Gotowe bibliografie tematyczne / ChiTn antibody

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Gotowa bibliografia na temat „ChiTn antibody”

Autor: Grafiati

Data publikacji: 5 czerwca 2025

Data aktualizacji: 2 sierpnia 2025

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Artykuły w czasopismach na temat "ChiTn antibody"

Ryan, G. B., W. T. Jones, R. E. Mitchell, and V. Mett. "Polyclonal Antibody Production Against Chito-Oligosaccharides." Food and Agricultural Immunology 13, no. 2 (2001): 127–30. http://dx.doi.org/10.1080/09540100120055600.

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Tokura, Seiichi, Osatoshi Hasegawa, Shin-Ichiro Nishimura, Norio Nishi, and Takehiko Takatori. "Induction of methamphetamine-specific antibody using biodegradable carboxymethyl-chitin." Analytical Biochemistry 161, no. 1 (1987): 117–22. http://dx.doi.org/10.1016/0003-2697(87)90660-9.

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Grabińska, Kariona A., Paula Magnelli, and Phillips W. Robbins. "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length." Eukaryotic Cell 6, no. 2 (2006): 328–36. http://dx.doi.org/10.1128/ec.00203-06.

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ABSTRACT Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is

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Sendid, B., N. Dotan, S. Nseir, et al. "Antibodies against Glucan, Chitin, and Saccharomyces cerevisiae Mannan as New Biomarkers of Candida albicans Infection That Complement Tests Based on C. albicans Mannan." Clinical and Vaccine Immunology 15, no. 12 (2008): 1868–77. http://dx.doi.org/10.1128/cvi.00200-08.

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ABSTRACT Antibodies against Saccharomyces cerevisiae mannan (ASCA) and antibodies against synthetic disaccharide fragments of glucans (ALCA) and chitin (ACCA) are biomarkers of Crohn's disease (CD). We previously showed that Candida albicans infection generates ASCA. Here, we explored ALCA and ACCA as possible biomarkers of invasive C. albicans infection (ICI). ASCA, ALCA, ACCA, and Candida mannan antigen and antibody detection tests were performed on 69 sera obtained sequentially from 18 patients with ICIs proven by blood culture, 59 sera from CD patients, 47 sera from hospitalized subjects c

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Fonseca, Fernanda L., Leonardo Nimrichter, Radames J. B. Cordero, et al. "Role for Chitin and Chitooligomers in the Capsular Architecture of Cryptococcus neoformans." Eukaryotic Cell 8, no. 10 (2009): 1543–53. http://dx.doi.org/10.1128/ec.00142-09.

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ABSTRACT Molecules composed of β-1,4-linked N-acetylglucosamine (GlcNAc) and deacetylated glucosamine units play key roles as surface constituents of the human pathogenic fungus Cryptococcus neoformans. GlcNAc is the monomeric unit of chitin and chitooligomers, which participate in the connection of capsular polysaccharides to the cryptococcal cell wall. In the present study, we evaluated the role of GlcNAc-containing structures in the assembly of the cryptococcal capsule. The in vivo expression of chitooligomers in C. neoformans varied depending on the infected tissue, as inferred from the di

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Ju, Ruibao, Yanjing Lu, Zhiwen Jiang, et al. "A Thermosensitive and Degradable Chitin-Based Hydrogel as a Brucellosis Vaccine Adjuvant." Polymers 16, no. 19 (2024): 2815. http://dx.doi.org/10.3390/polym16192815.

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Brucellosis is a zoonotic infectious disease that has long endangered the development of animal husbandry and human health. Currently, vaccination stands as the most efficacious method for preventing and managing brucellosis. Alum, as the most commonly used adjuvant for the brucellosis vaccine, has obvious disadvantages, such as the formation of granulomas and its non-degradability. Therefore, the aims of this study were to prepare an absorbable, injectable, and biocompatible hydroxypropyl chitin (HPCT) thermosensitive hydrogel and to evaluate its immunization efficacy as an adjuvant for Bruce

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Stefanov, Emily, Nicolas Kin, Brian Dizon, and John Kearney. "Antibodies generated against conserved antigens suppress allergic airway disease (125.13)." Journal of Immunology 188, no. 1_Supplement (2012): 125.13. http://dx.doi.org/10.4049/jimmunol.188.supp.125.13.

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Abstract There has been a sharp rise in allergic asthma and asthma-related deaths in the developed world. The hygiene hypothesis proposes that excessively sanitary conditions early in life result in autoimmune and allergic phenomena because of a failure of the immune system to receive proper microbial stimulation during development. Chitin, a biopolymer of N-acetyl glucosamine (GlcNAc), is produced by many allergen-bearing organisms including: fungi, the exoskeleton of insects, crabs, shrimp and parasitic nematodes. We demonstrate that antibodies generated against chitin and other conserved ba

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Aguilar-Díaz, Hugo, Juan Pedro Laclette, and Julio César Carrero. "Silencing ofEntamoeba histolyticaGlucosamine 6-Phosphate Isomerase by RNA Interference Inhibits the Formation of Cyst-Like Structures." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/758341.

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Encystment is an essential process in the biological cycle of the human parasiteEntamoeba histolytica. In the present study, we evaluated the participation ofE. histolyticaGln6Pi in the formation of amoeba cyst-like structures by RNA interference assay. Amoeba trophozoites transfected with two Gln6Pi siRNAs reduced the expression of the enzyme in 85%, which was confirmed by western blot using an anti-Gln6Pi antibody. TheE. histolyticaGln6Pi knockdown with the mix of both siRNAs resulted in the loss of its capacity to form cyst-like structures (CLSs) and develop a chitin wall under hydrogen per

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Greppi, Chloe. "Cryosectioning and Immunohistochemistry of Peripheral Tissues of Mosquitoes." Cold Spring Harbor Protocols 2023, no. 1 (2022): pdb.prot107914. http://dx.doi.org/10.1101/pdb.prot107914.

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Immunohistochemistry analysis of mosquitoes is complicated by the outer cuticle that prevents reagents from penetrating peripheral tissues. This protocol incorporates a cryosectioning method that provides a higher resolution of the internal architecture of mosquito peripheral sensory tissues and enables the visualization of protein expression. This eliminates the need for enzymatic steps to digest the outer cuticle that encases these tissues. This protocol can also be adapted for other tissues, such as the brain and the legs, as chitin exoskeleton thickness does not affect antibody penetration

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DAVIES, D. R., and S. CHACKO. "ChemInform Abstract: Antibody Structure." ChemInform 24, no. 49 (2010): no. http://dx.doi.org/10.1002/chin.199349321.

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Części książek na temat "ChiTn antibody"

Jain, Dr B. K., Dr Ankita Alice Singh, Dr Kaminee Sahu, and Dr Seema Kohli. "AN OVERVIEW OF CHITOSAN NANOPARTICLES AS DRUG CARRIERS." In Futuristic Trends in Biotechnology Volume 3 Book 22. Iterative International Publishers, Selfypage Developers Pvt Ltd, 2024. http://dx.doi.org/10.58532/v3bkbt22p2ch1.

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Many traditional diseases may have greater potential if new drug delivery methods are developed. Chitosan has been preferred as a drug delivery vehicle due to its beneficial properties such as biodegradability, biocompatibility, non-toxicity, non-immunogenicity, non-carcinogenicity and antibacterial ability. In addition, it has attracted great interest as a new drug delivery method because it is widely used in the transport of protein, gene and antibody drugs, as well as in many ways such as mouth, nose, urine, injection. The second most abundant polysaccharide after cellulose is chitosan, whi

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Tokura, Seiichi, Yoshiaki Miura, Masayoshi Johmen, Norio Nishi, and Shin-Ichiro Nishimura. "Induction of drug specific antibody and the controlled release of drug by 6-O-carboxymethyl-chitin." In Advances in Drug Delivery Systems, 6. Elsevier, 1994. http://dx.doi.org/10.1016/b978-0-444-82027-3.50027-4.

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