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Vincent Raussens

Vincent Raussens,Université Libre de Bruxelles,Biophysics,Molecular Biology,Plant & Animal Science

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Vincent Raussens

Université Libre de Bruxelles

Publications: 18 | Citations: 172

Fields: Biophysics, Molecular Biology, Plant & Animal Science

Collaborated with 53 co-authors from 1996 to 2011 | Cited by 647 authors

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Publications (18)

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Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

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Journal: Experientia , vol. 68, no. 8, pp. 1429-1438, 2011

Calcium Ions Promote Formation of Amyloid beta-Peptide (1-40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease (Citations: 1)

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Journal: PLOS One , 2011

Acylated and unacylated ghrelin binding to membranes and to ghrelin receptor: Towards a better understanding of the underlying mechanisms

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Journal: Biochimica Et Biophysica Acta-biomembranes - BBA-BIOMEMBRANES , vol. 1798, no. 11, pp. 2102-2113, 2010

Aggregation of the Aβ(1-40) peptide: Secondary structure change from oligomers to fibrils

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Journal: Alzheimers & Dementia - ALZHEIMERS DEMENT , vol. 6, no. 4, pp. S242-S242, 2010

Corrigendum to “Purification and characterization of a wound-inducible thaumatin-like protein from the latex of Carica papaya” [Phytochemistry 70 (2009) 970–978]

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Journal: Phytochemistry , vol. 71, no. 10, pp. 1181-1181, 2010

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Citations (172 times by 158 publications)

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

, , , , , ,

Journal: Experientia , vol. 68, no. 8, pp. 1429-1438, 2011

Utilization of the sludge derived from dyestuff-making wastewater coagulation for unfired bricks (Citations: 1)

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Journal: Construction and Building Materials - CONSTR BUILD MATER , vol. 25, no. 4, pp. 1699-1706, 2011

Laticifer proteins play a defensive role against hemibiotrophic and necrotrophic phytopathogens (Citations: 1)

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Journal: Planta , vol. 234, no. 1, pp. 183-193, 2011

Selenomethionine Incorporation into Amyloid Sequences Regulates Fibrillogenesis and Toxicity

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Journal: PLOS One , vol. 6, no. 11, 2011

Assessment of cardiac involvement of hepatitis C virus; tissue Doppler imaging and NTproBNP study

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Journal: Journal of The Saudi Heart Association , vol. 23, no. 4, pp. 217-223, 2011

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Co-authors (53)

Journals (12)

Keywords (64)

Vincent Raussens,Université Libre de Bruxelles,Biophysics,Molecular Biology,Plant & Animal Science

Publications (18)

BibTeX | RIS | RefWorks Download

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

Calcium Ions Promote Formation of Amyloid beta-Peptide (1-40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease (Citations: 1)

Acylated and unacylated ghrelin binding to membranes and to ghrelin receptor: Towards a better understanding of the underlying mechanisms

Aggregation of the Aβ(1-40) peptide: Secondary structure change from oligomers to fibrils

Corrigendum to “Purification and characterization of a wound-inducible thaumatin-like protein from the latex of Carica papaya” [Phytochemistry 70 (2009) 970–978]

Citations (172 times by 158 publications)

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

Utilization of the sludge derived from dyestuff-making wastewater coagulation for unfired bricks (Citations: 1)

Laticifer proteins play a defensive role against hemibiotrophic and necrotrophic phytopathogens (Citations: 1)

Selenomethionine Incorporation into Amyloid Sequences Regulates Fibrillogenesis and Toxicity

Assessment of cardiac involvement of hepatitis C virus; tissue Doppler imaging and NTproBNP study


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Vincent Raussens,Université Libre de Bruxelles,Biophysics,Molecular Biology,Plant & Animal Science

Publications (18) BibTeX | RIS | RefWorks Download

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

Calcium Ions Promote Formation of Amyloid beta-Peptide (1-40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease (Citations: 1)

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure (Citations: 2)

Utilization of the sludge derived from dyestuff-making wastewater coagulation for unfired bricks (Citations: 1)

Laticifer proteins play a defensive role against hemibiotrophic and necrotrophic phytopathogens (Citations: 1)

Publications (18)

BibTeX | RIS | RefWorks Download