Relevant bibliographies by topics / L1-CAM

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'L1-CAM'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "L1-CAM"

1

Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. "The neural cell adhesion molecule N-CAM enhances L1-dependent cell-cell interactions." Journal of Cell Biology 110, no. 1 (January 1, 1990): 193–208. http://dx.doi.org/10.1083/jcb.110.1.193.

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On neural cells, the cell adhesion molecule L1 is generally found coexpressed with N-CAM. The two molecules have been suggested, but not directly shown, to affect each other's function. To investigate the possible functional relationship between the two molecules, we have characterized the adhesive interactions between the purified molecules and between cultured cells expressing them. Latex beads were coated with purified L1 and found to aggregate slowly. N-CAM-coated beads did not aggregate, but did so after addition of heparin. Beads coated with both L1 and N-CAM aggregated better than L1-coated beads. Strongest aggregation was achieved when L1-coated beads were incubated together with beads carrying both L1 and N-CAM. In a binding assay, the complex of L1 and N-CAM bound strongly to immobilized L1, but not to the cell adhesion molecules J1 or myelin-associated glycoprotein. N-CAM alone did not bind to these glycoproteins. Cerebellar neurones adhered to and sent out processes on L1 immobilized on nitrocellulose. N-CAM was less effective as substrate. Neurones interacted most efficiently with the immobilized complex of L1 and N-CAM. They adhered to this complex even when its concentration was at least 10 times lower than the lowest concentration of L1 found to promote adhesion. The complex became adhesive for cells only when the two glycoproteins were preincubated together for approximately 30 min before their immobilization on nitrocellulose. The adhesive properties between cells that express L1 only or both L1 and N-CAM were also studied. ESb-MP cells, which are L1-positive, but N-CAM negative, aggregated slowly under low Ca2+. Their aggregation could be completely inhibited by antibodies to L1 and enhanced by addition of soluble N-CAM to the cells before aggregation. N2A cells, which are L1 and N-CAM positive aggregated well under low Ca2+. Their aggregation was partially inhibited by either L1 or N-CAM antibodies and almost completely by the combination of both antibodies. N2A and ESb-MP cells coaggregated rapidly and their interaction was similarly inhibited by L1 and N-CAM antibodies. These results indicate that L1 is involved in two types of binding mechanisms. In one type, L1 serves as its own receptor with slow binding kinetics. In the other, L1 is modulated in the presence of N-CAM on one cell (cis-binding) to form a more potent receptor complex for L1 on another cell (trans-binding).
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Gavert, Nancy, Amir Ben-Shmuel, Shani Raveh, and Avri Ben-Ze'ev. "L1-CAM in cancerous tissues." Expert Opinion on Biological Therapy 8, no. 11 (October 10, 2008): 1749–57. http://dx.doi.org/10.1517/14712598.8.11.1749.

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Nishimura, Kazunari, Fumie Yoshihara, Takuro Tojima, Noriko Ooashi, Woohyun Yoon, Katsuhiko Mikoshiba, Vann Bennett, and Hiroyuki Kamiguchi. "L1-dependent neuritogenesis involves ankyrinB that mediates L1-CAM coupling with retrograde actin flow." Journal of Cell Biology 163, no. 5 (December 1, 2003): 1077–88. http://dx.doi.org/10.1083/jcb.200303060.

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The cell adhesion molecule L1 (L1-CAM) plays critical roles in neurite growth. Its cytoplasmic domain (L1CD) binds to ankyrins that associate with the spectrin–actin network. This paper demonstrates that L1-CAM interactions with ankyrinB (but not with ankyrinG) are involved in the initial formation of neurites. In the membranous protrusions surrounding the soma before neuritogenesis, filamentous actin (F-actin) and ankyrinB continuously move toward the soma (retrograde flow). Bead-tracking experiments show that ankyrinB mediates L1-CAM coupling with retrograde F-actin flow in these perisomatic structures. Ligation of the L1-CAM ectodomain by an immobile substrate induces L1CD–ankyrinB binding and the formation of stationary ankyrinB clusters. Neurite initiation preferentially occurs at the site of these clusters. In contrast, ankyrinB is involved neither in L1-CAM coupling with F-actin flow in growth cones nor in L1-based neurite elongation. Our results indicate that ankyrinB promotes neurite initiation by acting as a component of the clutch module that transmits traction force generated by F-actin flow to the extracellular substrate via L1-CAM.
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Whittard, John D., Takeshi Sakurai, Melanie R. Cassella, Mihaela Gazdoiu, and Dan P. Felsenfeld. "MAP Kinase Pathway–dependent Phosphorylation of the L1-CAM Ankyrin Binding Site Regulates Neuronal Growth." Molecular Biology of the Cell 17, no. 6 (June 2006): 2696–706. http://dx.doi.org/10.1091/mbc.e06-01-0090.

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The growth of neuronal processes depends critically on the function of adhesion proteins that link extracellular ligands to the cytoskeleton. The neuronal adhesion protein L1-CAM serves as a receptor for nerve growth–promoting proteins, a process that is inhibited by the interaction between L1-CAM and the cytoskeleton adaptor ankyrin. Using a novel reporter based on intramolecular bioluminescence resonance energy transfer, we have determined that the MAP kinase pathway regulates the phosphorylation of the FIGQY motif in the adhesion protein L1-CAM and its interaction with ankyrin B. MAP kinase pathway inhibitors block L1-CAM–mediated neuronal growth. However, this blockade is partially rescued by inhibitors of L1-CAM–ankyrin binding. These results demonstrate that the MAP kinase pathway regulates L1-CAM–mediated nerve growth by modulating ankyrin binding, suggesting that nerve growth can be regulated at the level of individual receptors.
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Sakurai, Takeshi, Marc Lustig, Joanne Babiarz, Andrew J. W. Furley, Steven Tait, Peter J. Brophy, Stephen A. Brown, Lucia Y. Brown, Carol A. Mason, and Martin Grumet. "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in cerebellar granule cell development." Journal of Cell Biology 154, no. 6 (September 17, 2001): 1259–74. http://dx.doi.org/10.1083/jcb.200104122.

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The structurally related cell adhesion molecules L1 and Nr-CAM have overlapping expression patterns in cerebellar granule cells. Here we analyzed their involvement in granule cell development using mutant mice. Nr-CAM–deficient cerebellar granule cells failed to extend neurites in vitro on contactin, a known ligand for Nr-CAM expressed in the cerebellum, confirming that these mice are functionally null for Nr-CAM. In vivo, Nr-CAM–null cerebella did not exhibit obvious histological defects, although a mild size reduction of several lobes was observed, most notably lobes IV and V in the vermis. Mice deficient for both L1 and Nr-CAM exhibited severe cerebellar folial defects and a reduction in the thickness of the inner granule cell layer. Additionally, anti-L1 antibodies specifically disrupted survival and maintenance of Nr-CAM–deficient granule cells in cerebellar cultures treated with antibodies. The combined results indicate that Nr-CAM and L1 play a role in cerebellar granule cell development, and suggest that closely related molecules in the L1 family have overlapping functions.
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Seilheimer, B., and M. Schachner. "Studies of adhesion molecules mediating interactions between cells of peripheral nervous system indicate a major role for L1 in mediating sensory neuron growth on Schwann cells in culture." Journal of Cell Biology 107, no. 1 (July 1, 1988): 341–51. http://dx.doi.org/10.1083/jcb.107.1.341.

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The involvement of the adhesion molecules L1, N-CAM, and J1 in adhesion and neurite outgrowth in the peripheral nervous system was investigated. We prepared Schwann cells and fibroblasts (from sciatic nerves) and neurons (from dorsal root ganglia) from 1-d mice. These cells were allowed to interact with each other in a short-term adhesion assay. We also measured outgrowth of dorsal root ganglion neurons on Schwann cell and fibroblast monolayers. Schwann cells (which express L1, N-CAM, and J1) adhered most strongly to dorsal root ganglion neurons by an L1-dependent mechanism and less by N-CAM and J1. Schwann cell-Schwann cell adhesion was mediated by L1 and N-CAM, but not J1. Adhesion of fibroblasts (which express N-CAM, but not L1 or J1) to neurons or Schwann cells was mediated by L1 and N-CAM and not J1. However, inhibition by L1 and N-CAM antibodies was found to be less pronounced with fibroblasts than with Schwann cells. N-CAM was also strongly involved in fibroblast-fibroblast adhesion. Neurite outgrowth was most extensive on Schwann cells and less on fibroblasts. A difference in extent of neurite elongation was seen between small- (10-20 microns) and large- (20-35 microns) diameter neurons, with the larger neurons tending to exhibit longer neurites. Fab fragments of polyclonal L1, N-CAM, and J1 antibodies exerted slightly different inhibitory effects on neurite outgrowth, depending on whether the neurites were derived from small or large neurons. L1 antibodies interfered most strikingly with neurite outgrowth on Schwann cells (inhibition of 88% for small and 76% for large neurons), while no inhibition was detectable on fibroblasts. Similarly, although to a smaller extent than L1, N-CAM appeared to be involved in neurite outgrowth on Schwann cells and not on fibroblasts. Antibodies to J1 only showed a very small effect on neurite outgrowth of large neurons on Schwann cells. These observations show for the first time that identified adhesion molecules are potent mediators of glia-dependent neurite formation and attribute to L1 a predominant role in neurite outgrowth on Schwann cells which may be instrumental in regeneration.
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Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. "Functional cooperation between the neural adhesion molecules L1 and N-CAM is carbohydrate dependent." Journal of Cell Biology 110, no. 1 (January 1, 1990): 209–18. http://dx.doi.org/10.1083/jcb.110.1.209.

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The neural cell adhesion molecules L1 and N-CAM have been suggested to interact functionally by formation of a complex between the two molecules (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. 1990. J. Cell Biol. 110:193-208). To determine the molecular mechanisms underlying this functional cooperation, we have studied the contribution of carbohydrates to the association of the two molecules at the cell surface. Aggregation or adhesion between L1- and N-CAM-positive neuroblastoma N2A cells was reduced when the synthesis of complex and/or hybrid glycans was modified by castanospermine. Fab fragments of polyclonal antibodies to L1 inhibited aggregation and adhesion of castanospermine-treated cells almost completely, whereas untreated cells were inhibited by approximately 50%. Fab fragments of polyclonal antibodies to N-CAM did not interfere with the interaction between castanospermine-treated cells, whereas they inhibited aggregation or adhesion of untreated cells by approximately 50%. These findings indicate that cell interactions depending both on L1 and N-CAM ("assisted homophilic" binding) can be reduced to an L1-dominated interaction ("homophilic binding"). Treatment of cells with the carbohydrate synthesis inhibitor swainsonine did not modify cell aggregation in the absence or presence of antibodies compared with untreated cells, indicating that castanospermine-sensitive, but swainsonine-insensitive glycans are involved. To investigate whether the appropriate carbohydrate composition is required for an association of L1 and N-CAM in the surface membrane (cis-interaction) or between L1 on one side and L1 and N-CAM on the other side of interacting partner cells (trans-interaction), an L1-positive lymphoid tumor cell line was coaggregated with and adhered to neuroblastoma cells in the various combinations of castanospermine-treated and untreated cells. The results show that it is the cis-interaction between L1 and N-CAM that depends on the appropriate carbohydrate structures.
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Martini, R., and M. Schachner. "Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and myelin-associated glycoprotein) in regenerating adult mouse sciatic nerve." Journal of Cell Biology 106, no. 5 (May 1, 1988): 1735–46. http://dx.doi.org/10.1083/jcb.106.5.1735.

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The localization of the neural cell adhesion molecules L1, N-CAM, and the myelin-associated glycoprotein was studied by pre- and postembedding staining procedures at the light and electron microscopic levels in transected and crushed adult mouse sciatic nerve. During the first 2-6 d after transection, myelinated and nonmyelinated axons degenerated in the distal part of the proximal stump close to the transection site and over the entire length of the distal part of the transected nerve. During this time, regrowing axons were seen only in the proximal, but not in the distal nerve stump. In most cases L1 and N-CAM remained detectable at cell contacts between nonmyelinating Schwann cells and degenerating axons as long as these were still morphologically intact. Similarly, myelin-associated glycoprotein remained detectable in the periaxonal area of the degenerating myelinated axons. During and after degeneration of axons, nonmyelinating Schwann cells formed slender processes which were L1 and N-CAM positive. They resembled small-diameter axons but could be unequivocally identified as Schwann cells by chronical denervation. Unlike the nonmyelinating Schwann cells, only few myelinating ones expressed L1 and N-CAM. At the cut ends of the nerve stumps a cap developed (more at the proximal than at the distal stump) that contained S-100-negative and fibronectin-positive fibroblast-like cells. Most of these cells were N-CAM positive but always L1 negative. Growth cones and regrowing axons expressed N-CAM and L1 at contact sites with these cells. Regrowing axons of small diameter were L1 and N-CAM positive where they made contact with each other or with Schwann cells, while large-diameter axons were only poorly antigen positive or completely negative. 14 d after transection, when regrowing axons were seen in the distal part of the transected nerve, regrowing axons made L1- and N-CAM-positive contacts with Schwann cells. When contacting basement membrane, axons were rarely found to express L1 and N-CAM. Most, if not all, Schwann cells associated with degenerating myelin expressed L1 and N-CAM. In crushed nerves, the immunostaining pattern was essentially the same as in the cut nerve. During formation of myelin, the sequence of adhesion molecule expression was the same as during development: L1 disappeared and N-CAM was reduced on myelinating Schwann cells and axons after the Schwann cell process had turned approximately 1.5 loops around the axon. Myelin-associated glycoprotein then appeared both periaxonally and on the turning loops of Schwann cells in the uncompacted myelin.(ABSTRACT TRUNCATED AT 400 WORDS)
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Colombo, Federico, and Jacopo Meldolesi. "L1-CAM and N-CAM: From Adhesion Proteins to Pharmacological Targets." Trends in Pharmacological Sciences 36, no. 11 (November 2015): 769–81. http://dx.doi.org/10.1016/j.tips.2015.08.004.

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Abe, Kouki, Hiroko Katsuno, Michinori Toriyama, Kentarou Baba, Tomoyuki Mori, Toshio Hakoshima, Yonehiro Kanemura, Rikiya Watanabe, and Naoyuki Inagaki. "Grip and slip of L1-CAM on adhesive substrates direct growth cone haptotaxis." Proceedings of the National Academy of Sciences 115, no. 11 (February 26, 2018): 2764–69. http://dx.doi.org/10.1073/pnas.1711667115.

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Chemical cues presented on the adhesive substrate direct cell migration, a process termed haptotaxis. To migrate, cells must generate traction forces upon the substrate. However, how cells probe substrate-bound cues and generate directional forces for migration remains unclear. Here, we show that the cell adhesion molecule (CAM) L1-CAM is involved in laminin-induced haptotaxis of axonal growth cones. L1-CAM underwent grip and slip on the substrate. The ratio of the grip state was higher on laminin than on the control substrate polylysine; this was accompanied by an increase in the traction force upon laminin. Our data suggest that the directional force for laminin-induced growth cone haptotaxis is generated by the grip and slip of L1-CAM on the substrates, which occur asymmetrically under the growth cone. This mechanism is distinct from the conventional cell signaling models for directional cell migration. We further show that this mechanism is disrupted in a human patient with L1-CAM syndrome, suffering corpus callosum agenesis and corticospinal tract hypoplasia.
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Dissertations / Theses on the topic "L1-CAM"

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Schulze, Annekatrin. "L1-CAM - ein Tumormarker für das Kolorektale Karzinom?" Doctoral thesis, Universitätsbibliothek Leipzig, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-212580.

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Das Kolorektale Karzinom (KRK) ist eines der häufigsten malignen Erkrankungen, an der in Deutschland jährlich 26000 Menschen versterben. Auf der Suche nach einem neuen Biomarker für dieses Malignom wurde in dieser Arbeit L1-CAM, ein neuronales Zell-Adhäsionsmolekül, untersucht. Es ist, exprimiert an der Zelloberfläche, assoziiert mit einem signifikant schlechteren Outcome bedingt durch eine raschere lokale Tumorausbreitung und Metastasierung. Es zeigte sich anhand der Untersuchung von 62 Tumorpräparate und 39 präoperativ gewonnenen Seren, dass L1-CAM sowohl immunhistologisch nachgewiesen auf der Tumoroberfläche als auch mittels ELISA bestimmt im Serum der Patienten nachweisbar ist. Patienten mit L1-CAM positiven Tumoren waren im Mittel deutlich jünger als Patienten ohne L1-CAM Expression (60 vs. 69 Jahre). Zudem zeigte sich, dass Patienten mit schwach L1-CAM positiven Tumoren im Mittel einen signifikant höheren BMI aufwiesen (Kruskal Wallis Test p=0,0354). Die L1-CAM Expression hatte in unserem Patientengut keinen signifikanten Einfluss auf die Tumorausbreitung, wenngleich wir eine häufigere Metastasierung in die Leber (44%) bei L1-CAM positiven Tumoren gegenüber Patienten ohne L1-CAM Expression im Tumor (29%) beobachteten. Gleiches gilt für die Infiltration der Perineuralscheiden durch Tumorzellen. Bei der Untersuchung der L1-CAM Serumkonzentrationen zeigte sich im Mittel kein signifikanter Unterschied zu einer gesunden Vergleichsgruppe, sodass L1-CAM als Serum-Tumormarker ungeeignet ist.
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Knogler, Karin. "Expression, Reinigung und Charakterisierung rekombinanter anti-L1-CAM Antikörper chCE₇." Zürich : ETH, Eidgenössische Technische Hochschule Zürich, Dept. Angewandte Biowissenschaften, Institut Pharmazeutische Wissenschaften, 2002. http://e-collection.ethbib.ethz.ch/show?type=dipl&nr=73.

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Heiz, Monika. "Growth control and L1-CAM phosphorylation in renal tumor cells diploma work /." Zürich : ETH, Eidgenössische Technische Hochschule Zürich, Departement Angewandte Biowissenschaften, Institut für Pharmazeutische Wissenschaften, 2000. http://e-collection.ethbib.ethz.ch/show?type=dipl&nr=14.

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Jouet, Monique Marie Helene. "The molecular genetics of X-linked hydrocephalus." Thesis, Open University, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295639.

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Schäfer, Michael. "Funktionelle Analyse krankheits-assoziierter Mutationen von L1 CAM und Charakterisierung eines neuen Mitglieds der Immunglobulinsuperfamilie." [S.l.] : [s.n.], 2004. http://www.diss.fu-berlin.de/2004/264/index.html.

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Schulze, Annekatrin [Verfasser], Robin [Akademischer Betreuer] Wachowiak, Ulf [Akademischer Betreuer] Bühligen, Uwe [Gutachter] Eichfeld, and Michael [Gutachter] Tachezy. "L1-CAM - ein Tumormarker für das Kolorektale Karzinom? / Annekatrin Schulze ; Gutachter: Uwe Eichfeld, Michael Tachezy ; Robin Wachowiak, Ulf Bühligen." Leipzig : Universitätsbibliothek Leipzig, 2016. http://d-nb.info/1240629613/34.

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Klinz, Stephan Georg. "Analysis of cell adhesion molecules L1 and N-CAM in phosphorylation-mediated signal transduction pathways in growth cones from fetal rat brain /." [S.l.] : [s.n.], 1995. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=11290.

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Pruvost, Née Dequidt Caroline. "Etude de la dynamique des adhésions neuronales N-cadhérine et L1 dans la croissance axonale et la synaptogenèse." Phd thesis, Université Victor Segalen - Bordeaux II, 2007. http://tel.archives-ouvertes.fr/tel-00164823.

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Lors des processus développementaux d'élongation axonale et de synaptogenèse, les protéines d'adhésion telles les cadhérines ou les Ig-CAM jouent des rôles fondamentaux en permettant la formation de contacts entre neurones. Pour étudier la dynamique de ces contacts et leurs rôles dans ces processus, nous avons mis en œuvre des techniques d'imagerie sur des neurones primaires d'hippocampe (clivage thrombine, FRAP, pinces optiques, quantum-dots), ceux-ci étant associés à un système semi-artificiel de microsphères recouvertes de protéines d'adhésion purifiées (N-cadhérine et L1). En utilisant une construction L1 portant une étiquette GFP extracellulaire clivable à la thrombine, j'ai pu précisé l'implication des processus de diffusion membranaire et d'exo- endocytose dans la dynamique des contacts L1-dépendants et obtenir des données quantitatives relatives à l'interaction homophile L1. J'ai également contribué à caractériser la liaison extracellulaire entre N-cadhérine et GluR2, sous-unité des récepteurs AMPA, et l'influence de l'expression de la N-cadhérine sur la mobilité de GluR2. L'interaction entre ces deux protéines pourrait être impliquée dans la formation et/ou la maturation des synapses.
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Krickhahn, Annika [Verfasser]. "Korrelation von L1-CAM-Expression im Neuroblastom mit klinischem Überleben / vorgelegt von Annika Krickhahn." 2008. http://d-nb.info/998105686/34.

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Schäfer, Michael [Verfasser]. "Funktionelle Analyse krankheits-assoziierter Mutationen von L1 CAM und Charakterisierung eines neuen Mitglieds der Immunglobulinsuperfamilie / vorgelegt von Michael Schäfer." 2004. http://d-nb.info/972494693/34.

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Conference papers on the topic "L1-CAM"

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Milde-Langosch, K., C. Schröder, V. Mueller, U. Schumacher, R. Wirtz, P. Altevogt, S. Krenkel, and F. Jaenicke. "Expression and Prognostic Value of L1-CAM in Breast Cancer." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-3044.

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Milde-Langosch, K., V. Dippel, C. Schröder, D. Wicklein, S. Hein, F. Jänicke, V. Müller, and U. Schumacher. "P2-01-17: L1-CAM Promotes Adhesion of Breast Cancer Cells to the Endothelium." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p2-01-17.

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Bondong, Sandra, Thomas Hielscher, Alain Zeimet, Robert Zeillinger, Isabelle Cadron, Jalid Sehouli, Ignace Vergote, et al. "Abstract 4723: Soluble L1-CAM in the ascites is a prognostic marker in ovarian cancer." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4723.

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Hong, Hao, Christine E. Brown, Stephen J. Forman, and Michael C. Jensen. "Abstract LB-166: Adoptive immunotherapy for ovarian cancer utilizing T cells engineered to target L1-CAM." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-lb-166.

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Tischler, Verena M., Silke Hausladen, Glen Kristiansen, Peter Altevogt, Holger Moch, and Alex Soltermann. "Abstract 2324: The cell adhesion molecule L1-CAM is expressed in non-small cell lung cancer and is a prognostic marker for progression free survival." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2324.

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