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Roberto Boi

Researcher

Roberto Boi
Researcher
roberto.boi@neuro.gu.se

Postal Address: Box 432, 40530 Göteborg
Visiting Address: Medicinaregatan 11-13 , 41390 Göteborg


Department of Physiology at Institute of Neuroscience and Physiology (More Information)
Box 432
405 30 Göteborg
Visiting Address: Medicinaregatan 11-13 , 413 90 Göteborg

About Roberto Boi

 Researcher at the University of Gothenburg, Department of Neuroscience and Physiology, Njurcentrum, since 2016.

My previous projects in Gothenburg (titles):
Geranylgeranylation of the RhoGTPase protein family in podocytes and its importance for preserving glomerular filter function (ongoing),
Melanocortin-1 receptor in nephrotic syndrome as a target for cytoskeletal stabilization of podocytes (recently published),
ARGHEF7 triggered activation of Rac-1 GTPase causes loss of stressed fibers in podocytes (ongoing),
clinical outcome forecast in patients with idiopathic membrane nephropathy of initial anti- PLA2R antibody levels (ongoing).

Curriculum vitae:

2013-2015: Researcher at the LVR Clinic, Duisburg-Essen University (Germany); PepMIP Marie Curie project. Evaluation and development of next generation separation materials, designed to bind amyloid beta peptides (supposed Alzheimer's disease biomarkers);

2008-2012: PhD in Proteomics, University "Cattolica del Sacro Cuore" in Rome (Italy): Proteomics of saliva and other biological fluids, characterization of post-translational modifications of proteins and glycoproteins, their relevance to oral physiology;
2006-2008: Master's Degree in Experimental and Applied Biology (Cagliari University, Italy);

2003-2006: Bachelor's Degree in Experimental Biology (Cagliari

Publications:

[1] Amplification of the Melanocortin-1 Receptor in Nephrotic Syndrome Identifies a Target for Podocyte Cytoskeleton Stabilization. Sci Rep. 2018 Oct 24; 8 (1): 15731.

[2] HPLC-ESI-MS and MS / MS structural characterization of multi-fucosylated N-glycoforms of the basic proline rich protein IB-8a CON1 + in human saliva. J Sep Sci. 2012 May; 35 (9): 1079-86.

[3] The surprising composition of the salivary proteome or preterm human newborn. Mol Cell Proteomics. 2011 Jan; 10 (1): M110.003467.

[4] Age-dependent modifications of the human salivary secretory protein complex. J Proteome Res. 2009 Aug; 8 (8): 4126-34. doi: 10.1021 / pr900212u.

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