
Article
Number of reproductions:
1
Percentiles:
7
Reference:
Rebaud, S., Wang, C. K., Sarkis, J., Mason, L., Simon, A., Blum, L. J., Hofmann, A., Girard-Egrot, A. P. (2014). Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins. Biochimica et Biophysica Acta, 1838(10), 2698-2707. https://doi.org/10.1016/j.bbamem.2014.06.021
2-year Impact Factor: 3.836|2014
Times cited: 12|2024-02-02
Indexed document: Yes
Quartile: Q1
Keywords: Visinin-LIke Proteins (VILIPs) / Neuronal Calcium Sensor (NCS) proteins / Calcium-myristoyl switch / Phosphoinositides / Langmuir monolayer / Protein-lipid interactions

Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins

Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins