Relevant bibliographies by topics / Antibody recognition

Academic literature on the topic 'Antibody recognition'

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Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "Antibody recognition"

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Janin, J., J. Cherfils, and S. Duquerroy. "Simulating antigen-antibody recognition." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (August 21, 1993): c148. http://dx.doi.org/10.1107/s0108767378095793.

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MacRaild, Christopher A., Jack S. Richards, Robin F. Anders, and Raymond S. Norton. "Antibody Recognition of Disordered Antigens." Structure 24, no. 1 (January 2016): 148–57. http://dx.doi.org/10.1016/j.str.2015.10.028.

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Haji-Ghassemi, Omid, Ryan J. Blackler, N. Martin Young, and Stephen V. Evans. "Antibody recognition of carbohydrate epitopes." Glycobiology 25, no. 9 (June 1, 2015): 920–52. http://dx.doi.org/10.1093/glycob/cwv037.

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Zhou, T., D. H. Hamer, W. A. Hendrickson, Q. J. Sattentau, and P. D. Kwong. "Interfacial metal and antibody recognition." Proceedings of the National Academy of Sciences 102, no. 41 (September 29, 2005): 14575–80. http://dx.doi.org/10.1073/pnas.0507267102.

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Nauchitel, Vladimir V., and Rajmund L. Somorjai. "Antigen-antibody recognition. Model calculations." Biophysical Chemistry 51, no. 2-3 (August 1994): 337–47. http://dx.doi.org/10.1016/0301-4622(94)00054-9.

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Nandakumar, Kutty Selva. "Pathogenic antibody recognition of cartilage." Cell and Tissue Research 339, no. 1 (June 9, 2009): 213–20. http://dx.doi.org/10.1007/s00441-009-0816-8.

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Smith, Thomas J. "Introduction: Antibody recognition of viruses." Seminars in Virology 6, no. 4 (August 1995): 217–18. http://dx.doi.org/10.1006/smvy.1995.0026.

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Thornthwaite, Jerry T., Emily C. McDuffee, Robert B. Harris, Julie R. Secor McVoy, and I. W. Lane. "The cancer recognition (CARE) antibody test." Cancer Letters 216, no. 2 (December 2004): 227–41. http://dx.doi.org/10.1016/s0304-3835(03)00161-7.

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Wu, Nicholas C., and Ian A. Wilson. "Influenza Hemagglutinin Structures and Antibody Recognition." Cold Spring Harbor Perspectives in Medicine 10, no. 8 (December 23, 2019): a038778. http://dx.doi.org/10.1101/cshperspect.a038778.

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KOBAYASHI, Norihiro, and Junichi GOTO. "Antibody Engineering for Advanced Molecular Recognition." YAKUGAKU ZASSHI 127, no. 1 (January 1, 2007): 41–42. http://dx.doi.org/10.1248/yakushi.127.41.

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Dissertations / Theses on the topic "Antibody recognition"

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Bristow, Richard G. W. "Antibody recognition of HIV-1 glycoproteins." Thesis, Open University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315370.

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Davies, Julian. "Antibody VH domains as small recognition units." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263483.

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Robakiewicz, Stefania. "Minimal structural glyco-epitope for antibody recognition." Thesis, Lille 1, 2020. http://www.theses.fr/2020LIL1S101.

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L'importance biologique de la glycosylation pour la santé et la maladie est largement reconnue. Les structures tronquées à terminaison mannose consistant en 1 à 3 résidus de mannose, deux N-acétylglucosamines et un nombre variable de fragments fucose sont appelées paucimannose. Les N-glycanes paucimannosidiques sont abondamment exprimés dans les plantes et les invertébrés. Cependant, chez les vertébrés, leur présence est limitée à certaines conditions pathophysiologiques, telles que le cancer, les troubles immunitaires, les infections et l'inflammation, et chez les individus en bonne santé, ils ne sont détectables qu'en quantités infimes. Il a été démontré que le Mannitou, un anticorps monoclonal murin, reconnaît spécifiquement les glycoépitopes de paucimannose.Une tentative de caractérisation de la structure de Mannitou IgM a été faite en appliquant des techniques de modélisation d'homologie, de microscopie cryoélectronique et de cristallisation. L'anticorps complet de Mannitou a été généré en utilisant la technologie des hybridomes. Le Fab recombinant de Mannitou a été exprimé avec succès de manière transitoire dans des cellules HEK293T. La spécificité de liaison de Mannitou envers différents N-glycanes de paucimannose ont été élucidées par une combinaison de méthodes expérimentales. Le criblage par microréseau a révélé que le glyco-épitope minimal était Man2GlcNAc2. À son tour, Man3GlcNAc2 a manifesté l'une des interactions les plus fortes avec l'anticorps Mannitou. Des études de reconnaissance moléculaire, utilisant des mesures de résonance plasmonique de surface et une calorimétrie de titrage isotherme, ont établi une affinité de liaison micromolaire de l'anticorps Mannitou envers le glycane Man3GlcNAc2. La cartographie de l'épitope de liaison par résonance magnétique nucléaire de transfert de saturation a démontré que Manα1-3 est le principal résidu impliqué dans la reconnaissance des anticorps de Mannitou. La régulation positive des N-glycanes paucimannosidiques dans des conditions physiopathologiques fait de l'anticorps Mannitou un outil diagnostique et thérapeutique prometteur.Pour déterminer la structure minimale des glycanes requise pour mimer l'activité antigénique du polysaccharide MenX natif, des études de résonance plasmonique de surface ont été réalisées. Les expériences ont consisté à étudier les interactions de liaison entre un anticorps anti-MenX et des oligosaccharides capsulaires du sérogroupe X de Neisseria meningitides de différentes longueurs. Les résultats suggèrent que la portion minimale de saccharide capable d'assurer une protection contre les infections à MenX pourrait être DP5, ce qui en fait un candidat prometteur pour le développement de vaccins
The biological importance of glycosylation in health and disease is broadly acknowledged. The truncated, mannose-terminating structures consisting of 1–3 mannose residues, two N-acetylglucosamines, and a variable number of fucose moieties are termed paucimannose. Paucimannosidic N-glycans are abundantly expressed in plants and invertebrates. However, in vertebrates their presence is restricted to some pathophysiological conditions, such as cancer, immune disorders, infections, and inflammation, and in healthy individuals, they are detectable only in trace amounts. Mannitou, a murine monoclonal antibody, has been demonstrated to specifically recognise paucimannose glycoepitopes. An attempt to characterise Mannitou IgM structure was made by applying homology modelling, cryo-electron microscopy, and crystallisation techniques. Full-length Mannitou antibody has been generated using hybridoma technology. Recombinant Mannitou Fab has been successfully transiently expressed in HEK293T cells. The binding specificity of Mannitou towards different paucimannose N-glycans have been unravelled by a combination of experimental methods. The microarray screening revealed the minimal glyco-epitope to be Man2GlcNAc2. In turn, Man3GlcNAc2 manifested one of the strongest interactions with Mannitou antibody. Molecular recognition studies, employing surface plasmon resonance measurements and isothermal titration calorimetry, established a micromolar binding affinity of Manniotu antibody towards Man3GlcNAc2 glycan (Kd = ~50 μM). The mapping of the binding epitope by saturation transfer difference nuclear magnetic resonance demonstrated Manα1-3 as the main residue involved in Mannitou antibody recognition. The upregulation of paucimannosidic N-glycans in pathophysiological conditions makes Mannitou antibody a promising diagnostic and therapeutic tool.For determining the minimal carbohydrate structure required for mimicking the antigenic activity of the native MenX polysaccharide, surface plasmon resonance studies were performed. The experiments involved studying the binding interactions between an anti-MenX antibody and Neisseria meningitides serogroup X capsular oligosaccharides of different length. The results suggest that the minimal saccharide portion capable of ensuring protection against MenX infections may be DP5, making it a promising candidate for vaccine development
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Scherer, Erin M. "Antibody recognition of a protein epitope close to a membrane : a novel solution." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510216.

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Webster, Duncan F. "Characterisation of human hepatic cytochrome P450 : comparison of metabolic markers and antibody recognition." Thesis, University of Aberdeen, 1997. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU530008.

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A cDNA library was produced in lambdagt11 from an induced human liver. Twenty-one clones were isolated. All clones were identified by two of the four antibodies used in the screening process. The phage insert was recovered by PCR with two specific primers. The PCR product was ligated into M13 vectors and sequenced. The DNA was a CYP2A sequence with highest identity to CYP2A6 but contained a point deletion mutation. Coumarin metabolism was measured in microsomal preparations of fifteen livers and was inhibited by three of the antibodies used in screening. RP1 monoclonal gave partial inhibition (60%) at ratios of 100:1. Two other antibodies IIB1 polyclonal and RP3 (monoclonal) were highly inhibitory at low ratios. IIB1 gave a 90% inhibition at 20:1 ratio, RP3 was 95% inhibitory at 6:1 ratio. O-dealkylation of alkoxyresorufins was determined for sixteen livers. BROD activity was partially inhibited by IIB1 polyclonal (60% at a 20:1 ratio). This supports the possibility that BROD is not a marker for CYP2B activity in humans and that BROD may be primarily metabolised by CYP4A. The results were compared with fifty-seven separate sets consisting of metabolism and antibody immunoquantification data. There were strong correlations between BROD activity and several CYP3A marker activities and protein levels identified by a polyclonal antibody that recognises P4503A. The metabolism of indomethacin was measured for fifteen livers. One of the metabolites of indomethacin, desmethylindomethacin, was produced by all livers. The metabolism could not be inhibited with antibodies as they interfered with the reaction in a non-specific manner. Comparisons with other metabolism in the same livers showed that indomethacin is probably a CYP3A substrate. The indomethacin method was modified ibuprofen and data was collected for fourteen livers. Two metabolites, I and II, were seen for each liver in 1:2 ratio respectively. These both correlated highly with tolbutamide metabolism.
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Raina, Monika. "Development of an impedimetric biosensor using a non-antibody based biological recognition molecule." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/6844/.

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The molecular recognition layer generally immobilised on the active interface of a biosensor is one of the key factors in governing the biosensor’s performance, and in particular its sensitivity and selectivity. The aim of this thesis was to investigate a novel non-immunoglobulin-based recognition molecule as the capture molecule for electrochemical biosensors with the aim to improve sensitivity and specificity of label-free biosensing. To understand the characteristics of the biomolecular layer of a biosensor formed from the non-immunoglobulin-based recognition molecule, the Adhiron scaffold developed at the University of Leeds was used as the model system. The Adhiron scaffold consists of one α-helix, four β-sheets, and three variable regions. The three variable regions comprise two surface-exposed loops and the N-terminus of the protein. Adhiron-based binders against a well-characterised antibody, the anti-myc tag antibody, were selected using phage-display and used as a model system for this study. The phage-display library was constructed by inserting randomised peptides into the three variable regions of the Adhiron scaffold. The best performing binder, selected from the ten Adhiron myc binders panned from a phage display screen against polyclonal anti-myc tag antibodies, myc binder 2, was chosen as the biological recognition molecules for the development of an electrochemical impedimetric biosensor. Cloning of the Adhiron binders in pET-11(a) expression vector, optimisation of expression and purification of the binders, was carried out and the binders were obtained in soluble form. Adhiron myc binder 2, which showed the best binding against monoclonal anti-myc tag antibodies, showed a high thermal stability of 85º C, with well-defined α-helical and β-sheet structures. This binder was thoroughly characterised further before being used as a recognition molecule of an electrochemical biosensor. An electrochemical Adhiron-based myc binder 2 sensor was fabricated to detect monoclonal anti-myc tag antibodies over a range of concentrations. The Adhiron myc binder 2 based EIS biosensor comprised a highly sensitive insulating layer formed by a self-assembled monolayer of carboxylic acid terminated alkylthiol-PEG onto which Adhiron myc binder 2 was grafted. The sensing mechanism was based on the change in phase of the electrochemical impedance measured at 0.1 Hz observed upon binding of monoclonal anti-myc tag antibodies onto the sensor. Monoclonal anti-myc tag antibodies were detected down to a concentration of less than 100 pM, over a range from 0.1–200 nM anti-myc tag antibodies. These findings demonstrated for the first time the successful use of Adhiron-based antibodymimetics as recognition molecules in label-free biosensors. To improve the sensitivity of the Adhiron-based electrochemical biosensor, and potentially to modulate the sensitivity in situ, the performance of the sensor at different electrochemical DC-biases was investigated. The sensitivity of the sensor was observed to increase with increasing DC bias applied to the sensor surface. This sensitivity modulation was demonstrated to be reversible, therefore opening up a range of opportunities for future label-free biosensor architectures.
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Topping, Katherine P. "Structural studies on serotype-specific opsonic antibody recognition of protective streptococcal M protein epitopes." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294877.

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Koh, W. W. L. "Characterisation of subtype C HIV-I envelope glycoproteins and their recognition by llama antibody fragments." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18999/.

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Subtype C HIV-1 is currently responsible for the majority of new infections in the world, particularly in parts of Africa where the adult prevalence rate is as high as 15%. In the absence of a viable vaccine in the near future, the study of new neutralising antibodies that can inhibit virus entry is urgently needed. To understand the subtype C HIV-1 envelopes, the env gene was cloned directly from 15 patient plasma samples obtained from a few countries in Africa and in the UK, and 18 replication-competent chimeric viruses were created. These envelopes were then characterised and compared with other envelopes in standard reference panels. We then exploited the unique properties of llama heavy-chain antibodies to create antibody fragments (VHH) that can recognise HIV-1 envelopes and prevent infection. Four VHH that recognise a conformation dependent epitope on gp41 were isolated from a llama that was immunised with recombinant gp140 derived from a subtype B’/C isolate after panning of the phage libraries on recombinant gp41. These VHH were more potent in neutralising subtype C isolates than subtype B isolates. Based on the success of an earlier study on VHH that recognise an epitope overlapping the CD4 binding site on gp120, a novel strategy was used to isolate variants of the VHH to create a family-specific VHH library. Thirty-one new VHH were characterised and grouped according to their neutralisation breadth against 3 subtype C viruses. The neutralisation breadth of the VHH correlated with its dissociation rate with gp120, and was found to be dependent on 3 amino acid residues in the third complementarity determining region of the VHH. These VHH may have further use in applications such as HIV-1 microbicides development and immunogen design through reverse immunology.
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Naqid, Ibrahim. "Investigation of antibody-based immune recognition of infections with Salmonella enterica serovars Typhimurium and Enteritidis." Thesis, University of Nottingham, 2016. http://eprints.nottingham.ac.uk/33141/.

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Salmonellosis causes significant economic losses to the pig and poultry industries. Pigs and chickens are also a significant source of Salmonella for humans, usually transmitted through the consumption of Salmonella contaminated chicken and pork products. Predominantly, Salmonella enterica serovar Typhimurium and Enteritidis remain a global health problem. Probiotics and prebiotics have been previously used as alternatives to antibiotic treatments in the protection against enteropathogens including S. Typhimurium. Here, we determined the effects of probiotic, prebiotic and synbiotic diets on humoral immune responses to oral S. Typhimurium challenge of pigs. The inclusion of probiotic Lactobacillus plantarum in the diet of piglets enhanced serum IgG, and IgM (p <0.001), and IgA (p <0.01) responses to S. Typhimurium infection. Similarly, inclusion of prebiotic lactulose in the diet increased serum levels of IgG and IgM (p <0.01) responses to pathogen, but not IgA levels. Inclusion of both feed additives as a synbiotic diet also significantly increased the level of IgG responses (p <0.05) to S. Typhimurium, but no differences were seen in the levels of IgM and IgA responses. However a significant interaction of the pre and probiotics was observed when considering the immune responses to S. Typhimurium (IgM P=0.004; IgG and IgA, P<0.001 for interaction). These data support the use of L. plantarum or lactulose as strategies to contribute to the protection of weaned piglets from zoonotic bacterial pathogens, but caution must be taken when combining dietary supplements as combinations can interact. The mapping of antibody-based immune responses to Salmonella enterica infections for identifying epitopes/mimotopes has an important role in the development of both novel serological diagnostic assays and vaccines. Serological assays often underpin disease surveillance programs and are also required for the differentation of infected from vaccinated animals (DIVA) to allow the full implementation of vaccines alongside such surveillance. Here, panning of phage display peptide libraries coupled with Next Generation Sequencing was applied to the mapping of B-cell responses to Salmonella infections in both pigs and chickens. IgG from 12 pigs infected with S. Typhimurium were probed in parallel and compared to the equivalent IgG from the same pigs prior to infection. Seventy-seven peptide were enriched against IgG from multiple infected pigs, thirty-one peptides were synthesised and tested in ELISA and twelve peptides were highly discriminatory for pure IgG from infected pigs (P<0.05). Similarly, IgY from chickens infected with different Salmonella serovars were probed in order to identify mimotopes specific for S. Enteritidis infection. Twenty-nine peptides were enriched against IgY from multiple infected chickens, and then synthesised and tested in ELISA assays, tweleve of them were highly discriminatory for IgY following S. Enteritidis infections (p<0.05). The technology was also used to identify multiple peptides that were specifically bound by IgY from Salmonella infected chickens compared to a live attenuated vaccine and a killed vaccine. Twenty-five and thirty-six peptides for attenuated and inactivated vaccines, respectively, were identified as being specifically enriched in multiple infected chickens. Twenty and twenty-six of the most discriminatory peptides for live and killed vaccines, respectively, were applied in multi-peptide diagnostic assays that diagnosed infection with 100% sensitivity and specificity. The results demostrate that the identified peptides can be used to design serological DIVA tests with established inactivated and attenuated vaccines. Overall, the described next generation phage display (NGPD) technology repeatedly identified panels of epitopes/mimotopes recognised by multiple animals with a particular infection, providing an extremely efficient method to map host polyclonal antibody responses to S.Typhimurium and S. Enteritidis infections.
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Grinstead, Jeffrey Scott. "Structural immunology of humoral and cellular recognition of a MUC1 breast cancer antigen /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8180.

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Books on the topic "Antibody recognition"

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1929-, Laver William Graeme, Air Gillian, and Cold Spring Harbor Laboratory, eds. Immune recognition of protein antigens. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1985.

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James, McCluskey, ed. Antigen processing and recognition. Boca Raton: CRC Press, 1991.

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Salama, Alan D. The patient with vasculitis. Edited by Giuseppe Remuzzi. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0159_update_001.

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Primary systemic vasculitis frequently leads to renal involvement and is responsible for significant numbers of patients progressing to end-stage renal disease. Frequently this is due to small vessel vasculitis, in association with antineutrophil cytoplasm antibody, which requires prompt recognition and timely therapeutic intervention to optimize renal and patient outcomes. Other organ systems are often affected. Relapses occur in about 50%.Less commonly medium or larger vessel vasculitis may involve the kidneys and through ischaemia lead to impaired renal function and renovascular hypertension, as in Takayasu’s or Kawasaki disease, and polyarteritis nodosa (PAN).
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Beattie, R. Mark, Anil Dhawan, and John W.L. Puntis. Coeliac disease. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198569862.003.0033.

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Who to investigate 234How to investigate 236Diagnosis 238Treatment 240Follow-up and support 242Coeliac disease is an immune-mediated enteropathy caused by a permanent sensitivity to gluten which is present in wheat, barley, and rye. It occurs in genetically susceptible children and adults. The classical presentation is with chronic diarrhoea, abdominal distension, and failure to thrive. The widespread availability of antibody screening has considerably changed the clinical spectrum of cases seen. The testing of children with less classical symptoms and screening of children at high risk has brought increasing recognition of the varied presentation and increased prevalence of this now very common condition....
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Martagon-Villamil, Jose, and Daniel J. Skiest. Clinical Syndromes and Differential Diagnosis in the HIV-Infected Patient. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190493097.003.0011.

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Acute HIV infection is often missed but should be recognized. Most chronically infected individuals are asymptomatic. However, some patients with chronic HIV infection may present with certain clinical and laboratory abnormalities prior to the diagnosis of an opportunistic infection. HIV wasting syndrome is infrequently diagnosed in the era of antiretroviral therapy (ART). Recognition of HIV wasting is important because it carries adverse prognostic implications. Management includes a multifaceted approach, including ART, lifestyle and nutritional support, appetite stimulation, and possibly hormonal agents. The newer antigen–antibody test can detect new HIV infection as early as 15 days after exposure. Screening is important because most chronic HIV infection is asymptomatic.
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Adler, M. Properties and potential of protein–DNA conjugates for analytic applications. Edited by A. V. Narlikar and Y. Y. Fu. Oxford University Press, 2017. http://dx.doi.org/10.1093/oxfordhb/9780199533053.013.25.

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This article examines the properties of protein-DNA conjugates and their potential for analytic applications. It begins with a discussion of DNA as a rigid construction tool for protein networks, reducing its functionality to the molecular equivalent of a steel bar in 'large-scale' architecture. It then describes DNA functionality in protein-DNA conjugates, like specific recognition of nucleotide sequences or its unique use as an amplification template. It also considers a range of applications for protein-DNA conjugates, including the use of artificial DNA-protein nanostructures as supramolecular building blocks and DNA-antibody conjugates for ultrasensitive antigen detection. Finally, it evaluates DNA-directed immobilization of protein-DNA adaptor molecules for flexible protein arrays. It shows that protein-DNA conjugates can be used as analytical targets for challenging and calibrating the properties of high-resolution atomic force microscopy, as well as analytical reagents for ultrasensitive target detection in immuno-PCR and related techniques.
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Cohen, Mary Ann, Harold Goforth, Joseph Lux, Sharon Batista, Sami Khalife, Kelly Cozza, and Jocelyn Soffer. Handbook of AIDS Psychiatry. Oxford University Press, 2010. http://dx.doi.org/10.1093/oso/9780195372571.001.0001.

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The Handbook of AIDS Psychiatry is a practical guide for AIDS psychiatrists and other mental health professionals as well as for other clinicians who work with persons with HIV and AIDS and a companion book to the Comprehensive Textbook of AIDS Psychiatry (Cohen and Gorman, 2008). The Handbook provides insights into the dynamics of adherence to risk reduction and medical care in persons with HIV and AIDS as well as strategies to improve adherence using a biopsychosocial approach. Psychiatric disorders can accelerate the spread of the virus by creating barriers to risk reduction. Risky sexual behaviors and sharing of needles in intravenous drug users account for the majority of new cases each year. Delirium, dementia, depression, substance dependence, PTSD, and other psychiatric disorders complicate the course and add considerably to the pain and suffering of persons with AIDS. HIV infection and AIDS also are risk factors for suicide, and the rate of suicide has been shown to be higher in persons with AIDS. Psychiatric care can help prevent HIV transmission through recognition and treatment of substance-related disorders, dementia, and mood disorders such as mania. Comprehensive, coordinated care by a multidisciplinary AIDS team, including AIDS psychiatrists, can provide a biopsychosocial approach that is supportive to patients, families, and clinicians. Psychiatric interventions are valuable in every phase of infection, from identification of risk behaviors to anticipation about HIV testing; from exposure and initial infection to confirmation with a positive HIV antibody test; from entry into systems of care to managing complex antiretroviral regimen; from healthy seropositive to onset of first AIDS-related illness; from late stage AIDS to end-stage AIDS and death. There is no comprehensive handbook of AIDS psychiatry to guide clinicians in providing much needed care. The Handbook of AIDS Psychiatry is a practical pocket guide that provides protocols for the recognition and treatment of the psychiatric disorders most prevalent in persons with AIDS and most relevant for primary physicians, infectious disease specialists, and other caregivers because of their impact on health, adherence, behavior, and quality of life.
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Book chapters on the topic "Antibody recognition"

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Hopkins, Neal A. E. "Antibody Engineering for Biosensor Applications." In Recognition Receptors in Biosensors, 451–529. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0919-0_12.

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Zhao, Jun, Ruth Nussinov, and Buyong Ma. "The Allosteric in Antibody-Antigen Recognition." In Methods in Molecular Biology, 175–83. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-1154-8_11.

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Ratner, Anna, and William R. Clark. "Derivatization of Cells with Antibody." In Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods, 487. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6814-4_51.

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Ratner, Anna, and William R. Clark. "Stimulation of CTL on Antibody-Coated Plates." In Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods, 497. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6814-4_56.

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Van Regenmortel, Marc H. V. "Specificity, Polyspecificity and Heterospecificity of Antibody-Antigen Recognition." In HIV/AIDS: Immunochemistry, Reductionism and Vaccine Design, 39–56. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-32459-9_4.

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Gildersleeve, Jeffrey C. "Insights into Antibody-Carbohydrate Recognition from Neoglycoprotein Microarrays." In ACS Symposium Series, 23–37. Washington, DC: American Chemical Society, 2020. http://dx.doi.org/10.1021/bk-2020-1346.ch002.

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Zajonc, Dirk M. "Antibody Recognition of Immunodominant Vaccinia Virus Envelope Proteins." In Subcellular Biochemistry, 103–26. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46503-6_4.

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Greenspan, N. S. "Affinity, Complementarity, Cooperativity, and Specificity in Antibody Recognition." In Current Topics in Microbiology and Immunology, 65–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-05783-4_5.

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Agostino, Mark, William Farrugia, Mauro S. Sandrin, Andrew M. Scott, Elizabeth Yuriev, and Paul A. Ramsland. "Structural Glycobiology of Antibody Recognition in Xenotransplantation and Cancer Immunotherapy." In Anticarbohydrate Antibodies, 203–28. Vienna: Springer Vienna, 2011. http://dx.doi.org/10.1007/978-3-7091-0870-3_9.

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Dingjan, Tamir, Mark Agostino, Paul A. Ramsland, and Elizabeth Yuriev. "Antibody-Carbohydrate Recognition from Docked Ensembles Using the AutoMap Procedure." In Methods in Molecular Biology, 41–55. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2874-3_4.

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Conference papers on the topic "Antibody recognition"

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Lord, S. T. "DIRECTED MUTAGENESIS OF HUMAN FIBRINOGEN: Aα CHAIN SUBSTITUTIONS THAT ALTER THROMBIN CLEAVAGE AND ANTIBODY RECOGNITION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642887.

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The initial event in fibrin clot formation is the thrombin catalized cleavage of the Aa chain of fibrinogen between Argl6 and Glyl7, releasing fibrinopeptide A. Previous data indicate that most of the information required for thrombin recognition and cleavage of the Aa chain lies within the amino terminal 51 residue CNBr fragment. In order to use protein engineering techniques to study the interaction of thrombin with the Aa chain, we have constructed a plasmid expression vector which encodes a tripartite protein consisting of amino acids 1-50 of the Aa chain of human fibrinogen followed by 60 amino acids of chicken collagen, and the beta-galactosidase protein from Escherichia coli. The codons for an initiator methionine and amino acids 1-50 were assembled from 7 oligonucleotides. Protein blot analysis of bacterial lysates of cells induced to synthesize this tribrid protein show a single band (MW = 125,000) crossreactive with a monoclonal antibody, Y-18, which recognizes the Aa chain of fibrinogen but not the products of thrombin cleavage. When these lysates are incubated with thrombin, fibrinopeptide A is released as demonstrated both by protein blot analysis and radioimmunoassay. By including one heterogeneous oligonucleotide in the assembly process, we have constructed plasmids which encode specific amino acid substitutions within residues 1-23. One of these substitutions, Glyl4 to val, significantly alters both cleavage by thrombin and recognition by Y-18. Substitution of ilu for Arg23 alters neither thrombin cleavage nor monoclonal recognition while substitution of leu for Argl6 alters thrombin cleavage, but not recognition by Y-18.
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Hsi-Kai Wang, Cheng-Han Tsai, Chung-Tao Tang, Pi-Chun Li, Jiun-Shyang Leou, Yin-Liang Tang, Hsyue-Jen Hsieh, Han-Chung Wu, and Chao-Min Cheng. "Monitoring the disease activity via the antibody-antigen recognition in paper." In 2013 8th IEEE International Conference on Nano/Micro Engineered and Molecular Systems (NEMS). IEEE, 2013. http://dx.doi.org/10.1109/nems.2013.6559721.

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Tomaslni, B. R., and D. F. Mosher. "PREFERENTIAL RECOGNITION OF VITRONECTIN (S-PR0TEIN) BY A MONOCLONAL ANTIBODY UPON INTERACTION WITH THROMBIN, ANTITHROMBIN AND GLYCOSAMINOGLYCANS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643634.

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V1tronect1n/S-Prote1n (VN/SP) is a glycoprotein present at a concentration of 200-400 ug/ml 1n plasma and serum. It has been shown to promote cel 1-substratum adhesion and to act as an Inhibitor of the membrane attack complex of complement and of the inactivation of thrombin by antithrombin III in the presence of low levels of heparin. We have previously shown that VN/SP binds more avidly to heparln-agarose and to a monoclonal antibody (MaVN/SP)-Sepharose column when present 1n serum rather than 1n plasma. In order to examine the possibility of a serum-induced conformational change, we utilized, 1n this study, an Indirect enzyme-linked Immunosorbent system to test for the exposure of new antigenic determinants. When MaVN/SP was Incubated with plasma or serum, recognition of VN/SP 1n serum was approximately 50 fold greater than recognition of VN/SP in plasma. Since VN/SP has been shown to Interact strongly with the thromb1n-ant1thrombin complex, we examined the antigenicity of VN/SP when Incubated with thrombin and antithrombin 1n the presence and absence of heparin. Incubation of VN/SP with heparin promoted a 2.5-fold Increase 1n recognition by MaVN/SP. When MaVN/SP was Incubated with thromb1n-ant1thrombin but not thrombin or antithrombin alone, recognition was Increased by 7-fold 1n the absence of heparin and by 32-fold 1n the presence of heparin. This differential recognition of VN/SP was not observed with a second monoclonal antibody raised originally against S-Prote1n. Treatment of VN/SP with various glycosaminoglycans and polysaccharides demonstrated the following relative potencies for Induction of the partial antigenic change: dextran sulfate>fucoidan>heparin> dermatan suIfate>hyaluronic acid. No effect was detected upon Incubation of VN/SP with keratan sulfate, heparan sulfate or chondroltln sulfate. These data suggest a conformational change Induced by thrombin-antlthrombin which may allow VN/SP to Interact more avidly with other molecules such as heparin. The physiological role of this putative conformational change is under investigation.
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Magalhães, André, Sandro Bordeira, Ana Cristina Almeida, Vanessa Fontes, Maria João L. Costa, Luís P. Fonseca, and João Garcia da Fonseca. "Antibody fragment recognition layers for surface plasmon resonance biosensing: a parametric study." In SPIE BiOS: Biomedical Optics, edited by Anita Mahadevan-Jansen, Tuan Vo-Dinh, and Warren S. Grundfest. SPIE, 2009. http://dx.doi.org/10.1117/12.808820.

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Chinh, T. T. Su, D. Handoko Stephanus, Chee-Keong Kwoh, Christian Schonbach, and Xiaoli Li. "A possible mutation that enables H1N1 influenza a virus to escape antibody recognition." In 2010 IEEE International Conference on Bioinformatics and Biomedicine (BIBM 2010). IEEE, 2010. http://dx.doi.org/10.1109/bibm.2010.5706541.

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Uray, Katalin, Regina Tugyi, Orsolya Tőke, and Ferenc Hudecz. "Effect of modification on the antibody recognition and secondary structure of a mucin 2 epitope." In Xth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2007. http://dx.doi.org/10.1135/css200709102.

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White, Mitch, James Head, Grith Sorensen, Uffe Holmskov, Erika Crouch, and Kevan L. Hartshorn. "Monoclonal Antibody Assisted Structure-function Analysis Of The Carbohydrate Recognition Domain Of Surfactant Protein D." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4973.

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Zhang, H. Y., L. Q. Yang, and W. M. Liu. "A laser scanning confocal imaging-surface plasmon resonance system application in real time detection of antibody-antigen interaction." In Seventh International Symposium on Multispectral Image Processing and Pattern Recognition (MIPPR2011), edited by Jianguo Liu, Jinwen Tian, Hongshi Sang, and Jie Ma. SPIE, 2011. http://dx.doi.org/10.1117/12.901521.

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Torres-Almonacid, Jorge, David Medina-Ortiz, Diego Alvarez-Saravia, Julio Aguila-Guerrero, Alvaro Olivera-Nappa, and Marcelo Navarrete. "Pattern recognition on antigen-antibody interactions from protein microarrays based on data mining and bioinformatics analysis." In 2019 38th International Conference of the Chilean Computer Science Society (SCCC). IEEE, 2019. http://dx.doi.org/10.1109/sccc49216.2019.8966421.

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Selwyna, P. G. C., P. R. Loganathan, and K. H. Begam. "Development of electrochemical biosensor for breast cancer detection using gold nanoparticle doped CA 15-3 antibody and antigen interaction." In 2013 International Conference on Signal Processing, Image Processing, and Pattern Recognition (ICSIPR). IEEE, 2013. http://dx.doi.org/10.1109/icsipr.2013.6497963.

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Reports on the topic "Antibody recognition"

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Guntupalli, Rajesh, Eric Olsen, Ludmila Globa, Jacob Bosarge, Timothy Moore, Iryna Sorokulova, and Vitaly Vadyanoy. Specific Recognition and Detection of MRSA Based on Molecular Probes Comprised of Lytic Phage and Antibody. Fort Belvoir, VA: Defense Technical Information Center, March 2011. http://dx.doi.org/10.21236/ada540436.

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