MISEVIC GRADIMIR

Prof. MISEVIC GRADIMIR

CEO Gimmune GmbH, Switzerland
+2

Research Focus & Metrics

Academic Career Length

38Years (1989-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
24 February 1995 in Science
Verified
Journal Article
Closed access
PDF file
UDUlrich Dammer
Ulrich Dammer
OPOctavian Popescu
Octavian Popescu
PWPeter Wagner
Peter Wagner
DADario Anselmetti
Dario Anselmetti
HGHans-Joachim Güntherodt
Hans-Joachim Güntherodt
MISEVIC GRADIMIRMISEVIC GRADIMIR
MISEVIC GRADIMIR
Measurement of binding forces intrinsic to adhesion molecules is necessary to assess their contribution to the maintenance of the anatomical integrity of multicellular organisms. Atomic force microscopy was used to measure the binding strength between cell adhesion proteoglycans from a marine sponge. Under physiological conditions, the adhesive force between two cell adhesion molecules was found to be up to 400 piconewtons. Thus a single pair of molecules could hold the weight of 1600 cells. High intermolecular binding forces are likely to form the basis for the integrity of the multicellular sponge organism.

1 March 1995 in Journal of Biological Chemistry
Verified
Journal Article
Open access
DSDorothe Spillmann
Dorothe Spillmann
JTJane E. Thomas-Oates
Jane E. Thomas-Oates
JKJ. Albert van Kuik
J. Albert van Kuik
JVJohannes F.G. Vliegenthart
Johannes F.G. Vliegenthart
MISEVIC GRADIMIRMISEVIC GRADIMIR
MISEVIC GRADIMIR
Jukka FinneJukka Finne
Jukka Finne
Species-specific cell reaggregation in the marine sponge Microciona prolifera is mediated by an adhesion proteoglycan. Two interactions are involved in the process: a Ca(2+)-dependent homophilic binding between proteoglycan molecules and a Ca(2+)-independent binding between the molecule and cells. Both interactions are mediated by the glycan moieties of the proteoglycan. The interaction of the proteoglycan with itself has been characterized as a carbohydrate-carbohydrate interaction of multiple low affinity sites. The monoclonal antibodies Block 1 and Block 2 raised against the purified aggregation proteoglycan and selected for inhibition of aggregation bind to these glycans. In a previous report the structure, [formula: see text] was assigned to the oligosaccharide reacting with Block 1 antibody (Spillmann, D., Hård, K., Thomas-Oates, J., Vliegenthart, J. F. G., Misevic, G., Burger, M. M., and Finne, J. (1993) J. Biol. Chem. 268, 13378-13387). By the technique of attaching the water-soluble acid-degraded fragments to a lipid carrier for immunochemical detection and by chemical, enzymatic and spectroscopic methods the structure, [formula: see text] was assigned to the oligosaccharide reacting with the aggregation-blocking monoclonal antibody Block 2. The structure, [formula: see text] was assigned to a major nonreactive oligosaccharide, which outlined the molecular requirements of antibody binding of the two aggregation-associated epitopes. These data demonstrate that two different functional sites with distinct structural characteristics and antibody reactivities are involved in the reaggregation of sponge cells, a model of carbohydrate-carbohydrate-mediated cell interactions.

1 March 1997 in Nature
Verified
Journal Article
Closed access
OPOctavian Popescu
Octavian Popescu
MISEVIC GRADIMIRMISEVIC GRADIMIR
MISEVIC GRADIMIR

1 October 2007 in Annual Review of Microbiology
Verified
Journal Article
Closed access
Vic NorrisVic Norris
Vic Norris
Tanneke Den BlaauwenTanneke Den Blaauwen
Tanneke Den Blaauwen
RDRoy H Doi
Roy H Doi
RHRasika M Harshey
Rasika M Harshey
LJLaurent Janniere
Laurent Janniere
MTMichel Thellier
Michel Thellier
Bacterial cells contain many large, spatially extended assemblies of ions, molecules, and macromolecules, called hyperstructures, that are implicated in functions that range from DNA replication and cell division to chemotaxis and secretion. Interactions between these hyperstructures would create a level of organization intermediate between macromolecules and the cell itself. To explore this level, a taxonomy is needed. Here, we describe classification criteria based on the form of the hyperstructure and on the processes responsible for this form. These processes include those dependent on coupled transcription-translation, protein-protein affinities, chromosome site-binding by protein, and membrane structures. Various combinations of processes determine the formation, maturation, and demise of many hyperstructures that therefore follow a trajectory within the space of classification by form/process. Hence a taxonomy by trajectory may be desirable. Finally, we suggest that working toward a taxonomy based on speculative interactions between hyperstructures promises most insight into life at this level.

5 April 2013 in PLOS ONE
Verified
Journal Article
Open access
PDF file
ZVZoran B. Vosika
Zoran B. Vosika
GLGoran Lazovic
Goran Lazovic
MISEVIC GRADIMIRMISEVIC GRADIMIR
MISEVIC GRADIMIR
JSJovana B. Simic-Krstic
Jovana B. Simic-Krstic
Fractional calculus is a mathematical approach dealing with derivatives and integrals of arbitrary and complex orders. Therefore, it adds a new dimension to understand and describe basic nature and behavior of complex systems in an improved way. Here we use the fractional calculus for modeling electrical properties of biological systems. We derived a new class of generalized models for electrical impedance and applied them to human skin by experimental data fitting. The primary model introduces new generalizations of: 1) Weyl fractional derivative operator, 2) Cole equation, and 3) Constant Phase Element ( CPE ). These generalizations were described by the novel equation which presented parameter related to remnant memory and corrected four essential parameters We further generalized single generalized element by introducing specific partial sum of Maclaurin series determined by parameters We defined individual primary model elements and their serial combination models by the appropriate equations and electrical schemes. Cole equation is a special case of our generalized class of models for Previous bioimpedance data analyses of living systems using basic Cole and serial Cole models show significant imprecisions. Our new class of models considerably improves the quality of fitting, evaluated by mean square errors, for bioimpedance data obtained from human skin. Our models with new parameters presented in specific partial sum of Maclaurin series also extend representation, understanding and description of complex systems electrical properties in terms of remnant memory effects.

1 April 2004 in Journal of Biological Chemistry
Verified
Journal Article
Open access
PDF file
YGYann Guerardel
Yann Guerardel
XCXavier Czeszak
Xavier Czeszak
LSLazar T. Sumanovski
Lazar T. Sumanovski
Yannis KaramanosYannis Karamanos
Yannis Karamanos
OPOctavian Popescu
Octavian Popescu
MISEVIC GRADIMIRMISEVIC GRADIMIR
MISEVIC GRADIMIR
Glyconectins (GNs) represent a new class of proteoglycan-like cell adhesion and recognition molecules found in several Porifera species. Physico-chemical properties of GN carbohydrate moieties, such as size, composition, and resistance to most glycosaminoglycan-degrading enzymes, distinguish them from any other type of known glycoproteins. The molecular mechanism of GN-mediated self/non-self discrimination function is based on highly species-specific and Ca2+-dependent GN to GN associations that approach the selectivity of the evolutionarily advanced immunoglobulin superfamily. Carbohydrates of glyconectins 1, 2, and 3 are essential for species-specific auto-aggregation properties in three respective Porifera species. To obtain a structural insight into the molecular mechanisms, we performed carbohydrate structural analyses of glyconectins isolated from the three sponge model systems, Microciona prolifera (GN1), Halichondria panicea (GN2), and Cliona celata (GN3). The glycan content of all three GNs ranged between 40 and 60% of their total mass. Our approach using sequential and selective chemical degradation of GN glycans and subsequent mass spectrometric and NMR analyses revealed that each glyconectin presents novel and highly species-specific carbohydrate sequences. All three GNs include distinct acid-resistant and acid-labile carbohydrate domains, the latter composed of novel repetitive units. We have sequenced four short sulfated and one pyruvilated unit in GN1, eight larger and branched pyruvilated oligosaccharides in GN2, which represent a heterogeneous but related family of structures, and four sulfated units in GN3.