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Relevant bibliographies by topics / Protein-Antibody recognition

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Academic literature on the topic 'Protein-Antibody recognition'

Author: Grafiati

Published: 9 March 2023

Last updated: 19 July 2025

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Journal articles on the topic "Protein-Antibody recognition"

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Ferrigno, Paul Ko. "Non-antibody protein-based biosensors." Essays in Biochemistry 60, no. 1 (2016): 19–25. http://dx.doi.org/10.1042/ebc20150003.

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Biosensors that depend on a physical or chemical measurement can be adversely affected by non-specific interactions. For example, a biosensor designed to measure specifically the levels of a rare analyte can give false positive results if there is even a small amount of interaction with a highly abundant but irrelevant molecule. To overcome this limitation, the biosensor community has frequently turned to antibody molecules as recognition elements because they are renowned for their exquisite specificity. Unfortunately antibodies can often fail when immobilised on inorganic surfaces, and alter

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Addis, Philip W., Catherine J. Hall, Shaun Bruton, et al. "Conformational Heterogeneity in Antibody-Protein Antigen Recognition." Journal of Biological Chemistry 289, no. 10 (2014): 7200–7210. http://dx.doi.org/10.1074/jbc.m113.492215.

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Pierce, Brian G., Zhen-Yong Keck, Patrick Lau, et al. "Global mapping of antibody recognition of the hepatitis C virus E2 glycoprotein: Implications for vaccine design." Proceedings of the National Academy of Sciences 113, no. 45 (2016): E6946—E6954. http://dx.doi.org/10.1073/pnas.1614942113.

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The E2 envelope glycoprotein is the primary target of human neutralizing antibody response against hepatitis C virus (HCV), and is thus a major focus of vaccine and immunotherapeutics efforts. There is emerging evidence that E2 is a highly complex, dynamic protein with residues across the protein that are modulating antibody recognition, local and global E2 stability, and viral escape. To comprehensively map these determinants, we performed global E2 alanine scanning with a panel of 16 human monoclonal antibodies (hmAbs), resulting in an unprecedented dataset of the effects of individual alani

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Huang, Jiachen, Darren Diaz, and Jarrod J. Mousa. "Antibody recognition of the Pneumovirus fusion protein trimer interface." PLOS Pathogens 16, no. 10 (2020): e1008942. http://dx.doi.org/10.1371/journal.ppat.1008942.

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Wang, Meryl, David Zhu, Jianwei Zhu, Ruth Nussinov, and Buyong Ma. "Local and global anatomy of antibody-protein antigen recognition." Journal of Molecular Recognition 31, no. 5 (2017): e2693. http://dx.doi.org/10.1002/jmr.2693.

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Kanaujia, G. V., S. Motzel, M. A. Garcia, P. Andersen, and M. L. Gennaro. "Recognition of ESAT-6 Sequences by Antibodies in Sera of Tuberculous Nonhuman Primates." Clinical Diagnostic Laboratory Immunology 11, no. 1 (2004): 222–26. http://dx.doi.org/10.1128/cdli.11.1.222-226.2004.

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ABSTRACT Previous work in our laboratory showed that the ESAT-6 protein of Mycobacterium tuberculosis and Mycobacterium bovis induces strong antibody responses in a large proportion (∼90%) of experimentally or naturally infected nonhuman primates. Here, the antibody response to ESAT-6 in tuberculous monkeys was characterized at the epitope level by measuring antibodies to overlapping, synthetic peptides spanning the ESAT-6 sequence. The antibody response against the COOH-terminal portion of the protein was the strongest in both experimentally and naturally infected animals. Moreover, these ant

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Margulies, David, and Andrew D. Hamilton. "Combinatorial protein recognition as an alternative approach to antibody-mimetics." Current Opinion in Chemical Biology 14, no. 6 (2010): 705–12. http://dx.doi.org/10.1016/j.cbpa.2010.07.017.

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Otlewski, J., and W. Apostoluk. "Structural and energetic aspects of protein-protein recognition." Acta Biochimica Polonica 44, no. 3 (1997): 367–87. http://dx.doi.org/10.18388/abp.1997_4392.

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Specific recognition between proteins plays a crucial role in a great number of vital processes. In this review different types of protein-protein complexes are analyzed on the basis of their three-dimensional structures which became available in recent years. The complexes which are analyzed include: those resulting from different types of recognition between proteinase and protein inhibitor (canonical inhibitors of serine proteinases, hirudin, inhibitors of cysteine proteinases, carboxypeptidase inhibitor), barnase-barstar, human growth hormone-receptor and antibody-antigen. It seems obvious

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Zhu, Jing, and Gang Sun. "Bio-functionalized nanofibrous membranes as a hybrid platform for selective antibody recognition and capturing." RSC Advances 5, no. 36 (2015): 28115–23. http://dx.doi.org/10.1039/c5ra01140j.

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Fuchs, Stephen M., Krzysztof Krajewski, Richard W. Baker, Victoria L. Miller, and Brian D. Strahl. "Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition." Current Biology 21, no. 1 (2011): 53–58. http://dx.doi.org/10.1016/j.cub.2010.11.058.

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Dissertations / Theses on the topic "Protein-Antibody recognition"

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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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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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Easton, Donna Meredith, and n/a. "Functional and Antigenic Characterisation of the Moraxella catarrhalis protein M35." University of Canberra. n/a, 2008. http://erl.canberra.edu.au./public/adt-AUC20081217.083105.

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This thesis reports the characterisation of a novel outer membrane protein (OMP) from M. catarrhalis, designated M35, with a molecular mass of 36.1 kDa. This protein is structurally homologous to classic Gram-negative porins, such as OMP C from E. coli and OMP K36 from K. pneumoniae, with a predicted structure of 8 surface loops connecting 16 antiparallel -sheets. Comparison of the DNA sequences of the M35 genes from 18 diverse clinical isolates showed that the gene was highly conserved (99.6-100 % of nucleotides) with only one isolate (ID78LN266) having base variations that resulted in amino

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Al, Qaraghuli Mohammed. "Investigating the antibody recognition of different hapten classes using a combination of phage display and protein modelling." Thesis, University of Aberdeen, 2014. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=214816.

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Ting, Joy Holtvluwer. "Molecular ecology of mate recognition in the harpacticoid copepod Tigriopus : antibody production, protein purification, and fitness consequences." Diss., Georgia Institute of Technology, 2001. http://hdl.handle.net/1853/25202.

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Diestel, Uschi [Verfasser], та Yves A. [Akademischer Betreuer] Muller. "Structural Basis for TGF-β-Receptor Interaction and Antibody Recognition of HCMV Envelope Protein gB / Uschi Diestel. Gutachter: Yves A. Muller". Erlangen : Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 2014. http://d-nb.info/1075832683/34.

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Joel, Smita. "ENGINEERING PROTEINS WITH UNIQUE CHARACTERISTICS FOR DIAGNOSTICS AND BIOSENSORS." UKnowledge, 2011. http://uknowledge.uky.edu/gradschool_diss/180.

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Proteins possess a broad range of structural and functional properties and, therefore, can be employed in a variety of biomedical applications. While a good number of protein-based biosensing systems and biosensors for target analytes have been developed, the search for versatile, highly sensitive and selective sensors with long term stability able to provide fast detection of target analytes continues to be a challenge. To that end, we now report the design and development of modified proteins with tailored characteristics and their further utilization in the development of biosensing systems

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SIRONI, LAURA. "Nanoparticles for in-vitro and in-vivo biosensing and imaging." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2011. http://hdl.handle.net/10281/19278.

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In the last two decades several groups have investigated the changes of chemical and physical properties of materials with size in nanometric scales. These studies have highlighted a number of possible applications for nanostructures, which are now employed, for example, in biology and medicine for imaging, disease detection, diagnosis, sensing and therapy. Noble metals (especially gold and silver nanoparticles) are particularly versatile for these applications due to the phenomenon known as surface plasmon resonance (SPR), an in-phase oscillations of all the conduction band electrons that re

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Agnew, Heather Dawn. "Rapid Construction of Protein Capture Agents with Chemically Designed Stability and Antibody-Like Recognition Properties." Thesis, 2010. https://thesis.library.caltech.edu/5583/11/Thesis.pdf.

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<p>This thesis describes technologies for the rapid and scalable production of high-affinity, high-specificity protein capture agents which possess the affinities and specificities of antibodies, but also exhibit improved chemical, biochemical, and physical stability. I will discuss how the chemical flexibility of comprehensive, one-bead-one-compound (OBOC) libraries of oligopeptides may be combined with iterative in situ click chemistry to select multi-ligand capture agents. Large OBOC libraries form the basis of individual peptide ligands, and also permit chemically designed stability thro

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Kuo, Ting Yu, and 郭庭佑. "A study of antibody X in the recognition of Helicobacter pylori neutrophil-activating protein as a new antigen." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/15235655246083217830.

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碩士<br>國立清華大學<br>分子與細胞生物研究所<br>104<br>Helicobacter pylori (H. pylori) is a major pathogen involved in gastritis, peptic ulcer disease, and gastric cancer. Helicobacter pylori neutrophil-activating protein (HP-NAP) is an important virulence factor of H. pylori. The inflammation of the gastric mucosa caused by H. pylori infection might be resulted from the cytokines and reactive oxygen species (ROS) produced by HP-NAP-stimulated human leukocytes. Thus, H. pylori-induced inflammation of the gastric mucosa could be attenuated by blocking the activity of HP-NAP. Here, I found that antibody X not

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Books on the topic "Protein-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 Laboratory, 1985.

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E, Sercarz Eli, and Berzofsky Jay A, eds. Immunogenicity of protein antigens: Repertoire and regulation. CRC Press, 1987.

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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 supramolec

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Book chapters on the topic "Protein-Antibody recognition"

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Janin, Joël, Jacqueline Cherfils, and Stéphane Duquerroy. "Principles of Protein — Protein Recognition in Protease-Inhibitor and Antigen-Antibody Complexes." In Computation of Biomolecular Structures. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77798-1_9.

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Jones, Susan, and Janet M. Thornton. "Analysis and classification of protein-protein interactions from a structural perspective." In Protein-Protein Recognition. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637614.003.0002.

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Abstract Interactions between macromolecules are fundamental to many biological processes. Such interactions are central to the functioning of the vertebrate immune system, enzyme regulation, neurotransmitter release in the nervous system, and cell adhesion. The characterization of the interfaces formed when proteins interact is important if these and other systems are to be fully understood, and if the potential to control these interactions for medical and industrial applications is to be explored. The Brookhaven Protein Data Bank (PDB) (1, 2) now contains the three-dimensional coordinates of more than 12000 structures; an ever-increasing number of which are protein-protein complexes, including: oligomeric proteins; enzyme-inhibitor complexes; and antibody-protein complexes. Their deposition allows the analysis of large numbers of these structures, and such computational studies have provided important overviews of the physical and chemical properties of these associations (see, for example, refs 3-6). Protein-protein complexes with different interaction histories and functions require different modes of interaction. This chapter begins with the classification of these associations, considering functional classes of complexes, permanent and non-obligate complexes, and biological and crystallographic associations. The physical and chemical characteristics of biological associations are then discussed, presenting an overview of the properties favouring associations, namely hydrophobic and electrostatic interactions, and shape complementarity. These are then considered in more detail with reference to computational studies conducted on large data sets of protein complexes.

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Hilyard, Kate L., David Staunton, Alison E. Jones,, and Anthony R. Rees. "Protein Engineering of Antibody Combining Sites." In Protein Engineering. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780199631391.003.0011.

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Abstract 1. Introduction The immunoglobulin G (IgG) molecule consists of a tetramer of two identical 25 kDa polypeptides (the light chain, L) and two identical 50 kDa polypeptides (the heavy chain, H). Crystal structures of IgG and IgG fragments have shown the antibody combining site (ACS) to be formed by the juxtaposition of six hypervariable loops or complementarity determining regions (CDRs), three from the light chain variable domain and three from the heavy chain variable domain. The CDRs of each chain are supported on a framework region which consists of conserved 13-strands that fold to form a β-sandwich. When a light and heavy chain come together, one surface of each sandwich associates to form a β-barrel structure (Figure la, b). Supported on this β-barrel scaffold the six CDRs, pack together in the tertiary structure to form a relatively flat platform with a surface area of about 700 Å2 (1). This variable domain, which contains all the determinants of antigen recognition, is one of six domains in the lgG molecule, the remaining five being Constant or C-type domains. The relative positions of these domains in the characteristic Y-shaped IgG and their nomenclature are shown in Figure lc.

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Stone, Julie M., and John C. Walker. "Interaction cloning of protein kinase partners." In Protein Phosphorylation. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780199637294.003.0012.

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Abstract Historically, protein kinase partner proteins have been isolated by biochemical means, which requires purification of the interacting protein for antibody production or microsequencing before a cDNA clone can be obtained. However, two molecular biological approaches, the yeast two-hybrid system (Chapter 14) and interaction (or expression) cloning (1), directly yield a cDNA clone encoding the interacting protein. In this chapter we describe some of the recent advances in interaction cloning as a simple, rapid, and powerful alternative to biochemical approaches to identify protein kinase partners. The recombinant protein kinase of interest is enzymatically labelled with 32P by virtue of a five amino recognition site for cAMP-dependent protein kinase (PKA), to facilitate the identification of cDNA clones encoding interacting partners. Briefly, expression of polypeptides encoded by cDNA inserts from a bacteriophage X. expression library is induced, and the polypeptides adsorbed on to nitrocellulose filters. The library is then screened with the radiolabelled protein probe to identify cDNA clones expressing interacting protein kinase partners (see Figure 1).

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James, Dominika Lipowska, and Maryam Jowza. "Protein Function as Immunoglobulins and Hormones." In Basic Anesthesia Review, edited by Alaa Abd-Elsayed. Oxford University PressNew York, 2024. http://dx.doi.org/10.1093/med/9780197584569.003.0323.

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Abstract All living things depend on proteins for their existence. Proteins are some of the most structurally complex biological molecules, whose three-dimensional configuration is inherently correlated with their function. Proteins serve a wide array of physiological processes within the human body; they not only are the primary building blocks of many tissues, but also serve as hormones coordinating physiological activities, as well as carrying immune function as immunoglobulins. Protein hormones are specific proteins involved in cell signaling and communication. They are secreted by endocrine organs and are involved in regulation of many biological processes such as growth, metabolism, sexual development, and procreation. Protein hormones vary in size and structure and as such can be divided into amines, peptides, proteins, and glycoproteins. Immunoglobulins, otherwise known as antibodies, are immunologically specialized plasma proteins produced by B cells, which are essential to proper function of humoral immunity. Antibodies serve two main immunological functions: recognition and identification of pathogens and their destruction. There are five distinct antibody classes, which differ in structure and function: IgG, IgM, IgA, IgE, IgD. Structure of immunoglobulins is based on their peptide chain amino acid sequences and defines their role and antigen-binding specificity. Each antibody is capable of recognizing specific antigens. Pathogen neutralization may occur via antibody mediated processes such as cellular lysis, phagocytosis, opsonization, and complement activation.

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"Macromolecule-Imprinted Polymers: Antibody/Receptor Mimics for Protein Recognition and Catalysis." In Biomedical Nanosensors. Jenny Stanford Publishing, 2012. http://dx.doi.org/10.1201/b13721-4.

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LAVER, W. G., P. M. COLMAN, G. M. AIR, et al. "Recognition of Protein Antigens by Antibodies: Crystal Structure of Antibody Fab Fragments Complexed with Influenza Virus Neuraminidase." In Immune Recognition and Evasion: Molecular Aspects of Host�parasite Interaction. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-711710-2.50010-8.

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Smith, Patricia R., Keith M. Wilson, Ian E. G. Morrison, Richard J. Cherry,, and Nelson Fernandez. "Imaging of individual cell surface MHC antigens using fluorescent particles." In MHC. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780199635559.003.0007.

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Abstract Class I and class II major histocompatibility complex (MHC) molecules are cell surface, transmembrane glycoproteins that have similar overall structure but have readily distinguishable subunit structures (1). The two classes of MHC molecules present peptides, produced from different intracellular compartments, at the cell surface where they are recognized by two major subsets of T cells, CD4 and CDS, respectively. Integral membrane glycoproteins are able to diffuse to varying degrees within the plane of the membrane and so can potentially form protein clusters (2). This clustering of cell surface receptors in response to a particular signal or antibody is important in transmembrane signal transduction (3, 4). The density of class I and class II subsets and their relationship with other cell surface molecules in the correct orientation is thought to be vital for effective T cell recognition.

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"Analysis by specific binding." In Immunoassays, edited by James P. Gosling. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637119.003.0001.

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Abstract In the last 30 years analytical methods that depend on the recognition of analytes by high-affinity, specific binding proteins and oligonucleotides have found so many applications in diverse areas of biochemical analysis that they now represent a standard analytical principle, such as colorimetry or chromatography. While there are many kinds of high-affinity, specific binding proteins in nature (hormone receptors, for example), the special properties of antibodies have made them the most popular choice for protein binding assays (Table 1 ). Measurement procedures that use antibodies as specific binding reagents are called immunoassays, as are assays that use antigens for the detection or quantification of specific antibodies. It is because of the extraordinary affinity, specificity and variety of antibody-antigen binding reactions, that immunoassays are used for routine analyses and for research purposes throughout the biological and medical sciences.

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Price, Michael R., and Kami Beyzavi. "Preparative immunoaffinity techniques." In Peptide Antigens. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780199634521.003.0005.

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Abstract Immunoaffinity chromatography is one of the most powerful separative procedure-s for the purification of antigens or antibodies. The technique exploits the exquisite immunological specificity of their recognition and binding, which occurs even in complex mixtures. The procedure is highly empirical, but often separations resulting in purification of a product by several thousand-fold may be achieved by using simple chromatographic techniques. The technique has found application in the purification of diverse macro-molecules. This has been particularly enhanced over the last decade or so, following the development of hybridoma technology for the production of stable cell hybrids secreting homogeneous monoclonal antibodies of identical immunological and biochemical characteristics (1). Moreover, it is feasible to identify the epitopes for many monoclonal antibodies and, in the case of protein antigens, to prepare synthetic peptides corresponding to the native epitopes. This is being exploited in an attempt to enhance our understanding of the antigen-antibody interaction, and at the practical level to provide novel approaches in immunoaffinity techniques.

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Conference papers on the topic "Protein-Antibody recognition"

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Lord, S. T. "DIRECTED MUTAGENESIS OF HUMAN FIBRINOGEN: Aα CHAIN SUBSTITUTIONS THAT ALTER THROMBIN CLEAVAGE AND ANTIBODY RECOGNITION". У 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

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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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Pancham, N., M. Dumas, J. Brown, T. C. Michaud, and W. J. Knowles. "SYNTHETIC PEPTIDE ANTIBODIES RECOGNIZE PLASMA AND RECOMBINANT FVIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644027.

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Monoclonal antibodies were raised against synthetic peptides corresponding to the N-termini of the 90kd and 80kd subunits of human FVIII. Preliminary screening was performed directly against the peptides (linked to albumin) coated onto polystyrene wells. IgG was purified by Protein A-Sepharose and affinity purified using the immunogen peptides linked to Sepharose. Immunoreactivity with both plasma and recombinant FVIII was compared by Western blotting, two-site ELISA employing a neutralizing rabbit anti-FVIII IgG as capture antibody, and inhibition in a fluid phase FVIII activity assay. None o

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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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Thiesen, Ana Paula, Bruna Mielczarski, and Ricardo Francalacci Savaris. "DEEP LEARNING NEURAL NETWORK IMAGE ANALYSIS OF IMMUNOHISTOCHEMICAL PROTEIN EXPRESSION REVEALS A SIGNIFICANTLY REDUCED EXPRESSION OF BIGLYCAN IN BREAST CANCER." In Brazilian Breast Cancer Symposium 2022. Mastology, 2022. http://dx.doi.org/10.29289/259453942022v32s2014.

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Objective: The aim of this study was to compare the protein expression of biglycan (BGN) in normal breast tissue and in breast cancer using deep learning and digital HScore techniques. Methods: In this case-control study, 24 formalin-fixed, paraffin-embedded tissues were obtained from pathological archives for analysis. Normal breast (n=9) and breast cancer (n=15) tissue sections were analyzed by immunohistochemistry using BGN monoclonal antibody (M01 – Abnova), clone 4E1-1G7 at dilution 1:300 at pH 6, and 3,3’-diaminobenzidine (DAB) as the chromogen. Photomicrographs of the slides were analyz

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Lima, Beatriz Alves, Andressa da Silva Pereira, Bruna Alves Lima, et al. "PREDICTORS OF BREAST CANCER PROGNOSIS BASED ON TUMOR BIOMARKERS." In Abstracts from the Brazilian Breast Cancer Symposium - BBCS 2021. Mastology, 2021. http://dx.doi.org/10.29289/259453942021v31s2022.

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Objective: To analyze the tumor biological markers of breast cancer associated with the prognostic of the disease. Methodology: A systematic review was carried out on the Scielo, PubMed, and the National Cancer Institute databases on the topic. Descriptors used were: tumor biomarkers, breast cancer, and prognosis. Thus, 15 articles published between 2001 and 2020 were selected. Results: Breast cancer, characterized by the disordered multiplication of breast cells, is the most incident in women in the world, representing 24.2% of the total cases in 2018, and the most frequent cause of death in

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Vermeer, C., BA M. Soute, and MM W. Ulrich. "IN VITRO CARBOXYLATION OF EXOGENOUS PROTEIN SUBSTRATES BY VITAMIN K-DEPENDENT CARBOXYLASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643994.

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In vivo treatment of experimental animals with vitamin K-antagonists induces the accumulation of non-carboxylated coagulation factor precursors in the liver, where they are tightly bound to vitamin K-dependent carboxylase. If hepatic carboxylase is isolated from warfarin-treated animals, it is obtained therefore almost exclusively in the form of an enzyme/substrate complex. If carboxylase is prepared from non-treated animals, on the other hand, the resulting enzyme is predominantly substrate-free. Small substrates like F L E E L or decarboxylated osteocalcinare carboxylated equally well by bot

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Reports on the topic "Protein-Antibody recognition"

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Spiegel, Yitzhak, Michael McClure, Itzhak Kahane, and B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7613015.bard.

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Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previou

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