Relevant bibliographies by topics / C-lectins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'C-lectins'

Author: Grafiati
Published: 4 June 2025
Last updated: 1 August 2025

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Journal articles on the topic "C-lectins"

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Kothari, Sajani, Rebecca Heineman, and Rene Harrison. "Optimizing Lectin Staining Methodology to Assess Glycocalyx Composition of Legionella-Infected Cells." Undergraduate Research in Natural and Clinical Science and Technology (URNCST) Journal 7, no. 7 (2023): 1–10. http://dx.doi.org/10.26685/urncst.490.

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Introduction: Legionella is a gram-negative bacterium that replicates intracellularly within macrophages. Legionella utilizes effector proteins to hijack ER-Golgi vesicle trafficking to sustain proliferation in its intracellular niche. Legionella has a considerable influence on O-glycosylation but not N-glycosylation events in the Golgi of infected cells. This research aims to optimize the use of fluorescent lectins, which are proteins that bind carbohydrates, to effectively label host-cell glycocalyx during Legionella infection. Methods: Epifluorescence imaging or flow cytometry were used to
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Matsuno, Keita, Noriko Kishida, Katsuaki Usami, et al. "Different Potential of C-Type Lectin-Mediated Entry between Marburg Virus Strains." Journal of Virology 84, no. 10 (2010): 5140–47. http://dx.doi.org/10.1128/jvi.02021-09.

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ABSTRACT The glycoproteins (GPs) of filoviruses are responsible for virus entry into cells. It is known that GP interacts with cellular C-type lectins for virus attachment to cells. Since primary target cells of filoviruses express C-type lectins, C-type lectin-mediated entry is thought to be a possible determinant of virus tropism and pathogenesis. We compared the efficiency of C-type lectin-mediated entry between Marburg virus strains Angola and Musoke by using a vesicular stomatitis virus (VSV) pseudotype system. VSV pseudotyped with Angola GP (VSV-Angola) infected K562 cells expressing the
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Melgarejo, Luz Marina, Nohora Vega, and Gerardo Pérez. "Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds." Brazilian Journal of Plant Physiology 17, no. 3 (2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.

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Two lectins were isolated from Canavalia ensiformis and Dioclea grandiflora seeds. Gel filtration produced a fraction corresponding to Con A or D. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (RBCs) but not rabbit RBCs. Hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on Lac-Sepharose showing similar properties to that of the Phenyl-Sepharose-purified lectin.
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MISTRY, Abinash Chandra, Shinji HONDA, and Shigehisa HIROSE. "Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica)." Biochemical Journal 360, no. 1 (2001): 107–15. http://dx.doi.org/10.1042/bj3600107.

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Using a Japanese-eel (Anguilla japonica) gill cDNA subtraction library, two novel β-d-galactose-binding lectins were identified that belong to group VII of the animal C-type lectin family. The eel C-type lectins, termed eCL-1 and eCL-2, are simple lectins composed of 163 amino acid residues, including a 22-residue signal peptide for secretion and a single carbohydrate-recognition domain (CRD) of ∼ 130 residues typical of C-type lectins. The galactose specificity of the CRD was suggested by the presence of a QPD motif and confirmed by a competitive binding assay. Using Ruthenium Red staining, t
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Ahmmed, Mirja Kaizer, Shuva Bhowmik, Stephen G. Giteru, et al. "An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications." Marine Drugs 20, no. 7 (2022): 430. http://dx.doi.org/10.3390/md20070430.

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins
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Drickamer, Kurt, and Andrew J. Fadden. "Genomic analysis of C-type lectins." Biochemical Society Symposia 69 (October 1, 2002): 59–72. http://dx.doi.org/10.1042/bss0690059.

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Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are p
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Ahmed, E. M. "Lectin Quantitation in Peanut and Soybean Seeds1." Peanut Science 13, no. 1 (1986): 4–7. http://dx.doi.org/10.3146/i0095-3679-13-1-2.

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Abstract A method was developed to determine amounts of lectin in peanut and soybean seeds. Both types of seeds contained active lectins in amounts ranging from 144.7 to 112.2 μg/g defatted meal for peanut and soybean seed, respectively. Lectins were inactivated by heat; moist heat was more effective than dry heat. Roasted peanuts seeds (177 C for 30 min) and boiled peanuts (5% saline solution for 1 hr) were devoid of active lectin.
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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 (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 proteol
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Chen, Pengyu, Kristof De Schutter, Els J. M. Van Damme, and Guy Smagghe. "Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?" Insects 12, no. 6 (2021): 497. http://dx.doi.org/10.3390/insects12060497.

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Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions. Many plant lectins were identified as exogenous stimuli of vertebrate immunity. Despite being the largest and most diverse taxon on earth, the study of lectins and their functions in insects is lagging behind. In insects, research on lectins and their biological importance has mainly focused on the C-type lectin (CTL) family, limiting our global understanding of the functio
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Lefebre, Jonathan, Torben Falk, Yunzhan Ning, and Christoph Rademacher. "Secondary sites of the C-type lectin-like fold." Chemistry: A European Journal 30, no. 30 (2024): e202400660. https://doi.org/10.5281/zenodo.10908543.

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C-type lectins are a large superfamily of proteins involved in a multitude of biological processes. In particular, their involvement in immunity and homeostasis has rendered them attractive targets for diverse therapeutic interventions. They share a characteristic C-type lectin-like domain whose adaptability enables them to bind a broad spectrum of ligands beyond the originally defined canonical Ca<sup>2+</sup>-dependent carbohydrate binding. Together with variable domain architecture and high-level conformational plasticity, this enables C-type lectins to meet diverse functional demands. Seco
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Dissertations / Theses on the topic "C-lectins"

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Didak, Blanka. "Synthèse de néoglycoconjugués et dendrimères glycomimétiques utilisés pour le développement de puces à lectines de type C et leur validation." Thesis, Université Grenoble Alpes (ComUE), 2018. http://www.theses.fr/2018GREAV036.

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Les lectines de type-C (CLR) sont des protéines de liaison au glycane qui reconnaissent les sucres de manière dépendante du Ca2+. Ils ont des rôles divers dans l'organisme humain. Ils sont responsables des interactions et de l'internalisation d'agents pathogènes tels que Candida albicans, Mycobacterium tuberculosis, le VIH ou le virus Ebola. Ils sont également impliqués dans le développement ou la prévention du cancer par la reconnaissance de glycanes spécifiques exprimés à la surface des cellules tumorales.L'importance cruciale est de trouver des ligands pour les CLR qui induiront une réponse
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Bouyain, Samuel. "Binding of fucosylated and anionic glycans to C-type animal lectins." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393429.

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Kerscher, Berhard Gerhard Richard. "Characterisation of the C-type lectin receptor Clecsf8." Thesis, University of Aberdeen, 2016. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=230779.

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C-type lectin-like receptors (CTLRs) play critical roles in immunity and homeostasis by recognising a variety of microbial or endogenous ligands. Clecsf8 is a member of the Dectin-2 family of CTLRs. Clecsf8 shares important similarities with its relatives Mincle and Dectin-2, such as the lack of an integral signalling motif and a single, calcium dependent ligand binding domain. They were shown to associate with the FcRγ adaptor, which is essential for receptor surface expression and downstream signalling. Recent publications revealed an important role for Clecsf8 in anti-mycobacterial immunity
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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.<br>"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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Goti, G. "GLYCOMIMETIC ANTAGONISTS OF C-TYPE LECTINS: IMPROVING LIGAND POTENCY AND MULTIVALENT PRESENTATION." Doctoral thesis, Università degli Studi di Milano, 2017. http://hdl.handle.net/2434/483585.

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Le lectine di tipo C sono recettori calcio dipendenti in grado di riconoscere in modo selettivo e di legarsi a carboidrati esposti da patogeni e cellule danneggiate, agendo quindi come un’importante meccanismo di prima difesa. Tuttavia, lectine di tipo C possono essere responsabili della patogenesi di infezioni e malattie infiammatorie, costituendo così un promettente bersaglio terapeutico. Le interazioni proteina-carboidrato sono generalmente deboli, con costanti di dissociazione nell’ordine del millimolare. Tale problema di bassa ffinità è stato risolto in Natura ricorrendo alla multivale
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Freitas, Alcides Alves de. "Detec??o de prote?nas em Plectranthus barbatus e avalia??o da atividade biol?gica sobre linhagens de c?lulas RAW 264.7 e A549." UFVJM, 2017. http://acervo.ufvjm.edu.br/jspui/handle/1/1674.

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Submitted by Raniere Barreto (raniere.barros@ufvjm.edu.br) on 2018-05-10T17:58:30Z No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) alcides_alves_freitas.pdf: 1707403 bytes, checksum: f9233629066db73fd877b2885aa875bd (MD5)<br>Approved for entry into archive by Rodrigo Martins Cruz (rodrigo.cruz@ufvjm.edu.br) on 2018-05-14T14:47:32Z (GMT) No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) alcides_alves_freitas.pdf: 1707403 bytes, checksum: f9233629066db73fd877b2885aa875bd (MD5)<br>Made available in DSpace o
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Raziunaite, Ingrida. "Use of C-type lectin receptor probes and human monoclonal antibodies to map the dynamics of the fungal cell wall." Thesis, University of Aberdeen, 2018. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=238675.

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Martin, Nicole C. Couillard Nicole. "Differential dengue tropism & neutralization : potential mechanisms of pathogenesis /." Download the dissertation in PDF, 2006. http://www.lrc.usuhs.mil/dissertations/pdf/Martin2006.pdf.

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Ishizuka, Edson Kiyotaka. "Modulação da função de macrófagos pela nattectina: uma lectina tipo C do veneno de Thalassophryne nattereri." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/42/42133/tde-26012012-093519/.

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A Nattectina é uma toxina isolada do veneno de Thalassophryne nattereri que possui homologia com lectinas tipo C. Este estudo consistiu em avaliar a ação da Nattectina sobre as funções de macrófagos e a influência de citocinas Th1/Th2 nessa ativação. Nossos resultados mostram que a Nattectina induziu o aumento da expressão de moléculas coestimuladoras dependente da sinalização MAPK p38 e PI3K em macrófagos derivados da medula óssea, e também um aumento na capacidade endocítica e expressão de MHC de classe II dependentes da sinalização ERK1/2 e da ligação da Nattectina ao carboidrato. Verificam
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Spearman, Catherine Wendy Nest. "The effect of two novel C-type lectins, Ba100 and Ba25, isolated from the venom of the puff adder, Bitis arietans on T lymphocyte proliferative responses." Doctoral thesis, University of Cape Town, 2008. http://hdl.handle.net/11427/3469.

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Books on the topic "C-lectins"

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Yamasaki, Sho, ed. C-Type Lectins in Immune Homeostasis. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-62237-4.

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Yamasaki, Sho, ed. C-Type Lectin Receptors in Immunity. Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56015-9.

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C, Lee Y., and Lee Reiko T, eds. Recognition of carbohydrates in biological systems: Edited by Yuan C. Lee, Reiko T. Lee. Academic Press, 2003.

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Yamasaki, Sho. C-Type Lectins in Immune Homeostasis. Springer International Publishing AG, 2021.

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Yamasaki, Sho. C-Type Lectins in Immune Homeostasis. Springer International Publishing AG, 2020.

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Cell Adhesion Molecules: C-Type Lectins, Cadherins, Igsf, Integrins, Siglec, Selectins, Collagen, Calreticulin, Fibronectin, Versican. Books LLC, 2010.

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Yamasaki, Sho. C-Type Lectin Receptors in Immunity. Springer, 2018.

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Yamasaki, Sho. C-Type Lectin Receptors in Immunity. Springer Japan, 2016.

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Book chapters on the topic "C-lectins"

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Johannssen, Timo, Julia Hütter, Stephanie Zimmermann, and Bernd Lepenies. "C-Type Lectins." In Glycoscience: Biology and Medicine. Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_138-1.

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Johannssen, Timo, Julia Hütter, Stephanie Zimmermann, and Bernd Lepenies. "C-Type Lectins." In Glycoscience: Biology and Medicine. Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_138.

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Gupta, Anita, and G. S. Gupta. "C-Type Lectins Family." In Animal Lectins: Form, Function and Clinical Applications. Springer Vienna, 2012. http://dx.doi.org/10.1007/978-3-7091-1065-2_22.

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Clemetson, Kenneth J. "Reptile Venom C-Type Lectins." In Handbook of Venoms and Toxins of Reptiles, 2nd ed. CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204-21.

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Gupta, G. S. "Emerging Groups of C-Type Lectins." In Animal Lectins: Form, Function and Clinical Applications. Springer Vienna, 2012. http://dx.doi.org/10.1007/978-3-7091-1065-2_40.

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Foster, Amy J., Jessie H. Bird, Mattie S. M. Timmer, and Bridget L. Stocker. "The Ligands of C-Type Lectins." In C-Type Lectin Receptors in Immunity. Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56015-9_13.

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Zhu, Yibin, Xi Yu, and Gong Cheng. "Insect C-Type Lectins in Microbial Infections." In Advances in Experimental Medicine and Biology. Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1580-4_5.

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Clemetson, Kenneth J. "Snaclecs (Snake C-Type Lectins) that Activate Platelets." In Toxins and Hemostasis. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9295-3_35.

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Raymond, Benjamin B. A., Olivier Neyrolles, and Yoann Rombouts. "C-type Lectins in Immunity to Lung Pathogens." In Current Topics in Microbiology and Immunology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/82_2020_197.

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Cambi, Alessandra, and Carl G. Figdor. "C-Type Lectins: Multifaceted Receptors in Phagocyte Biology." In Phagocyte-Pathogen Interactions. ASM Press, 2014. http://dx.doi.org/10.1128/9781555816650.ch7.

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Conference papers on the topic "C-lectins"

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Jiang, Yan, Yong Pan, Patrea R. Rhea, Richard Lee, Zhimin Lu, and Peiying Yang. "Abstract 4845: Fraxini and mistletoe lectins inhibit the proliferation of hepatocellular carcinoma by promoting proteasomal degradation of c-Myc." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4845.

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Gonzatto, Vitor, Maria Eduarda Bezerra Milhomem, Ana Carolina Lima Delfino, Kátia Bonfim Leite de Moura Sérvulo, and Lidiane Pereira de Albuquerque. "INVESTIGAÇÃO DA PRESENÇA DE LECTINAS EM PREPARAÇÕES DE FOLHAS DE Anacardium occidentale L. E Syzigium cumini (L.) SKEELS." In I Congresso Brasileiro de Biotecnologia On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/795.

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Introdução: Lectinas são glicoproteínas que reconhecem glicoconjugados de superfícies celulares, possibilitando diversas aplicações biotecnológicas. Objetivo: Investigar a presença de lectinas em folhas de A. occidentale e S. cumini Material e métodos: A farinha das folhas secas de S. cumini e A.occidentale foram homogeneizadas em NaCl 0,15 M. Após filtração e centrifugação, o sobrenadante correspondeu ao extrato. As proteínas presentes no extrato foram precipitadas com (NH4)2SO4 obtendo-se a fração proteica F0-60% (após centrifugação/dialise). As preparações foram avaliadas quanto à concentra
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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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Storjord, Elin, Bård Ove Karlsen, and Ole-Lars Brekke. "04147 C-type lectin 10A as a potential biomarker in acute intermittent porphyria." In Abstracts of the International Conference of Porphyrins and Porphyrias, Pamplona, Spain, 21–25 September 2024. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/bmjgast-2024-icpp.29.

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Klapa, Sebastian, Anja Kerstein, Andreas Koch, et al. "SAT0021 ELEVATED NUMBERS OF C-TYPE LECTIN CD161 POSITIVE PR3-SPECIFIC T-CELLS IN GPA." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6771.

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Ameen, K., M. Stoff, S. Pavasutthipaisit, et al. "C-type lectin domain family 12 member A deficiency enhances antiviral responses during neurotropic virus infection." In 66. Jahrestagung der Fachgruppe Pathologie der Deutschen Veterinärmedizinischen Gesellschaft. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0043-1770889.

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Wang, Xian-Wei. "Collaboration between a soluble C-type lectin and calreticulin facilitates white spot syndrome virus infection in shrimp." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.112494.

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Kennelley, Gabrielle, Eric Yuan, Mohammad Shatat, et al. "Abstract 1831: Mistletoe lectin induces apoptosis in MYC-driven cancers through post-translational downregulation of c-MYC protein." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1831.

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Okada, Tomoko, and Norihiko Minoura. "Fluorescence emission and polarization analyses for evaluating binding of ruthenium metalloglycocluster to lectin and tetanus toxin c-fragment." In BiOS, edited by Samuel Achilefu and Ramesh Raghavachari. SPIE, 2010. http://dx.doi.org/10.1117/12.841792.

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Naylor, Amy, Corinna Wehmeyer, Adam Croft, et al. "04.08 Members of the type 14 c-type lectin family protect from inflammatory arthritis but differentially regulate bone erosions." In 37th European Workshop for Rheumatology Research 2–4 March 2017 Athens, Greece. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2016-211051.8.

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