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Journal articles on the topic 'Ig superfamily'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Taheri, Maryam, Uri Saragovi, Abraham Fuks, Joe Makkerh, John Mort, and Clifford P. Stanners. "Self Recognition in the Ig Superfamily." Journal of Biological Chemistry 275, no. 35 (2000): 26935–43. http://dx.doi.org/10.1016/s0021-9258(19)61463-8.

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2

Resnick, David, Alan Pearson, and Monty Krieger. "The SRCR superfamily: a family reminiscent of the Ig superfamily." Trends in Biochemical Sciences 19, no. 1 (1994): 5–8. http://dx.doi.org/10.1016/0968-0004(94)90165-1.

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3

Engel, P., N. Wagner, A. S. Miller, and T. F. Tedder. "Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand." Journal of Experimental Medicine 181, no. 4 (1995): 1581–86. http://dx.doi.org/10.1084/jem.181.4.1581.

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CD22 is a B cell-restricted member of the immunoglobulin (Ig) superfamily that functions as an adhesion receptor for leukocytes and erythrocytes. CD22 is unique among members of the Ig superfamily in that it has been suggested to bind a series of sialic acid-dependent ligands, potentially through different functional domains expressed by different splice variants of CD22. In this study, the epitopes identified by a large panel of function-blocking and non-function-blocking CD22 monoclonal antibodies were localized to specific Ig-like domains, revealing that all function-blocking monoclonal ant

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4

Jin, D. Y., Z. L. Li, Q. Jin, Y. W. Hao, and Y. D. Hou. "Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily." Journal of Experimental Medicine 170, no. 2 (1989): 571–76. http://dx.doi.org/10.1084/jem.170.2.571.

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Striking similarities between vaccinia virus hemagglutinin (VVHA) and proteins belonging to the Ig superfamily clearly indicate that VVHA, a 315-amino acid glycoprotein expressed on the surface of the infected cells, is a novel viral protein that can be added to the expanding list of the Ig superfamily. Its deduced amino acid sequence contains one Ig-like domain at the NH2 terminus, followed by two tandem repeating units and a hydrophobic region, suggestive of membrane spanning. The results offer an opportunity for the further study of the probable evolutionary and possible functional relation

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5

Zhang, S. M. "Diversification of Ig Superfamily Genes in an Invertebrate." Science 305, no. 5681 (2004): 251–54. http://dx.doi.org/10.1126/science.1088069.

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6

Mokady, O. "Occam's Razor, invertebrate allorecognition and Ig superfamily evolution." Research in Immunology 147, no. 4 (1996): 241–46. http://dx.doi.org/10.1016/0923-2494(96)87227-0.

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7

Wang, Li, Rotem Rubinstein, Janet L. Lines, et al. "VISTA, a novel mouse Ig superfamily ligand that negatively regulates T cell responses." Journal of Experimental Medicine 208, no. 3 (2011): 577–92. http://dx.doi.org/10.1084/jem.20100619.

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The immunoglobulin (Ig) superfamily consists of many critical immune regulators, including the B7 family ligands and receptors. In this study, we identify a novel and structurally distinct Ig superfamily inhibitory ligand, whose extracellular domain bears homology to the B7 family ligand PD-L1. This molecule is designated V-domain Ig suppressor of T cell activation (VISTA). VISTA is primarily expressed on hematopoietic cells, and VISTA expression is highly regulated on myeloid antigen-presenting cells (APCs) and T cells. A soluble VISTA-Ig fusion protein or VISTA expression on APCs inhibits T

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8

de la Fuente, Miguel Angel, Pilar Pizcueta, Marga Nadal, Jaime Bosch, and Pablo Engel. "CD84 Leukocyte Antigen Is a New Member of the Ig Superfamily." Blood 90, no. 6 (1997): 2398–405. http://dx.doi.org/10.1182/blood.v90.6.2398.

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Abstract cDNA isolated from a human B-cell line Raji library was analyzed and shown to encode the full-length cDNA sequence of a novel cell-surface glycoprotein, initially termed HLy9-β. The predicted mature 307-amino acid protein was composed of two extracellular Ig-like domains, a hydrophobic transmembrane region, and an 83-amino acid cytoplasmic domain. The extracellular Ig-like domains presented structural and sequence homology with a group of members of the Ig superfamily that included CD2, CD48, CD58, and Ly9. Northern blot analysis showed that the expression of HLy9-β was predominantly

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9

de la Fuente, Miguel Angel, Pilar Pizcueta, Marga Nadal, Jaime Bosch, and Pablo Engel. "CD84 Leukocyte Antigen Is a New Member of the Ig Superfamily." Blood 90, no. 6 (1997): 2398–405. http://dx.doi.org/10.1182/blood.v90.6.2398.2398_2398_2405.

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cDNA isolated from a human B-cell line Raji library was analyzed and shown to encode the full-length cDNA sequence of a novel cell-surface glycoprotein, initially termed HLy9-β. The predicted mature 307-amino acid protein was composed of two extracellular Ig-like domains, a hydrophobic transmembrane region, and an 83-amino acid cytoplasmic domain. The extracellular Ig-like domains presented structural and sequence homology with a group of members of the Ig superfamily that included CD2, CD48, CD58, and Ly9. Northern blot analysis showed that the expression of HLy9-β was predominantly restricte

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10

Wai Wong, Chee, Danielle E. Dye, and Deirdre R. Coombe. "The Role of Immunoglobulin Superfamily Cell Adhesion Molecules in Cancer Metastasis." International Journal of Cell Biology 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/340296.

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Metastasis is a major clinical problem and results in a poor prognosis for most cancers. The metastatic pathway describes the process by which cancer cells give rise to a metastatic lesion in a new tissue or organ. It consists of interconnecting steps all of which must be successfully completed to result in a metastasis. Cell-cell adhesion is a key aspect of many of these steps. Adhesion molecules belonging to the immunoglobulin superfamily (Ig-SF) commonly play a central role in cell-cell adhesion, and a number of these molecules have been associated with cancer progression and a metastatic p

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11

George, Andrew, James S. Huston, and Edgar Haber. "Exploring and exploiting the antibody and Ig superfamily combining sites." Nature Biotechnology 14, no. 5 (1996): 584. http://dx.doi.org/10.1038/nbt0596-584.

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12

Mansour, M. H., and E. L. Cooper. "Tunicate Thy-1 — An invertebrate member of the ig superfamily." Developmental & Comparative Immunology 10, no. 1 (1986): 115. http://dx.doi.org/10.1016/0145-305x(86)90086-8.

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13

Daffre, Sirlei, and Ingrid Faye. "Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily." FEBS Letters 408, no. 2 (1997): 127–30. http://dx.doi.org/10.1016/s0014-5793(97)00397-9.

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14

Cole, Francesca, and Robert S. Krauss. "Microform Holoprosencephaly in Mice that Lack the Ig Superfamily Member Cdon." Current Biology 13, no. 5 (2003): 411–15. http://dx.doi.org/10.1016/s0960-9822(03)00088-5.

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15

Ferguson, K., H. Long, S. Cameron, W. T. Chang, and Y. Rao. "The Conserved Ig Superfamily Member Turtle Mediates Axonal Tiling in Drosophila." Journal of Neuroscience 29, no. 45 (2009): 14151–59. http://dx.doi.org/10.1523/jneurosci.2497-09.2009.

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16

Aguila, Brittany, Adina Brett Morris, Raffaella Spina, et al. "The Ig superfamily protein PTGFRN coordinates survival signaling in glioblastoma multiforme." Cancer Letters 462 (October 2019): 33–42. http://dx.doi.org/10.1016/j.canlet.2019.07.018.

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17

Faivre-Sarrailh, Catherine, France Gauthier, Natalia Denisenko-Nehrbass, André Le Bivic, Geneviève Rougon, and Jean-Antoine Girault. "The Glycosylphosphatidyl Inositol-Anchored Adhesion Molecule F3/Contactin Is Required for Surface Transport of Paranodin/Contactin-Associated Protein (Caspr)." Journal of Cell Biology 149, no. 2 (2000): 491–502. http://dx.doi.org/10.1083/jcb.149.2.491.

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Paranodin/contactin-associated protein (caspr) is a transmembrane glycoprotein of the neurexin superfamily that is highly enriched in the paranodal regions of myelinated axons. We have investigated the role of its association with F3/contactin, a glycosylphosphatidyl inositol (GPI)-anchored neuronal adhesion molecule of the Ig superfamily. Paranodin was not expressed at the cell surface when transfected alone in CHO or neuroblastoma cells. Cotransfection with F3 resulted in plasma membrane delivery of paranodin, as analyzed by confocal microscopy and cell surface biotinylation. The region that

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18

Streuli, M., N. X. Krueger, L. R. Hall, S. F. Schlossman, and H. Saito. "A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen." Journal of Experimental Medicine 168, no. 5 (1988): 1523–30. http://dx.doi.org/10.1084/jem.168.5.1523.

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A human gene (LAR) that hybridizes to mouse leukocyte common antigen cDNA under relaxed hybridization conditions was isolated. The LAR gene is expressed in a broad range of cells, including T lymphocytes, kidney, and prostate cells. The structure of the protein encoded by the LAR gene was deduced by determining the nucleotide sequences of a 7.7-kb LAR cDNA. The putative LAR protein is composed of a 1,234 amino acid extracellular region, a 24 amino acid transmembrane segment, and a 623 amino acid cytoplasmic region. The cytoplasmic region contains two homologous domains that have extensive sequ

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19

Seaver, E. C., E. M. Carpenter, and M. J. Bastiani. "REGA-1 is a GPI-linked member of the immunoglobulin superfamily present on restricted regions of sheath cell processes in grasshopper." Development 122, no. 2 (1996): 567–78. http://dx.doi.org/10.1242/dev.122.2.567.

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REGA-1 is a glycoprotein localized to sheath cell processes in the developing CNS when NBs are producing progeny and neurons are maturing and extending processes. It is also present on a subset of muscles and on the lumenal surface of the ectoderm in the embryonic appendages when pioneer neurons are growing into the CNS. REGA-1 is associated with the extracellular side of the cell membrane by a glycosyl-phosphatidylinositol linkage. We have identified a cDNA clone encoding REGA-1 using a sequence from purified protein. Sequence analysis defines REGA-1 as a novel member of the immunoglobulin su

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20

Zhou, H., A. Fuks, G. Alcaraz, TJ Bolling, and CP Stanners. "Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds." Journal of Cell Biology 122, no. 4 (1993): 951–60. http://dx.doi.org/10.1083/jcb.122.4.951.

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Both carcinoembryonic antigen (CEA) and neural cell adhesion molecule (NCAM) belong to the immunoglobulin supergene family and have been demonstrated to function as homotypic Ca(++)-independent intercellular adhesion molecules. CEA and NCAM cannot associate heterotypically indicating that they have different binding specificities. To define the domains of CEA involved in homotypic interaction, hybrid cDNAs consisting of various domains from CEA and NCAM were constructed and were transfected into a CHO-derived cell line; stable transfectant clones showing cell surface expression of CEA/NCAM chi

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21

Watson, F. L. "Extensive Diversity of Ig-Superfamily Proteins in the Immune System of Insects." Science 309, no. 5742 (2005): 1874–78. http://dx.doi.org/10.1126/science.1116887.

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22

Tan, Liming, Kelvin Xi Zhang, Matthew Y. Pecot, et al. "Ig Superfamily Ligand and Receptor Pairs Expressed in Synaptic Partners in Drosophila." Cell 163, no. 7 (2015): 1756–69. http://dx.doi.org/10.1016/j.cell.2015.11.021.

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23

Leppert, Christian A., Heike Diekmann, Claudia Paul, et al. "Neurolin Ig Domain 2 Participates in Retinal Axon Guidance and Ig Domains 1 and 3 in Fasciculation." Journal of Cell Biology 144, no. 2 (1999): 339–49. http://dx.doi.org/10.1083/jcb.144.2.339.

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The optic disk–directed growth of retinal ganglion cell axons is markedly disturbed in the presence of polyclonal antineurolin antibodies, which mildly affect fasciculation (Ott, H., M. Bastmeyer, and C.A.O. Stuermer, 1998. J. Neurosci. 18:3363–3372). New monoclonal antibodies (mAbs) against goldfish neurolin, an immunoglobulin (Ig) superfamily cell adhesion/recognition molecule with five Ig domains, were generated to assign function (guidance versus fasciculation) to specific Ig domains. By their ability or failure to recognize Chinese hamster ovary cells expressing recombinant neurolin with

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24

Marg, Andreas, Pinar Sirim, Frank Spaltmann, et al. "Neurotractin, A Novel Neurite Outgrowth-promoting Ig-like Protein that Interacts with CEPU-1 and LAMP." Journal of Cell Biology 145, no. 4 (1999): 865–76. http://dx.doi.org/10.1083/jcb.145.4.865.

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The formation of axon tracts in nervous system histogenesis is the result of selective axon fasciculation and specific growth cone guidance in embryonic development. One group of proteins implicated in neurite outgrowth, fasciculation, and guidance is the neural members of the Ig superfamily (IgSF). In an attempt to identify and characterize new proteins of this superfamily in the developing nervous system, we used a PCR-based strategy with degenerated primers that represent conserved sequences around the characteristic cysteine residues of Ig-like domains. Using this approach, we identified a

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25

Vielmetter, J., J. F. Kayyem, J. M. Roman, and W. J. Dreyer. "Neogenin, an avian cell surface protein expressed during terminal neuronal differentiation, is closely related to the human tumor suppressor molecule deleted in colorectal cancer." Journal of Cell Biology 127, no. 6 (1994): 2009–20. http://dx.doi.org/10.1083/jcb.127.6.2009.

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Using a monoclonal antibody, we have identified and characterized a previously unknown cell surface protein in chicken that we call neogenin and have determined its primary sequence. The deduced amino acid sequence and structure of neogenin characterize it as a member of the immunoglobulin (Ig) superfamily. Based on amino acid sequence similarities, neogenin is closely related to the human tumor suppressor molecule DCC (deleted in colorectal cancer). Neogenin and DCC define a subgroup of Ig superfamily proteins structurally distinct from other Ig molecules such as N-CAM, Ng-CAM, and Bravo/Nr-C

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26

Wang, Xiaoxu, Menno Van Lookeren Campagne, Kenneth J. Katschke, et al. "Prevention of Fatal C3 Glomerulopathy by Recombinant Complement Receptor of the Ig Superfamily." Journal of the American Society of Nephrology 29, no. 8 (2018): 2053–59. http://dx.doi.org/10.1681/asn.2018030270.

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Background C3 glomerulopathy (C3G) is a life-threatening kidney disease caused by dysregulation of the alternative pathway of complement (AP) activation. No approved specific therapy is available for C3G, although an anti-C5 mAb has been used off-label in some patients with C3G, with mixed results. Thus, there is an unmet medical need to develop other inhibitors of complement for C3G.Methods We used a murine model of lethal C3G to test the potential efficacy of an Fc fusion protein of complement receptor of the Ig superfamily (CRIg-Fc) in the treatment of C3G. CRIg-Fc binds C3b and inhibits C3

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27

Cheng, Yi, Xiaobin Li, John Kamholz, and Frank R. Burns. "Organization of the mouse GP42/Basigin gene: a member of the Ig superfamily." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1217, no. 3 (1994): 307–11. http://dx.doi.org/10.1016/0167-4781(94)90290-9.

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28

Bettencourt, Raul, Humberto Lanz-Mendoza, Katarina Roxstrom Lindquist, and Ingrid Faye. "Cell Adhesion Properties of Hemolin, an Insect Immune Protein in the Ig Superfamily." European Journal of Biochemistry 250, no. 3 (1997): 630–37. http://dx.doi.org/10.1111/j.1432-1033.1997.00630.x.

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29

Kang, J. S. "BOC, an Ig superfamily member, associates with CDO to positively regulate myogenic differentiation." EMBO Journal 21, no. 1 (2002): 114–24. http://dx.doi.org/10.1093/emboj/21.1.114.

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30

BENIAN, G. "Twitchin and related giant Ig superfamily members of C. elegans and other invertebrates." Advances in Biophysics 33 (1996): 183–98. http://dx.doi.org/10.1016/0065-227x(96)81674-1.

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31

Schäcke, Heike, Werner E. G. Müller, Vera Gamulin, and Baruch Rinkevich. "The Ig superfamily includes members from the lowest invertebrates to the highest vertebrates." Immunology Today 15, no. 10 (1994): 497–98. http://dx.doi.org/10.1016/0167-5699(94)90198-8.

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32

Lefranc, Marie-Paule, and Gérard Lefranc. "Immunoglobulins or Antibodies: IMGT® Bridging Genes, Structures and Functions." Biomedicines 8, no. 9 (2020): 319. http://dx.doi.org/10.3390/biomedicines8090319.

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IMGT®, the international ImMunoGeneTics® information system founded in 1989 by Marie-Paule Lefranc (Université de Montpellier and CNRS), marked the advent of immunoinformatics, a new science at the interface between immunogenetics and bioinformatics. For the first time, the immunoglobulin (IG) or antibody and T cell receptor (TR) genes were officially recognized as ‘genes’ as well as were conventional genes. This major breakthrough has allowed the entry, in genomic databases, of the IG and TR variable (V), diversity (D) and joining (J) genes and alleles of Homo sapiens and of other jawed verte

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33

Kirschbaum, NE, RJ Gumina, and PJ Newman. "Organization of the gene for human platelet/endothelial cell adhesion molecule-1 shows alternatively spliced isoforms and a functionally complex cytoplasmic domain." Blood 84, no. 12 (1994): 4028–37. http://dx.doi.org/10.1182/blood.v84.12.4028.bloodjournal84124028.

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Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a cell-cell adhesion molecule that is expressed on circulating platelets, on leukocytes, and at the intercellular junctions of vascular endothelial cells and mediates the interactions of these cells during the process of transendothelial cell migration. The cDNA for PECAM-1 encodes an open reading frame of 738 amino acids (aa) that is organized into a 27- aa signal peptide, a 574-aa extracellular domain composed of 6 Ig homology units, and a relatively long cytoplasmic tail of 118 aa containing multiple sites for posttranslational modi

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34

Abraira, Victoria E., Andrew F. Tucker, and Lisa V. Goodrich. "The Ig superfamily protein Lrig3 controls inner ear morphogenesis by regulating Netrin-1 expression." Developmental Biology 319, no. 2 (2008): 504. http://dx.doi.org/10.1016/j.ydbio.2008.05.133.

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35

Kelsh, Robert N. "Spotting a role for an Ig superfamily cell adhesion molecule in pigment pattern formation." Pigment Cell & Melanoma Research 26, no. 2 (2012): 161–62. http://dx.doi.org/10.1111/pcmr.12054.

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36

Chen, X., T. D. Kim, C. V. Carman, L. Z. Mi, G. Song, and T. A. Springer. "Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization." Proceedings of the National Academy of Sciences 104, no. 39 (2007): 15358–63. http://dx.doi.org/10.1073/pnas.0707406104.

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37

Tulp, Abraham, and Desireé Verwoerd. "Analysis of members of the Ig-gene superfamily by thermal gradient polyacrylamide gel electrophoresis." Electrophoresis 13, no. 1 (1992): 662–64. http://dx.doi.org/10.1002/elps.11501301139.

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38

Vellanki, Sri HariKrishna, Cathy E. Richards, Yvonne E. Smith, and Ann M. Hopkins. "The Contribution of Ig-Superfamily and MARVEL D Tight Junction Proteins to Cancer Pathobiology." Current Pathobiology Reports 4, no. 2 (2016): 37–46. http://dx.doi.org/10.1007/s40139-016-0105-7.

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39

Cheng, Linna, Shu-Ang Li, Yamei Yu, and Qiang Chen. "Protein production, crystallization and preliminary crystallographic analysis of the four N-terminal immunoglobulin domains of Down syndrome cell adhesion molecule 1." Acta Crystallographica Section F Structural Biology Communications 71, no. 6 (2015): 775–78. http://dx.doi.org/10.1107/s2053230x15008201.

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Down syndrome cell adhesion molecule 1 (Dscam1), a member of the immunoglobulin (Ig) superfamily, plays important roles in both the nervous and the immune systems. Via alternative RNA splicing,DrosophilaDscam1 encodes a vast family of Ig-containing proteins that exhibit isoform-specific homophilic binding. Whether different Dscam1 isoforms adopt the same dimerization mode is under debate, and the detailed mechanism of Dscam1 specificity remains unclear. In this study, eight different isforms of Dscam1 Ig1–4 have been cloned, overexpressed, purified to homogeneity and crystallized. X-ray data w

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40

Kang, Jong-Sun, Min Gao, Jessica L. Feinleib, Philip D. Cotter, Sarah N. Guadagno, and Robert S. Krauss. "CDO: An Oncogene-, Serum-, and Anchorage-regulated Member of the Ig/Fibronectin Type III Repeat Family." Journal of Cell Biology 138, no. 1 (1997): 203–13. http://dx.doi.org/10.1083/jcb.138.1.203.

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Cell adhesion molecules of the Ig superfamily are implicated in a wide variety of biological processes, including cell migration, axon guidance and fasciculation, and growth control and tumorigenesis. Expression of these proteins can be highly dynamic and cell type specific, but little is known of the signals that regulate such specificity. Reported here is the molecular cloning and characterization of rat CDO, a novel cell surface glycoprotein of the Ig superfamily that contains five Ig-like repeats, followed by three fibronectin type III–like repeats in its extracellular region, and a 256-am

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Volkmer, H., R. Leuschner, U. Zacharias, and F. G. Rathjen. "Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites." Journal of Cell Biology 135, no. 4 (1996): 1059–69. http://dx.doi.org/10.1083/jcb.135.4.1059.

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Neurofascin and NrCAM are two axon-associated transmembrane glycoproteins belonging to the L1 subgroup of the Ig superfamily. In this study, we have analyzed the interaction of both proteins using neurite outgrowth and binding assays. A neurofascin-Fc chimera was found to stimulate the outgrowth of tectal cells when immobilized on an inert surface but not as a soluble form using polylysine as substrate. Antibody blocking experiments demonstrate that neurite extension on immobilized neurofascin is mediated by NrCAM on the axonal surface. Under the reverse experimental conditions where NrCAM ind

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42

Liao, F., H. K. Huynh, A. Eiroa, T. Greene, E. Polizzi, and W. A. Muller. "Migration of monocytes across endothelium and passage through extracellular matrix involve separate molecular domains of PECAM-1." Journal of Experimental Medicine 182, no. 5 (1995): 1337–43. http://dx.doi.org/10.1084/jem.182.5.1337.

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During the inflammatory response, the adhesion molecule PECAM plays a crucial role in transendothelial migration, the passage of leukocytes across endothelium. We report here an additional role for PECAM in the subsequent migration of monocytes through the subendothelial extracellular matrix. PECAM has six immunoglobulin (Ig) superfamily domains. Monoclonal antibodies whose epitopes map to domains 1 and/or 2 selectively block monocyte migration through the endothelial junction, whereas those that map to domain 6 block only the migration through the extracellular matrix, trapping the monocyte b

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43

Mizutani, Kiyohito, and Yoshimi Takai. "Nectin spot: a novel type of nectin-mediated cell adhesion apparatus." Biochemical Journal 473, no. 18 (2016): 2691–715. http://dx.doi.org/10.1042/bcj20160235.

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Nectins are Ca2+-independent immunoglobulin (Ig) superfamily cell adhesion molecules constituting a family with four members, all of which have three Ig-like loops at their extracellular regions. Nectins play roles in the formation of a variety of cell–cell adhesion apparatuses. There are at least three types of nectin-mediated cell adhesions: afadin- and cadherin-dependent, afadin-dependent and cadherin-independent, and afadin- and cadherin-independent. In addition, nectins trans-interact with nectin-like molecules (Necls) with three Ig-like loops and other Ig-like molecules with one to three

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44

Borges, Luis, and David Cosman. "LIRs/ILTs/MIRs, inhibitory and stimulatory Ig-superfamily receptors expressed in myeloid and lymphoid cells." Cytokine & Growth Factor Reviews 11, no. 3 (2000): 209–17. http://dx.doi.org/10.1016/s1359-6101(00)00007-1.

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45

Yamagata, M., and J. R. Sanes. "Expanding the Ig Superfamily Code for Laminar Specificity in Retina: Expression and Role of Contactins." Journal of Neuroscience 32, no. 41 (2012): 14402–14. http://dx.doi.org/10.1523/jneurosci.3193-12.2012.

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46

Suter, Daniel M., Laura D. Errante, Victoria Belotserkovsky, and Paul Forscher. "The Ig Superfamily Cell Adhesion Molecule, apCAM, Mediates Growth Cone Steering by Substrate–Cytoskeletal Coupling." Journal of Cell Biology 141, no. 1 (1998): 227–40. http://dx.doi.org/10.1083/jcb.141.1.227.

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Dynamic cytoskeletal rearrangements are involved in neuronal growth cone motility and guidance. To investigate how cell surface receptors translate guidance cue recognition into these cytoskeletal changes, we developed a novel in vitro assay where beads, coated with antibodies to the immunoglobulin superfamily cell adhesion molecule apCAM or with purified native apCAM, replaced cellular substrates. These beads associated with retrograde F-actin flow, but in contrast to previous studies, were then physically restrained with a microneedle to simulate interactions with noncompliant cellular subst

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47

Buonavista, Nathalie, Christine Balzano, Pierre Pontarotti, Denis Le Paslier, and Pierre Golstein. "Molecular linkage of the human CTLA4 and CD28 Ig-superfamily genes in yeast artificial chromosomes." Genomics 13, no. 3 (1992): 856–61. http://dx.doi.org/10.1016/0888-7543(92)90169-s.

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48

Treubert, Ullrich, та Thomas Brümmendorf. "Functional Cooperation of β1-Integrins and Members of the Ig Superfamily in Neurite Outgrowth Induction". Journal of Neuroscience 18, № 5 (1998): 1795–805. http://dx.doi.org/10.1523/jneurosci.18-05-01795.1998.

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Gennarini, G., G. Cibelli, G. Rougon, M. G. Mattei, and C. Goridis. "The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin." Journal of Cell Biology 109, no. 2 (1989): 775–88. http://dx.doi.org/10.1083/jcb.109.2.775.

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Abstract:

Several members of the Ig superfamily are expressed on neural cells where they participate in surface interactions between cell bodies and processes. Their Ig domains are more closely related to each other than to Ig variable and constant domains and have been grouped into the C2 set. Here, we report the cloning and characterization of another member of this group, the mouse neuronal cell surface antigen F3. The F3 cDNA sequence contains an open reading frame that could encode a 1,020-amino acid protein consisting of a signal sequence, six Ig-like domains of the C2 type, a long premembrane reg

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Rogalski, Teresa M., Mary M. Gilbert, Danelle Devenport, Kenneth R. Norman, and Donald G. Moerman. "DIM-1, a Novel Immunoglobulin Superfamily Protein in Caenorhabditis elegans, Is Necessary for Maintaining Bodywall Muscle Integrity." Genetics 163, no. 3 (2003): 905–15. http://dx.doi.org/10.1093/genetics/163.3.905.

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Abstract The UNC-112 protein is required during initial muscle assembly in C. elegans to form dense bodies and M-lines. Loss of this protein results in arrest at the twofold stage of embryogenesis. In contrast, a missense mutation in unc-112 results in viable animals that have disorganized bodywall muscle and are paralyzed as adults. Loss or reduction of dim-1 gene function can suppress the severe muscle disruption and paralysis exhibited by these mutant hermaphrodites. The overall muscle structure in hermaphrodites lacking a functional dim-1 gene is slightly disorganized, and the myofilament

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