]> BibSonomy publications for /author/Catapano http://www.bibsonomy.org/burst/author/Catapano BibSonomy BuRST Feed for /author/Catapano 2008-07-27T02:17:30+02:00 Report: Trends in Science Communication Today--Bridging the Gap Between Theory and Practice Report: Trends in Science Communication Today--Bridging the Gap Between Theory and Practice -- CATAPANO 22 (4): 438 -- Science Communicationhttp://www.bibsonomy.org/bibtex/2048c3cce04a981ed4cec1794d5e0d0d9/raffilicious raffilicious 2008-03-13T17:54:19+01:00 communication_today lv_wisskomm practice science_communication symposium
Report: Trends in Science Communication Today--Bridging the Gap Between Theory and Practice
PAOLA CATAPANO Science Communication 22 438-441 (2001)
to communication_today lv_wisskomm practice science_communication symposium by raffilicious on 2008-03-13 17:54:19 ]]> Science Communication4438-441{Report: Trends in Science Communication Today--Bridging the Gap Between Theory and Practice}222001communication_today lv_wisskomm practice science_communication symposium 2008-03-13 17:54:19.0PCST 2001 was the sixth in the series of the Public Communication of Science and Technology network meetings. Held early in February 2001 in Geneva, Switzerland, the conference attracted 250 delegates from thirty-one countries to discuss theoretical and practical issues in science communication. Following is a report on the conference by the conference chair. Epitope mapping analysis of apolipoprotein B-100 using a surface plasmon resonance-based biosensor. http://www.bibsonomy.org/bibtex/264fee8a74054cacb021a4106ed8baf1f/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping spr
Epitope mapping analysis of apolipoprotein B-100 using a surface plasmon resonance-based biosensor.
L. Laricchia Robbio and P. Uboldi and S. Marcovina and R. P. Revoltella and A. L. Catapano Biosens Bioelectron 16 963--969 (2001)
to apob epitope mapping spr by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Mutagenesis and Differentiation, CNR, Area della Ricerca San Cataldo, 56100 Via Moruzzi, Ghezzano-Pisa, Italy. lel@imd.pi.cnr.itBiosens BioelectronDecember9-12963--969Epitope mapping analysis of apolipoprotein B-100 using a surface plasmon resonance-based biosensor.162001apob epitope mapping spr 2006-07-07 01:10:50.0Using a surface plasmon resonance (SPR)-based biosensor (BIA-technology), we have studied the interaction of ten different murine monoclonal antibodies (mAbs, all IgG(1)), raised against the main protein constituent of human low density lipoprotein (LDL), i.e. the apolipoprotein B-100 (apoB-100). These mAbs identify distinct domains on apoB-100, relevant to LDL-receptor interaction: epitopes in the amino-terminal region (mAbs L7, L9, L10 and L11: aa 1-1297) and in the middle region (mAb 6B: aa 1480-1693; mAbs 2A, 3B: aa 2152-2377; mAbs 9A, L2 and L4: aa 2657-3248) of native apoB-100. A multisite binding analysis was performed to further characterize the epitopes recognized by all these mAbs. A rabbit anti-mouse IgG(1)-Fc antibody (RAM.Fc) was first coupled to the gold surface in order to capture one anti-human apoB-100 mAb. ApoB-100 protein was subsequently injected and allowed to react with this immobilized, oriented antibody. Multisite binding assays were then performed, by sequentially flowing other mAbs, in different orders, over the sensing surface. The capacity of each mAb to interact with the entrapped apoB-100 in a multimolecular complex was monitored in real time by SPR. The results achieved were comparable to those obtained by western immunoblotting using the same reagents. However, SPR ensures a more detailed epitope identification, demonstrating that BIA-technology can be successfully used for mapping distinct epitopes on apoB-100 protein in solution dispensing with labels and secondary tracers; moreover, compared with conventional immunoassays, it is significantly time saving (CNR-P.F. MADESS 2). Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction. http://www.bibsonomy.org/bibtex/28470a55ffd3031830371a1e0072d15bf/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping
Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.
S. Fantappiè and A. Corsini and A. Sidoli and P. Uboldi and A. Granata and T. Zanelli and P. Rossi and S. Marcovina and R. Fumagalli and A. L. Catapano Journal of Lipid Research 33 1111--1121 (1992)
to apob epitope mapping by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Pharmacological Sciences, University of Milano, Italy.Journal of Lipid ResearchAugust81111--1121Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.331992apob epitope mapping 2006-07-07 01:10:50.0We have characterized the epitopes for ten murine monoclonal antibodies (Mabs) to human low density lipoprotein (LDL) and studied their ability to interfere with the LDL-receptor interaction. The epitopes for the antibodies were defined by using the following approaches: 1) interaction with apoB-48; 2) interaction with apoB-100 thrombolytic fragments; and 3) interaction with beta-galactosidase-apoB fusion proteins spanning different areas of the apoB-100 sequence. The results obtained are consistent with the following map of epitopes: Mab 6E, amino acids (aa) 1-1297, Mabs 5A and 6B, aa 1480-1693, Mabs 2A, 7A, 3B, and 4B, aa 2152-2377, Mabs 8A and 9A, aa 2657-3248 and 3H, aa 4082-4306. Four Mabs (2A, 5A, 7A, and 9A) whose epitopes are located in three different areas of apoB, dramatically reduced (up to 95%) the LDL-receptor interaction on cultured human fibroblasts; Fab fragments were as effective as the whole antibodies. Mab 3H, on the other hand, increased LDL binding up to threefold. These findings are consistent with the hypothesis that several areas of apoB-100 are involved independently or in concert in modulating the apoprotein B conformation required for interaction with the LDL receptor. Immunoreactivity of apo B towards monoclonal antibodies that inhibit the LDL-receptor interaction: effects of LDL oxidation. http://www.bibsonomy.org/bibtex/2acca9a5e11f5de28586667a664f1e859/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping
Immunoreactivity of apo B towards monoclonal antibodies that inhibit the LDL-receptor interaction: effects of LDL oxidation.
S. Negri and P. Roma and R. Fogliatto and P. Uboldi and S. Marcovina and A. L. Catapano Atherosclerosis 101 37--41 (1993)
to apob epitope mapping by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Pharmacological Sciences, University of Milano, Italy.AtherosclerosisJune137--41Immunoreactivity of apo B towards monoclonal antibodies that inhibit the LDL-receptor interaction: effects of LDL oxidation.1011993apob epitope mapping 2006-07-07 01:10:50.0We studied the immunochemical stability of the epitopes for six monoclonal antibodies to human apolipoprotein B-100 upon Cu(2+)-mediated (20 microM) oxidation of LDL. The antibodies used in this study, some of which are known to interfere with the interaction of LDL with their cellular receptors, recognize epitopes in the amino terminal region (Mb 19), in the middle part (6B, 2A, 7A, and 9A) and near aa 3500 (Mb 47) of native apo B. All antibodies except one (7A) recognized native and oxidized LDL (OxLDL) equally well; the immunoreactivity of the epitope for Ab 7A was markedly reduced upon LDL oxidation. Since antibodies 2A, 7A, 9A, and Mb 47 inhibit the LDL-receptor interaction and OxLDL poorly interact in vitro with the LDL receptor we conclude that: (1) various epitopes for monoclonal antibodies against native apo B are spared upon LDL oxidation; and (2) the epitopes for antibodies 2A, 9A, and Mb 47 do not define a unique domain of apo B directly involved in the binding of LDL to their receptor. Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction. http://www.bibsonomy.org/bibtex/28a5794e6f329c353fcea2f5897cbd46b/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping
Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.
A. Corsini and S. Fantappiè and S. Marcovina and A. Granata and R. Fumagalli and A. L. Catapano Biochem Biophys Res Commun 162 908--915 (1989)
to apob epitope mapping by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Pharmacological Sciences, University of Milan, Italy.Biochem Biophys Res CommunAugust3908--915Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.1621989apob epitope mapping 2006-07-07 01:10:50.0In a panel of 10 monoclonal antibodies raised against human LDL we detected three antibodies (named 5A, 6B, and 6E) which recognize both apolipoprotein B-100 and B-48. Antibody 5A inhibited, in a dose dependent manner, the interaction of 125I-LDL with their receptor on human skin fibroblasts. Using thrombolytic fragments, the epitope of antibody 5A was mapped to the carboxy terminal region of apo B-48. MAB 5A was equipotent with MAB Mb 47, an inhibitory antibody whose epitope lies near a putative receptor binding domain of apo B in thrombolytic fragment T2. These findings suggest that areas other than the carboxy terminal portion of apo B-100 may participate in the LDL-receptor interaction, either directly or by determining the exposition of high affinity sites of apo B-100.