2014      2013      2012      2011


2014

  • Identification and affinity-quantification of ß-amyloid and α-synuclein polypeptides using on-line SAW-biosensor-mass spectrometry.
    Slamnoiu S, Vlad C, Stumbaum M, Moise A, Lindner K, Engel N, Vilanova M, Diaz M, Karreman C, Leist M, Ciossek T, Hengerer B, Vilaseca M, Przybylski M.
    J. Am. Soc. Mass Spectrom. 2014 Aug;25(8):1472-81
    Bioaffinity analysis using a variety of biosensors has become an established tool for detection and quantification of biomolecular interactions. Biosensors, however, are generally limited by the lack of chemical structure information ...
    http://www.ncbi.nlm.nih.gov/pubmed/24845351



    • 2013

  • Testing the feasibility of fully automated chip-based nanoelectrospray ionization mass spectrometry as a novel tool for rapid diagnosis of Fabry disease.
    Flangea C, Mosoarca C, Cozma C, Galusca M, Przybylski M, Zamfir AD.
    Electrophoresis. 2013 Jun;34(11):1572-80
    Fabry condition, a lysosomal storage disease (LSD) is characterized by the absence or reduction of the α-galactosidase A activity. Recently, a new diagnostic method for detection of α-galactosidase activity from dried blood spots (DBS) using a chemical substrate and quantification of reaction mixture...
    http://www.ncbi.nlm.nih.gov/pubmed/23483567



  • Epitope structure and binding affinity of single chain llama anti-ß-amyloid antibodies revealed by proteolytic excision affinity-mass spectrometry.
    Paraschiv G, Vincke C, Czaplewskac P, Manea M, Muyldermans S and Przybylski M
    J. Mol. Recognition, 2012, 26, 1–9
    ß-Amyloid (Aß) immunotherapy has become a promising strategy for reducing the level of Aß in brain. New immunological approaches have been recently proposed for rapid, early diagnosis, and molecular treatment of neurodegenerative diseases...
    http://www.ncbi.nlm.nih.gov/pubmed/23280612



  • Increased levels of antigen-bound ß-amyloid autoantibodies in serum and cerebrospinal fluid of Alzheimer's disease patients.
    Maftei M, Thurm F, Schnack C, Tumani H, Otto M, Elbert T, Kolassa IT, Przybylski M, Manea M, von Arnim CA.
    PLoS One. 2013 Jul 18;8(7):e68996
    Recent studies have suggested a protective role of physiological ß-amyloid autoantibodies (Aß-autoantibodies) in Alzheimer's disease (AD). However, the determination of both free and dissociated Aß-autoantibodies in serum...
    http://www.ncbi.nlm.nih.gov/pubmed/23874844



  • Application of MALDI-TOF-mass spectrometry to proteome analysis using stain-free gel electrophoresis.
    Susnea I, Bernevic B, Wicke M, Ma L, Liu S, Schellander K, Przybylski M.
    Top Curr Chem. 2013;331:37-54. doi: 10.1007/128_2012_321.
    The combination of MALDI-TOF-mass spectrometry with gel electrophoretic separation using protein visualization by staining procedures involving such as Coomassie Brilliant Blue has been established as a widely used approach in proteomics. Although this approach has been shown to present high detection sensitivity, drawbacks and limitations...
    http://www.ncbi.nlm.nih.gov/pubmed/22547356



    • 2012

  • When is Mass Spectrometry Combined with Affinity Approaches Essential? A Case Study of Tyrosine Nitration in Proteins
    Petre B-A, Ulrich M, Stumbaum M, Bernevic B, Moise A, Döring G, Przybylski M
    J. Am. Soc. Mass Spectrom. 2012, 23, 1831-1840
    Tyrosine nitration in proteins occurs under physiologic conditions and is increased at disease conditions associated with oxidative stress, such as inflammation and Alzheimer's disease. Identification and quantification of tyrosine-nitrations are crucial for understanding...
    http://www.ncbi.nlm.nih.gov/pubmed/22907170



  • Antigen-bound and free ß-amyloid autoantibodies in serum of healthy adults
    Maftei M, Thurm F, Leirer VM, von Arnim CAF, Elbert T, Przybylski M, Kolassa I-T, Manea M
    PLoS One. 2012;7(9):e44516
    Physiological ß-amyloid autoantibodies (Aß-autoantibodies) are currently investigated as potential diagnostic and therapeutic tools for Alzheimer's disease (AD). In previous studies, their determination in serum and cerebrospinal fluid (CSF) using indirect ELISA has provided controversial results...
    http://www.ncbi.nlm.nih.gov/pubmed/22973459



  • Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin.
    Jiménez-Castells C, Defaus S, Moise A, Przbylski M, Andreu D and Gutiérrez-Gallego R
    Anal Chem. 2012 Aug 7;84(15):6515-20
    Interest in powerful, nanosized tools to analyze in detail glycan-protein interactions has increased significantly over recent years. Here, we report two complementary approaches to characterize such interactions...

    http://www.ncbi.nlm.nih.gov/pubmed/22770358



  • Interaction structure of the complex between neuroprotective factor humanin and Alzheimer’s ß-amyloid peptide revealed by affinity mass spectrometry and molecular modeling.

    Maftei M, Tian X, Manea M, Exner TE, Schwanzar D, von Arnim CAF and Przybylski M
    J Pept Sci. 2012 Jun;18(6):373-82.
    Humanin (HN) is a linear 24-aa peptide recently detected in human Alzheimer's disease (AD) brain. HN specifically inhibits neuronal cell death in vitro induced by ß-amyloid (Aß) peptides and by amyloid precursor protein and its gene mutations in familial AD, thereby representing a potential therapeutic lead structure...
    http://www.ncbi.nlm.nih.gov/pubmed/22522311



  • Amino acids form prenucleation clusters: ESIMS as a fast detection method in comparison to analytical ultracentrifugation
    Kellermeier M, Rosenberg R, Moise A, Anders U, Przybylski M and Cölfen H
    Faraday Discuss., 2012,159, 23-45
    Electrospray ionisation mass spectrometry (ESI-MS) is a fast method which is able to provide molecular mass information with high precision. In this contribution, we show that prenucleation clusters − species recently found to play a pivotal role in crystallisation processes − are detected...
    http://pubs.rsc.org/en/content/articlelanding/2012/fd/c2fd20060k#!divAbstract



  • Why the structure but not the activity of the immunoproteasome subunit low molecular mass polypeptide 2 rescues antigen presentation
    Basler M, Lauer C, Moebius J, Weber R, Przybylski M, Kisselev AF, Tsu C and Groettrup M
    J Immunol. 2012 Aug 15;189(4):1868-77.
    The proteasome is responsible for the generation of most epitopes presented on MHC class I molecules. Treatment of cells with IFN-γ leads to the replacement of the constitutive catalytic subunits ß1, ß2, and ß5 by the inducible subunits low molecular mass polypeptide...
    http://www.ncbi.nlm.nih.gov/pubmed/22772448



  • Characterization of oligomerization-aggregation products of neurodegenerative target proteins by ion mobility mass spectrometry.
    Vlad C, Iurascu MI, Slamnoiu S, Hengerer B and Przybylski M
    Methods Mol Biol. 2012;896:399-412.
    Protein amyloidogenesis is generally considered to be a major cause of two most severe neurodegenerative disorders, Parkinson's disease (PD) and Alzheimer's disease (AD). Formation and accumulation of fibrillar aggregates and plaques...
    http://www.ncbi.nlm.nih.gov/pubmed/22821540



    • 2011

  • Toward Bioinspired Galectin Mimetics: Identification of Ligand-Contacting Peptides by Proteolytic-Excision Mass Spectrometry.
    Moise A, Andre S, Eggers F, Krzeminski M, Przybylski M and Gabius HJ
    J Am Chem Soc. 2011 Sep 28;133(38):14844-7.
    Clinically relevant bioactivities of human galectins (adhesion/growth−regulatory galactoside-specific lectins) inspired the design of peptides as new tools to elicit favorable effects (e.g., in growth control) or block harmful binding (e.g., in tissue invasion). To obtain the bioinspired lead compounds, we combined a proteolytic fragmentation approach without/with ligand contact (excision) with mass spectrometric identification of affinity−bound protein fragments...
    http://www.ncbi.nlm.nih.gov/pubmed/21861497



  • Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha–synuclein as revealed by ion mobility mass spectrometry.
    Vlad C, Lindner K, Karreman C, Schildknecht S, Leist M, Tomczyk N, Rontree J, Langridge J, Danzer K, Ciossek T, Petre A, Gross ML, Hengerer B and Przybylski M
    Chembiochem. 2011 Dec 16;12(18):2740-4.
    Gas-phase protein separation by ion mobility: With its ability to separate the Parkinson's disease protein α-synuclein and its autoproteolytic products-despite the small concentrations of the latter-ion-mobility MS has enabled the characterization of intermediate fragments...
    http://www.ncbi.nlm.nih.gov/pubmed/22162214



  • Study of metal-containing proteins in the roots of Elsholtzia splendens using LA-ICP-MS and LC- tandem mass spectrometry.
    Wu B, Susnea I, Chen Y, Przybylski M and Becker JS
    Int. J. Mass Spectrom., 2011, 307, 85-91.
    In the present study, the metal-containing proteins in the roots of Cu-tolerant plant Elsholtzia splendens were investigated. The proteins from the plant roots were extracted and separated by two-dimensional gel electrophoresis (2D GE). Laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) was used to screen metal-containing proteins...
    http://www.sciencedirect.com/science/article/pii/S1387380611000388



  • Biomarker candidates of Chlamydophila pneumoniae proteins and protein fragments identified by affinity-proteomics using FTICR-MS and LC-MS/MS.
    Susnea I, Bunk S, Wendel A, Hermann C and Przybylski M
    J Am Soc Mass Spectrom. 2011 Apr;22(4):784-8.
    We report here an affinity-proteomics approach that combines 2D-gel electrophoresis and immunoblotting with high performance mass spectrometry to the identification of both full length protein antigens and antigenic fragments of Chlamydophila pneumoniae (C. pneumoniae). The present affinity-mass spectrometry approach...
    http://www.ncbi.nlm.nih.gov/pubmed/21472615




  • Mass spectrometric protein identification from two-dimensional gel separation with stain-free detection and visualization using native fluorescence.
    Susnea I, Bernevic B, Svobodova E, Simeonova DD, Wicke M, Werner C, Schink B and Przybylski M
    Int. J. Mass Spectrom., 2011, 301, 22–28.
    We describe here an approach for the mass spectrometric identification of proteins in proteome analysis from 1D- and 2D-gel electrophoretic separation, using stain-free detection and visualization...
    http://www.sciencedirect.com/science/article/pii/S1387380610001867



  • Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry. Jung JE, Pierson NA, Marquardt A, Scheffner M, Przybylski M and Clemmer DE
    J Am Soc Mass Spectrom. 2011 Aug;22(8):1463-71.
    Modification of ubiquitin, a key cellular regulatory polypeptide of 76 amino acids, to polyubiquitin conjugates by lysine-specific isopeptide linkage at one of its seven lysine residues has been recognized as a central pathway determining its biochemical properties and cellular functions. Structural details and differences of distinct lysine-isopeptidyl ubiquitin conjugates...
    http://www.ncbi.nlm.nih.gov/pubmed/21953201



  • Identification of the epitope for anti-cystatin C antibody.
    Sladewska A, Szymanska A, Kordalska M, Lewandowska A, Kolodziejczyk AS, Paraschiv G, Przybylski M and Czaplewska P
    J Mol Recognit. 2011 Jul-Aug;24(4):687-99.
    Human cystatin C (hCC), like many other amyloidogenic proteins, has been shown to form dimers by exchange of subdomains of the monomeric protein. Considering the model of hCC fibrillogenesis by propagated domain swapping...
    http://www.ncbi.nlm.nih.gov/pubmed/21584879



  • Epitopemotif of anti-nitrotyrosine antibody specific for tyrosine-nitrated peptides revealed by combination of affinity approaches and mass spectrometry.
    Dragusanu M, Petre BA, Przybylski M
    J Pept Sci. 2011 Mar;17(3):184-91.
    Nitration of tyrosine residues has been shown to be an important oxidative modification in proteins and has been suggested to play a role in several diseases such as atherosclerosis, asthma, lung and neurodegenerative diseases. Detection of nitrated proteins has been mainly...
    http://www.ncbi.nlm.nih.gov/pubmed/21308874



  • Epitope structure of the carbohydrate recognition domain of asialglycoprotein receptor to a monoclonal antibody revealed by high resolution proteolytic excision mass spectrometry. Stefanescu R, Born R, Moise A, Ernst B and Przybylski M
    J Am Soc Mass Spectrom. 2011 Jan;22(1):148-57.
    Recent studies suggest that the H1 subunit of the carbohydrate recognition domain (H1CRD) of the asialoglycoprotein receptor is used as an entry site into hepatocytes by hepatitis A and B viruses and Marburg virus. Thus, molecules binding specifically to the CRD might exert inhibition towards...
    http://www.ncbi.nlm.nih.gov/pubmed/21472553