2006
DOI: 10.2174/138620706777452429
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Microarray Technology as a Universal Tool for High-Throughput Analysis of Biological Systems

Abstract: Over the last years microarray technology has become one of the principal platform technologies for the highthroughput analysis of biological systems. Starting with the construction of first DNA microarrays in the 1990s, microarray technology has flourished in the last years and many different new formats have been developed. Peptide and protein microarrays are now applied for the elucidation of interaction partners, modification sites and enzyme substrates. Antibody microarrays are envisaged to be of high imp… Show more

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Cited by 110 publications
(60 citation statements)
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References 182 publications
(226 reference statements)
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“…Furthermore, because the carboxy, amino, or epoxy-bearing residues are involved in protein folding, such multipoint-coupling methods can potentially lead to protein instability or even denaturation. Therefore, approaches enabling site-specific immobilization have attracted much attention [74][75][76][77]. These include the approaches based on F c antibody fragments or protein A or G. Currently available preparation methods for recombinant proteins and synthetic oligopeptides are expected to encourage the design and preparation of new protein bioreceptors having specifically located functionalities, for example histidine tags, oligopeptide tags for the covalent attachment of biotin or oligonucleotides, specific peptide sequences for coiled-coil hybridization [78], engineered antibody fragments, antibody mimetics, recombinant antigens, epitope structures, and peptide aptamers.…”
Section: Attachment Of Biorecognition Elementsmentioning
confidence: 99%
“…Furthermore, because the carboxy, amino, or epoxy-bearing residues are involved in protein folding, such multipoint-coupling methods can potentially lead to protein instability or even denaturation. Therefore, approaches enabling site-specific immobilization have attracted much attention [74][75][76][77]. These include the approaches based on F c antibody fragments or protein A or G. Currently available preparation methods for recombinant proteins and synthetic oligopeptides are expected to encourage the design and preparation of new protein bioreceptors having specifically located functionalities, for example histidine tags, oligopeptide tags for the covalent attachment of biotin or oligonucleotides, specific peptide sequences for coiled-coil hybridization [78], engineered antibody fragments, antibody mimetics, recombinant antigens, epitope structures, and peptide aptamers.…”
Section: Attachment Of Biorecognition Elementsmentioning
confidence: 99%
“…Using interaction domains for PPI studies is justifi ed by the fact that protein binding domains are usually restricted to short amino acid sequences. Thus, domains or synthetic peptides representing a protein binding site often show the same biological activity as the protein itself (88). However, it may be possible that the exposition of the entire domain outside of its native protein context may open additional interaction possibilities not normally observed for the protein in question.…”
Section: Library Construction and Protein Purifi Cationmentioning
confidence: 99%
“…1 They enable rapid, highly parallel analysis of target molecules in an unknown sample. A microarray-based analytical strategy is quicker and more convenient than serial testing for individual analytes, and it has been successfully applied to a variety of biological assays, such as sequencing by hybridization, 2 mutation detection, 3 assessment of gene copy number, 4 comparative genome hybridization, 5 drug discovery, 6 expression analysis, 7 immunoassays, 8 and proteomic analysis.…”
Section: Introductionmentioning
confidence: 99%