Oppermann, Martin

[["dc.bibliographiccitation.firstpage","405"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EXPERIMENTAL NEPHROLOGY"],["dc.bibliographiccitation.lastpage","411"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Grunewald, Rolf W."],["dc.contributor.author","Ehrhard, M."],["dc.contributor.author","Fiedler, Gabriele"],["dc.contributor.author","Schuttert, J. B."],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T09:32:11Z"],["dc.date.available","2018-11-07T09:32:11Z"],["dc.date.issued","2001"],["dc.description.abstract","Sorbitol plays a major role in the maintenance of cell volume and functional integrity of several renal cells. Sorbitol synthesis takes place in inner collecting duct cells, whereas sorbitol dehydrogenase activity, which catalyzes the degradation of sorbiotol to fructose, could mainly be detected in renal inner medullary interstitial cells. Therefore, we supposed that interstitial cells would require a sorbitol transport into the cells. However, such a transport system has not yet been described. Therefore, we have characterized the uptake of sorbitol in immortalized interstitial TK-173 cells, which were derived from human renal fibroblasts. Comparable to fresh isolated renal fibroblasts of the rat, immortalized TK-173 cells have a high sorbitol dehydrogenase activity. In this report, a temperature-dependent sorbitol uptake with saturation kinetics could be detected in immortalized TK-173 cells. The transport is characterized by a high velocity (V-max 84 mmol/l x h) and an apparent K-m of 10 mmol/l. The sorbitol uptake is independent of membrane potential, sodium, and chloride. Altogether, the physiological characteristics of this sorbitol transport are different from those of the osmotically regulated sorbitol efflux from epithelial cells. These results provide evidence that TK-173 cells derived from renal fibroblasts have a specific sorbitol transport. Furthermore, these data suggest a cooperation between epithelial and interstitial cells concerning osmoregulation. Copyright (C) 2001 S. Karger AG, Basel."],["dc.identifier.isi","000172203500008"],["dc.identifier.pmid","11702000"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31695"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1018-7782"],["dc.title","Evidence for a sorbitol transport system in immortalized human renal interstitial cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1201"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cellular Signalling"],["dc.bibliographiccitation.lastpage","1210"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:44:06Z"],["dc.date.available","2018-11-07T10:44:06Z"],["dc.date.issued","2004"],["dc.description.abstract","CC chemokine receptor 5 (CCR5) is a seven-transmembrane, G protein-coupled receptor (GPCR) which regulates trafficking and effector functions of memory/effector T-lymphocytes, macrophages, and immature dendritic cells. It also serves as the main coreceptor for the entry of R5 strains of human immunodeficiency virus (HIV-1, HIV-2). Chemokine binding to CCR5 leads to cellular activation through pertussis toxin-sensitive heterotrimeric G proteins as well as G protein-independent signalling pathways, Like many other GPCR, CCR5 is regulated by agonist-dependent processes which involve G protein coupled receptor kinase (GRK)-dependent phosphorylation, P-arrestin-mediated desensitization and internalization. This review discusses recent advances in the elucidation of the structure and function of CCR5, as well as the complex mechanisms that regulate CCR5 signalling and cell surface expression. (C) 2004 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.cellsig.2004.04.007"],["dc.identifier.isi","000223955300001"],["dc.identifier.pmid","15337520"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47199"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0898-6568"],["dc.title","Chemokine receptor CCR5: insights into structure, function, and regulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.volume","365"],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Kraft, K."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:31:35Z"],["dc.date.available","2018-11-07T10:31:35Z"],["dc.date.issued","2002"],["dc.format.extent","R18"],["dc.identifier.isi","000175030900068"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44148"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.issn","0028-1298"],["dc.title","Kinetic analysis of PKC- and GRK-mediated phosphorylation of chemokine receptor CCR5 by phosphosite-specific antibodies"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0157502"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Liebick, Marcel"],["dc.contributor.author","Schlaeger, Christian"],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:12:44Z"],["dc.date.available","2018-11-07T10:12:44Z"],["dc.date.issued","2016"],["dc.description.abstract","Chemokine receptors undergo internalization and desensitization in response to ligand activation. Internalized receptors are either preferentially directed towards recycling pathways (e.g. CCR5) or sorted for proteasomal degradation (e.g. CXCR4). Here we describe a method for the analysis of receptor internalization and recycling based on specific Bir A-mediated biotinylation of an acceptor peptide coupled to the receptor, which allows a more detailed analysis of receptor trafficking compared to classical antibody-based detection methods. Studies on constitutive internalization of the chemokine receptors CXCR4 (12.1% +/- 0.99% receptor internalization/h) and CCR5 (13.7% +/- 0.68%/h) reveals modulation of these processes by inverse (TAK779; 10.9% +/- 0.95%/h) or partial agonists (Met-CCL5; 15.6% +/- 0.5%/h). These results suggest an actively driven internalization process. We also demonstrate the advantages of specific biotinylation compared to classical antibody detection during agonist-induced receptor internalization, which may be used for immunofluorescence analysis as well. Site-specific biotinylation may be applicable to studies on trafficking of transmembrane proteins, in general."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [DFG Op42-10]"],["dc.identifier.doi","10.1371/journal.pone.0157502"],["dc.identifier.isi","000378029800087"],["dc.identifier.pmid","27310579"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13389"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40296"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Analysis of Chemokine Receptor Trafficking by Site-Specific Biotinylation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Molecular Immunology"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Pollok-Kopp, B."],["dc.contributor.author","Rethorn, S."],["dc.contributor.author","Schwarze, Katrin"],["dc.contributor.author","Huttenrauch, F."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T10:38:44Z"],["dc.date.available","2018-11-07T10:38:44Z"],["dc.date.issued","2006"],["dc.format.extent","149"],["dc.identifier.isi","000232021600087"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45879"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.conference","10th Meeting on Complement in Human Disease"],["dc.relation.eventlocation","Heidelberg, GERMANY"],["dc.relation.issn","0161-5890"],["dc.title","Protein kinase C beta-mediated phosphorylation of Serine-334 of the human C5a anaphylatoxin receptor (C5aR): Modulation by the adapter protein beta-arrestin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","277"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Ultrasound in Obstetrics and Gynecology"],["dc.bibliographiccitation.lastpage","283"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Viereck, Volker"],["dc.contributor.author","Pauer, H. U."],["dc.contributor.author","Bader, Werner"],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Hilgers, Ralf-Dieter"],["dc.contributor.author","Gauruder-Burmester, A."],["dc.contributor.author","Lange, Rainer"],["dc.contributor.author","Emons, G."],["dc.contributor.author","Hackenberg, R."],["dc.contributor.author","Krauss, T."],["dc.date.accessioned","2018-11-07T10:51:05Z"],["dc.date.available","2018-11-07T10:51:05Z"],["dc.date.issued","2004"],["dc.description.abstract","Objective To assess the topography of the bladder neck by introital ultrasound before and after open colposuspension. Methods Three hundred and ten women with urodynamically proven stress urinary incontinence were included in this long-term study to investigate the position and function of the bladder neck at rest and during straining. Height (H), distance (D), and urethrovesical angle of the bladder neck (beta) were measured by means of preoperative and postoperative introital ultrasound. Women were followed up; 152 of them (49%) completed 48 months of follow-up. Results At the 6-month follow-up examination, 90.0% of the women were continent (279/310), 3.5% (11/310) showed voiding difficulties, 3.5% (11/310) had urgency, and 1.6% (5/310) bad developed de novo urge incontinence. At the 48-month follow-up, 76.8% of the patients were still continent. All postoperative measurements yielded significantly lower values for angle beta at rest and during straining compared with the preoperative results (P < 0.0001). The median linear movement of the bladder neck during straining decreased from 18.0 mm before surgery to 6.4 mm at the 48-month follow-up (P < 0.0001). The median level of ventrocranial elevation of the vesicourethral junction was 14.3 mm immediately after surgery, 9.9 mm after 6 months and 6.6 mm after 48 months. The degree of surgical bladder-neck elevation was associated with postoperative urgency/de novo urge incontinence (P < 0.0001) and voiding difficulty (P < 0.0001). Conclusions The colposuspension procedure reduces angle at rest and during straining, restricts linear movement with straining, and elevates the bladder neck. Perioperative introital ultrasound improves understanding of this surgical procedure and might help to prevent postoperative complications. Copyright (C) 2004 ISUOG. Published by John Wiley Sons, Ltd."],["dc.identifier.doi","10.1002/uog.982"],["dc.identifier.isi","000220287300014"],["dc.identifier.pmid","15027018"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48802"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","John Wiley & Sons Ltd"],["dc.relation.issn","0960-7692"],["dc.title","Introital ultrasound of the lower genital tract before and after colposuspension: a 4-year objective follow-up"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","251"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","258"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Jozsi, M."],["dc.contributor.author","Manuelian, T."],["dc.contributor.author","Heinen, S."],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Zipfel, Peter F."],["dc.date.accessioned","2018-11-07T10:52:37Z"],["dc.date.available","2018-11-07T10:52:37Z"],["dc.date.issued","2004"],["dc.description.abstract","Complement is a central element of innate immunity and this vital defense system initiates and coordinates immediate immune reactions which attack and eliminate microbes, foreign particles and altered self cells. Newly generated activation products are extremely toxic and consequently, activation is highly restricted in terms of time and space. The initial activation of the alternative complement pathway occurs continuously and the early phase acts indiscriminatoryl and forms on any surface. However, the system discriminates between self and foreign, and therefore allows activation on foreign surfaces e.g. Microbes, and restricts activation on host cells. Consequently, self cells and tissues are protected from the harmful activation products. This protection is mediated by specific regulators or inhibitors, which exist in the fluid phase and/or in membrane-bound forms. Here we review a novel mechanism, i.e. the attachment of the soluble complement regulator factor H to the surface of self cells. This attachment, which is demonstrated experimentally by means of immunofluorescense microscopy and by flow cytometry, increases the inhibitory potential at the cell surface and mediates protection by reducing the local formation of toxic inflammatory products. This attachment is highly relevant and has pathophysiological consequences in several human diseases, including Factor H-associated hemolytic uremic syndrome (FH-HUS), membrano-proliferative glomerulonephritis type II, recurrent microbial infections and chronic inflammation, e.g. rheumatoid arthritis and immune evasion of tumor cells. Defects of this safeguard activity have been recently understood in patients with FH-HUS. Point mutations in the Factor H gene occurring in the C-terminus of the protein result in impaired cell binding capacity of Factor H and, consequently, during an inflammatory insult endothelial cells are not properly protected and are damaged."],["dc.identifier.isi","000188355400030"],["dc.identifier.pmid","14702193"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49151"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Attachment of the soluble complement regulator factor H to cell and tissue surfaces: relevance for pathology"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1966"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Pharmacology"],["dc.bibliographiccitation.lastpage","1976"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Lagane, B."],["dc.contributor.author","Ballet, S."],["dc.contributor.author","Planchenault, T."],["dc.contributor.author","Balabanian, K."],["dc.contributor.author","Le Poul, E."],["dc.contributor.author","Blanpain, C."],["dc.contributor.author","Percherancier, Y."],["dc.contributor.author","Staropoli, I."],["dc.contributor.author","Vassart, G."],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Parmentier, M."],["dc.contributor.author","Bachelerie, F."],["dc.date.accessioned","2018-11-07T10:57:24Z"],["dc.date.available","2018-11-07T10:57:24Z"],["dc.date.issued","2005"],["dc.description.abstract","CC chemokine receptor 5 (CCR5) is a G protein-coupled receptor that governs migration of leukocytes and serves as a coreceptor for the R5 tropic strains of human immunodeficiency virus (HIV). CCR5-mediated signaling in response to CC chemokines relies on G protein activation. Desensitization, which rapidly turns off G protein-dependent signaling, involves phosphorylation of CCR5 that promotes interaction of the receptor with beta-arrestins for endocytosis. Whether coupling to G proteins, desensitization, and endocytosis of CCR5 require the same structural determinants remains a matter of investigation. Here, we show that CCR5 displayed agonist-independent coupling to G proteins. This constitutive activity of the receptor was abrogated by TAK779 (N,N-dimethyl-N-[4-[[[2-(4-methylphenyl)-6,7-dihydro-5H-benzo-cyclohepten-8-yl]carbonyl]amino]benzyl]tetrahydro-2H-pyran-4-aminium chloride), a nonpeptidic CCR5 ligand that inhibits HIV infection and was found to depend on the integrity of the Asp-Arg-Tyr (DRY) motif. Changing Arg-126 by the neutral residue Asn (R126N-CCR5 mutant) abolished CCR5-mediated activation of G proteins, either constitutively or in response to agonists. In contrast, R126N-CCR5 not only retained agonist-promoted phosphorylation and beta-arrestin-dependent endocytosis but also displayed a higher basal phosphorylation than wild-type CCR5. Expression of beta-arrestin in R126N-CCR5-expressing cells resulted in receptor down-regulation, thereby suggesting that R126N-CCR5 spontaneously interacts with beta-arrestins. However, although expression of beta-arrestin favored wild-type CCR5-mediated chemotaxis, it failed to promote migration of cells expressing R126N-CCR5. Overall, these data indicate that structural requirements for CCR5-mediated activation of G proteins, albeit not involved in receptor desensitization and internalization, are needed for beta-arrestin-mediated chemotaxis. These results have implications for how distinct biological responses of CCR5 might rely on a different set of receptor conformations."],["dc.identifier.doi","10.1124/mol.104.009779"],["dc.identifier.isi","000229141200017"],["dc.identifier.pmid","15761117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50238"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Pharmacology Experimental Therapeutics"],["dc.relation.issn","0026-895X"],["dc.title","Mutation of the DRY motif reveals different structural requirements for the CC chemokine receptor 5-mediated signaling and receptor endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e2593"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Scholl, Hendrik P. N."],["dc.contributor.author","Issa, Peter Charbel"],["dc.contributor.author","Walier, Maja"],["dc.contributor.author","Janzer, Stefanie"],["dc.contributor.author","Pollok-Kopp, Beatrix"],["dc.contributor.author","Boerncke, Florian"],["dc.contributor.author","Fritsche, Lars G."],["dc.contributor.author","Chong, Ngaihang V."],["dc.contributor.author","Fimmers, Rolf"],["dc.contributor.author","Wienker, Thomas F."],["dc.contributor.author","Holz, Frank G."],["dc.contributor.author","Weber, Bernhard H. F."],["dc.contributor.author","Oppermann, Martin"],["dc.date.accessioned","2018-11-07T11:13:05Z"],["dc.date.available","2018-11-07T11:13:05Z"],["dc.date.issued","2008"],["dc.description.abstract","Dysregulation of the alternative pathway (AP) of complement cascade has been implicated in the pathogenesis of age-related macular degeneration (AMD), the leading cause of blindness in the elderly. To further test the hypothesis that defective control of complement activation underlies AMD, parameters of complement activation in blood plasma were determined together with disease-associated genetic markers in AMD patients. Plasma concentrations of activation products C3d, Ba, C3a, C5a, SC5b-9, substrate proteins C3, C4, factor B and regulators factor H and factor D were quantified in patients (n = 112) and controls (n = 67). Subjects were analyzed for single nucleotide polymorphisms in factor H (CFH), factor B-C2 (BF-C2) and complement C3 (C3) genes which were previously found to be associated with AMD. All activation products, especially markers of chronic complement activation Ba and C3d (p<0.001), were significantly elevated in AMD patients compared to controls. Similar alterations were observed in factor D, but not in C3, C4 or factor H. Logistic regression analysis revealed better discriminative accuracy of a model that is based only on complement activation markers Ba, C3d and factor D compared to a model based on genetic markers of the complement system within our study population. In both the controls' and AMD patients' group, the protein markers of complement activation were correlated with CFH haplotypes. This study is the first to show systemic complement activation in AMD patients. This suggests that AMD is a systemic disease with local disease manifestation at the ageing macula. Furthermore, the data provide evidence for an association of systemic activation of the alternative complement pathway with genetic variants of CFH that were previously linked to AMD susceptibility."],["dc.identifier.doi","10.1371/journal.pone.0002593"],["dc.identifier.isi","000263288200052"],["dc.identifier.pmid","18596911"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8260"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53812"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Systemic Complement Activation in Age-Related Macular Degeneration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","342"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Clinical & Experimental Immunology"],["dc.bibliographiccitation.lastpage","352"],["dc.bibliographiccitation.volume","144"],["dc.contributor.author","Oppermann, Martin"],["dc.contributor.author","Manuelian, T."],["dc.contributor.author","Jozsi, M."],["dc.contributor.author","Brandt, E."],["dc.contributor.author","Jokiranta, T. S."],["dc.contributor.author","Heinen, S."],["dc.contributor.author","Meri, S."],["dc.contributor.author","Skerka, C."],["dc.contributor.author","Gotze, O."],["dc.contributor.author","Zipfel, Peter F."],["dc.date.accessioned","2018-11-07T09:51:20Z"],["dc.date.available","2018-11-07T09:51:20Z"],["dc.date.issued","2006"],["dc.description.abstract","The complement inhibitor Factor H has three distinct binding sites for C3b and for heparin, but in solution uses specifically the most C-terminal domain, i.e. short consensus repeats (SCR) 20 for ligand interaction. Two novel monoclonal antibodies (mABs C14 and C18) that bind to the most C-terminal domain SCR 20 completely blocked interaction of Factor H with the ligands C3b, C3d, heparin and binding to endothelial cells. In contrast, several mAbs that bind to the N-terminus and to the middle regions of the molecule showed no or minor inhibitory effects when assayed by enzyme-linked immunosorbent assay (ELISA) and ligand interaction assays. This paradox between a single functional binding site identified for native Factor H versus multiple interaction sites reported for deletion constructs is explained by a compact conformation of the fluid phase protein with one accessible binding site. On zymosan particles mAbs C14 and C18 blocked alternative pathway activation completely. Thus demonstrating that native Factor H makes the first and initial contact with the C terminus, which is followed by N terminally mediated complement regulation. These results are explained by a conformational hypothetical model: the native Factor H protein has a compact structure and only one binding site accessible. Upon the first contact the protein unfolds and exposes the additional binding sites. This model does explain how Factor H mediates recognition functions during complement control and the clustering of disease associated mutations in patients with haemolytic uraemic syndrome that have been reported in the C-terminal recognition domain of Factor H."],["dc.identifier.doi","10.1111/j.1365-2249.2006.03071.x"],["dc.identifier.isi","000236766600021"],["dc.identifier.pmid","16634809"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35890"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0009-9104"],["dc.title","The C-terminus of complement regulator Factor H mediates target recognition: evidence for a compact conformation of the native protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]