Relevant bibliographies by topics / C-type lectin domain

Academic literature on the topic 'C-type lectin domain'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "C-type lectin domain"

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Zelensky, Alex N., and Jill E. Gready. "The C-type lectin-like domain superfamily." FEBS Journal 272, no. 24 (December 2005): 6179–217. http://dx.doi.org/10.1111/j.1742-4658.2005.05031.x.

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Eble, Johannes. "Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms." Toxins 11, no. 3 (March 1, 2019): 136. http://dx.doi.org/10.3390/toxins11030136.

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Snake venoms contain an astounding variety of different proteins. Among them are numerous C-type lectin family members, which are grouped into classical Ca2+- and sugar-binding lectins and the non-sugar-binding snake venom C-type lectin-related proteins (SV-CLRPs), also called snaclecs. Both groups share the robust C-type lectin domain (CTLD) fold but differ in a long loop, which either contributes to a sugar-binding site or is expanded into a loop-swapping heterodimerization domain between two CLRP subunits. Most C-type lectin (-related) proteins assemble in ordered supramolecular complexes with a high versatility of subunit numbers and geometric arrays. Similarly versatile is their ability to inhibit or block their target molecules as well as to agonistically stimulate or antagonistically blunt a cellular reaction triggered by their target receptor. By utilizing distinct interaction sites differentially, SV-CLRPs target a plethora of molecules, such as distinct coagulation factors and receptors of platelets and endothelial cells that are involved in hemostasis, thrombus formation, inflammation and hematogenous metastasis. Because of their robust structure and their high affinity towards their clinically relevant targets, SV-CLRPs are and will potentially be valuable prototypes to develop new diagnostic and therapeutic tools in medicine, provided that the molecular mechanisms underlying their versatility are disclosed.
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XU, Qiang, Xiang-Fu WU, Qi-Chang XIA, and Ke-Yi WANG. "Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri." Biochemical Journal 341, no. 3 (July 26, 1999): 733–37. http://dx.doi.org/10.1042/bj3410733.

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A galactose-binding lectin isolated from the venom of Trimeresurus stejnegeri is a homodimer C-type lectin. The cloned cDNA encoding the monomer of Trimeresurus stejnegerilectin (TSL) was sequenced and found to contain a 5′-end non-coding region, a sequence which encodes 135 amino acids, including a typical 23 amino acid signal peptide followed by the mature protein sequence, a 3′-end non-coding region, a polyadenylation signal, and a poly(A) region. To completely characterize the deduced amino acid sequence, on-line HPLC-MS and tandem MS were used to analyse the intact monomer and its proteolytic peptides. A modified peptide fragment was also putatively identified by HPLC-MS analysis. The deduced amino acid sequence was found to contain a carbohydrate-recognition domain homologous with those of some known C-type animal lectins. Thus TSL belongs to group VII of the C-type animal lectins as classified by Drickamer [(1993) Prog. Nucleic Acid Res. Mol. Biol. 45, 207-232]. At present, a number of C-type lectins have been purified from snake venom, but most of them have been characterized only at the protein level. To our knowledge, this is the first known cDNA sequence of a true C-type lectin from snake venom.
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Zhao, Zhi-Ying, Zhi-Xin Yin, Xiao-Peng Xu, Shao-Ping Weng, Xia-Yu Rao, Zong-Xian Dai, Yong-Wen Luo, et al. "A Novel C-Type Lectin from the Shrimp Litopenaeus vannamei Possesses Anti-White Spot Syndrome Virus Activity." Journal of Virology 83, no. 1 (October 22, 2008): 347–56. http://dx.doi.org/10.1128/jvi.00707-08.

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ABSTRACT C-type lectins play key roles in pathogen recognition, innate immunity, and cell-cell interactions. Here, we report a new C-type lectin (C-type lectin 1) from the shrimp Litopenaeus vannamei (LvCTL1), which has activity against the white spot syndrome virus (WSSV). LvCTL1 is a 156-residue polypeptide containing a C-type carbohydrate recognition domain with an EPN (Glu99-Pro100-Asn101) motif that has a predicted ligand binding specificity for mannose. Reverse transcription-PCR analysis revealed that LvCTL1 mRNA was specifically expressed in the hepatopancreas of L. vannamei. Recombinant LvCTL1 (rLvCTL1) had hemagglutinating activity and ligand binding specificity for mannose and glucose. rLvCTL1 also had a strong affinity for WSSV and interacted with several envelope proteins of WSSV. Furthermore, we showed that the binding of rLvCTL1 to WSSV could protect shrimps from viral infection and prolong the survival of shrimps against WSSV infection. Our results suggest that LvCTL1 is a mannose-binding C-type lectin that binds to envelope proteins of WSSV to exert its antiviral activity. To our knowledge, this is the first report of a shrimp C-type lectin that has direct anti-WSSV activity.
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Bezouška, Karel. "Carbohydrate and Non-Carbohydrate Ligands for the C-Type Lectin-Like Receptors of Natural Killer Cells. A Review." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 535–63. http://dx.doi.org/10.1135/cccc20040535.

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The superfamily of C-type animal lectins is defined by a sequence motif of the carbohydrate- recognition domains (CRDs) and comprises seven groups of molecules. The soluble proteins are group I proteoglycans, group III collectins, and group VII containing the isolated CRDs. Type I membrane proteins include group IV selectins and group VI macrophage receptors and related molecules. Type II membrane proteins are group II hepatic lectins and group V natural killer cell receptors. The latter group has recently attracted considerable attention of the biomedical community. These receptors are arranged at the surface of lymphocytes as homo- or heterodimers composed of two polypeptides consisting of N-terminal peptide tails responsible for signaling, transmembrane domain, neck regions of varying length, and C-terminal lectin-like domains (CTLDs). Since this group is evolutionarily most distant from the rest of C-type animal lectins, the sequence of the C-terminal ligand-binding domain has diversified to accommodate other ligands than calcium or carbohydrates. These domains are referred to as natural killer domains (NKDs) forming a large percentage of CTLDs in vertebrates. Here are summarized the data indicating that calcium, carbohydrates, peptides, and large proteins such as major histocompatibility complex (MHC) class I can all be ligands for NKDs. The wide range of ligands that can be recognized by NKDs includes some new, unexpected compounds such as signal peptide-derived fragments, heat shock proteins, or oxidized lipids. The biological importance of this extended range of recognition abilities is also discussed. A review with 134 references.
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Zhang, Huan, Xiaoyan Song, Lingling Wang, Pengfei Kong, Jialong Yang, Lin Liu, Limei Qiu, Ying Zhang, Lihua Qiu, and Linsheng Song. "AiCTL-6, a novel C-type lectin from bay scallop Argopecten irradians with a long C-type lectin-like domain." Fish & Shellfish Immunology 30, no. 1 (January 2011): 17–26. http://dx.doi.org/10.1016/j.fsi.2009.12.019.

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Flores-Ibarra, Andrea, Federico M. Ruiz, Sabine Vértesy, Sabine André, Hans-Joachim Gabius, and Antonio Romero. "Preliminary X-ray crystallographic analysis of an engineered variant of human chimera-type galectin-3 with a shortened N-terminal domain." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 184–88. http://dx.doi.org/10.1107/s2053230x15000023.

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How lectins translate sugar-encoded information into cellular effects not only depends on glycan recognition. Other domains of the protein can contribute to the functional profile of a lectin. Human galectin-3 (Gal-3), an adhesion/growth-regulatory galectin, is composed of three different domains and is thus called a chimera-type protein. In addition to the carbohydrate-recognition domain, this lectin encompasses an N-terminal domain consisting of a peptide harbouring two phosphorylation sites and nine non-triple-helical collagen-like repeats. This region plays an as yet structurally undefined role in Gal-3 aggregation and ligand recognition. To date, crystallization of full-length Gal-3 has not been achieved. With the aim of providing structural insights into this modular organization, a Gal-3 variant was crystallized maintaining the terminal peptide and three of the nine collagen-like repeats. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 94.04,b= 97.96,c= 236.20 Å, and diffracted to a resolution of 3.3 Å.
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Horstkorte, R., M. Schachner, J. P. Magyar, T. Vorherr, and B. Schmitz. "The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth." Journal of Cell Biology 121, no. 6 (June 15, 1993): 1409–21. http://dx.doi.org/10.1083/jcb.121.6.1409.

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We have previously shown that the neural adhesion molecules L1 and NCAM interact with each other to form a complex which binds more avidly to L1 than L1 to L1 alone (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. 1990a. J. Cell Biol. 110:193-208). This cis-association between L1 and NCAM is carbohydrate-dependent (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. 1990b. J. Cell Biol. 110:209-218). In the present study, we report that L1 and NCAM bind to each other via oligomannosidic carbohydrates expressed by L1, but not by NCAM, as shown in several experiments: (a) complex formation between L1 and NCAM is inhibited by a mAb to oligomannosidic carbohydrates and by the oligosaccharides themselves; (b) NCAM binds to oligomannosidic carbohydrates; (c) within the L1/NCAM complex, the oligomannosidic carbohydrates are hidden from accessibility to a mAb against oligomannosidic carbohydrates; (d) the recombinant protein fragment of NCAM containing the immunoglobulin-like domains and not the fragment containing the fibronectin type III homologous repeats binds to oligomannosidic glycans. Furthermore, the fourth immunoglobulin-like domain of NCAM shows sequence homology with carbohydrate recognition domains of animal C-type lectins and, surprisingly, also with plant lectins. A peptide comprising part of the C-type lectin consensus sequence in the fourth immunoglobulin-like domain of NCAM interferes with the association between L1 and NCAM. The functional importance of oligomannosidic glycans at the cell surface was shown for neurite outgrowth in vitro. When neurons from early postnatal mouse cerebellum were maintained on laminin or poly-L-lysine, neurite outgrowth was inhibited by oligomannosidic glycans, by glycopeptides, glycoproteins, or neoglycolipids containing oligomannosidic glycans, but not by nonrelated oligosaccharides or oligosaccharide derivates. Neurite outgrowth was also inhibited by the peptide comprising part of the C-type lectin consensus sequence in the fourth immunoglobulin-like domain of NCAM. The combined results suggest that carbohydrate-mediated cis-associations between adhesion molecules at the cell surface modulate their functional properties.
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Takada, Ayato, Kouki Fujioka, Makoto Tsuiji, Akiko Morikawa, Nobuaki Higashi, Hideki Ebihara, Darwyn Kobasa, Heinz Feldmann, Tatsuro Irimura, and Yoshihiro Kawaoka. "Human Macrophage C-Type Lectin Specific for Galactose and N-Acetylgalactosamine Promotes Filovirus Entry." Journal of Virology 78, no. 6 (March 15, 2004): 2943–47. http://dx.doi.org/10.1128/jvi.78.6.2943-2947.2004.

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ABSTRACT Filoviruses cause lethal hemorrhagic disease in humans and nonhuman primates. An initial target of filovirus infection is the mononuclear phagocytic cell. Calcium-dependent (C-type) lectins such as dendritic cell- or liver/lymph node-specific ICAM-3 grabbing nonintegrin (DC-SIGN or L-SIGN, respectively), as well as the hepatic asialoglycoprotein receptor, bind to Ebola or Marburg virus glycoprotein (GP) and enhance the infectivity of these viruses in vitro. Here, we demonstrate that a recently identified human macrophage galactose- and N-acetylgalactosamine-specific C-type lectin (hMGL), whose ligand specificity differs from DC-SIGN and L-SIGN, also enhances the infectivity of filoviruses. This enhancement was substantially weaker for the Reston and Marburg viruses than for the highly pathogenic Zaire virus. We also show that the heavily glycosylated, mucin-like domain on the filovirus GP is required for efficient interaction with this lectin. Furthermore, hMGL, like DC-SIGN and L-SIGN, is present on cells known to be major targets of filoviruses (i.e., macrophages and dendritic cells), suggesting a role for these C-type lectins in viral replication in vivo. We propose that filoviruses use different C-type lectins to gain cellular entry, depending on the cell type, and promote efficient viral replication.
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Melin Fürst, Camilla, Matthias Mörgelin, Kasper Vadstrup, Dick Heinegård, Anders Aspberg, and Anna M. Blom. "The C-Type Lectin of the Aggrecan G3 Domain Activates Complement." PLoS ONE 8, no. 4 (April 15, 2013): e61407. http://dx.doi.org/10.1371/journal.pone.0061407.

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Dissertations / Theses on the topic "C-type lectin domain"

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Zelensky, Alex N., and Alex Zelensky@anu edu au. "In silico analysis of C-type lectin domains’ structure and properties." The Australian National University. The John Curtin School of Medical Research, 2005. http://thesis.anu.edu.au./public/adt-ANU20050318.185314.

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Members of the C-type lectin domain (CTLD) superfamily are metazoan proteins functionally important in glycoprotein metabolism, mechanisms of multicellular integration and immunity. This thesis presents the results of several computational and experimental studies of the CTLD structure, function and evolution.¶ Core structural properties of the CTLD fold were explored in a comparative analysis of the 37 distinct CTLD structures available publicly, which demonstrate significant structural conservation despite low or undetectable sequence similarity. Pairwise structural alignments of all CTLD structures were created with three different methods (DALI, CE and LOCK) and analysed manually and using a computational algorithm developed for this purpose. The analysis revealed a set of conserved positions and interactions, which were classified based on their role in CTLD structure maintenance.¶ The CTLD family is large and diverse. To organize and annotate the several thousand of known CTLD-containing protein sequences and integrate the information on their evolution, structure and function a local database and a web-based interface to it were developed. The software is written in Perl, is based on bioperl, bioperl-db and Apache::ASP modules, and can be used for collaborative annotation of any collection of phylogenetically related sequences.¶ Several studies of CTLD genomics were performed. In one such study, carried out in collaboration with the RIKEN structural genomics centre, CTLD sequences from the Caenorhabditis elegans genome were identified and clustered into groups based on similarity. The most representative members of the groups were then selected, which if characterized structurally would tell most about the C. elegans CTLDs and provide templates for homology modelling of all C. elegans CTLD structures.¶ In the other whole-genome study, the CTLD family in the puffer fish Fugu rubripes was analysed using the draft genome sequence. This work extended and complemented three genome-level surveys on human, C. elegans and D. melanogaster reported previously. The study showed that the CTLD repertoire of Fugu rubripes is very similar to that of mammals, although several interesting differences exist, and that Fugu CTLD-encoding genes are selectively duplicated in a manner suggesting an ancient large-scale duplication event. Another important finding was the identification of several new CTLDcps, which had mammalian orthologues not recognized previously.¶ CBCP, a novel CTLD-containing protein highly conserved between fish and mammals with previously unknown domain architecture, was predicted in the Fugu study based solely on ab initio gene models from the Fugu locus and cross-species genomic DNA alignments. To test if the prediction was correct, a full-length cDNA of the mouse CBCP was cloned, its tissue distribution characterized and untranslated regions determined by RACE. The full-length mCBCP transcript is 10 kb long, encodes a protein of 2172 amino acids and confirms the original prediction. The presence of a large N-terminal NG2 domain makes CBCP a member of a small but very interesting family of Metazoan proteins.
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Pees, Barbara [Verfasser]. "The role of C-type lectin-like domain genes in C. elegans immunity / Barbara Pees." Kiel : Universitätsbibliothek Kiel, 2019. http://d-nb.info/1181096685/34.

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Poget, Sébastien François. "Functional and structural studies of C-type lectin domains." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621079.

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Zelensky, Alex N. "In silico analysis of C-type lectin domains' structure and properties /." View thesis entry in Australian Digital Theses Program, 2004. http://thesis.anu.edu.au/public/adt-ANU20050318.185314/index.html.

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Thesis (Ph.D.)--Australian National University, 2004.
"This CD contains the software (mostly written in Perl) used for comparative structure analysis reported in Chapter 4 (str_comp directory), and for the CTLD database system described in Chapter 2 (CTLD_DB directory)."
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Perrin, Christophe. "Variations quantitatives de l'état de sialylation de surface du macrophage alvéolaire exposé à l'inhalation de particules inorganiques et au cours de l'infection par HIV-1 et distribution cellulaire de la LSLCL, une nouvelle glycoprotéine à domaine lectine de type C." Aix-Marseille 2, 2001. http://theses.univ-amu.fr.lama.univ-amu.fr/2001AIX20690.pdf.

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L'activité phagocytaire du macrophage alvéolaire constitue la première ligne de défense du poumon contre les microorganismes et autres particules aérogènes. Cette fonction qui nécessite une première étape d'adhésion de la particule à ingérer à la membrane cellulaire, met en jeu des mécanismes spécifiques liés à la présence, en surface de la cellule, de récepteurs constitués en partie ou en totalité de structures glycoconjuguées. Aujourd'hui, il est admis que c'est la partie glucidique de ces complexes hydrocarbonés qui joue un rôle essentiel dans les phénomènes de reconnaissance moléculaire. Parmi les sucres impliqués, les acides sialiques sont particulièrement remarquables. En effet, leurs variations quantitatives et/ou qualitatives influencent l'interaction des récepteurs de membrane avec leurs ligands. Si de telles modifications conditionnent in fine l'interaction de la cellule avec son environnement extérieur, les facteurs qui en sont responsables ne sont pas clairement définis. Dans un travail portant sur le macrophage alvéolaire (MA) humain, nous montrons par immunofluorescence directe que la silice et surtout l'infection par HIV-1 entraînent une désialylation de surface significative. Plus encore, au cours du SIDA, nous mettons en évidence que cette perturbation de sialylation de membrane est particulièrement importante et que son intensité est spécifique de cette affection. La signification de cette modification de glycosylation, de même que ses conséquences au cours de l'infection par HIV-1, sont discutées. Les travaux mis en oeuvre au sein du laboratoire pour tenter de comprendre les mécanismes impliqués dans l'hyposialylation cellulaire rencontrée, ont permis de mettre en évidence l'existence d'une activité sialidase en surface du macrophage alvéolaire sans pour autant expliquer clairement la surdésialylation du MA objectivée au cours du SIDA. Surtout, ils ont permis d'isoler une nouvelle glycoprotéine à domaine lectine de type C dans le surnageant de culture de lignées lymphoblastiques infectées par le HIV-1. La recherche ex vivo de la distribution tissulaire et cellulaire de cette protéine, baptisée LSLCL, constitue la deuxième partie de ce manuscrit. Par immunocytochimie, western blot et northem blot, nous montrons que la LSLCL est spécifiquement localisée dans le cytoplasme des précurseurs médullaires de la lignée granuleuse neutrophile, et par méthode ELISA, que cette protéine essentiellement intracellulaire, est également sécrétée en petite quantité. La localisation cellulaire tout à fait précise de la LSLCL confrontée à son organisation structurale associant (i) un triplet RGD (NH2-terminal), (ii) un domaine leucine zipper comportant six heptades et enfin, (iii) un long domaine lectine de type C (COOH-terminal), lui confèrent de nombreuses hypothèses fonctionnelles qui font l'objet d'une discussion et ouvrent de nouvelles perspectives de recherche.
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Book chapters on the topic "C-type lectin domain"

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type Lectin Domain Family 4 Member E." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100318.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type Lectin-Domain Family 1 Member A." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100319.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type Lectin-Domain Family 1, Member a." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100320.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type Lectin-Domain Family 1, Member b." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100321.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type Lectin-Domain Family 5, Member A." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100322.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "CLEC1B, C-type Lectin-Domain Family 1, Member B." In Encyclopedia of Signaling Molecules, 413. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100280.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type (Calcium-Dependent, Carbohydrate Recognition Domain) Lectin Superfamily Member 9." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100316.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "C-type (Calcium-Dependent, Carbohydrate-Recognition Domain) lectin, Superfamily Member 5." In Encyclopedia of Signaling Molecules, 481. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100317.

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"C-Type Lectin Domain Family 4 Member E." In Encyclopedia of Signaling Molecules, 1241. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_100873.

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"C-Type Lectin-Domain Family 1 Member A." In Encyclopedia of Signaling Molecules, 1241. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_100874.

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Conference papers on the topic "C-type lectin domain"

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Hung, Chi, Yu-Hua Chow, Dan Ratner, and Lynn Schnapp. "Carbohydrate And Glycoprotein Binding By C-Type Lectin Domain In Endo180/uPARAP." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5571.

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