Results 271 to 280 of about 251,250 (306)

Protein interaction maps for model organisms

Nature Reviews Molecular Cell Biology, 2001
Until recently, classical genetics and biochemistry were the main techniques used to investigate how organisms develop, reproduce, behave and age. But with the availability of complete genome sequences new approaches are emerging. Complete sets of proteins — 'proteomes' — can be predicted from genome sequences and used to characterize protein functions
A J, Walhout, M, Vidal
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Mapping protein–protein interactions with combinatorial biology methods

Current Opinion in Biotechnology, 2001
Extremely diverse, DNA-encoded libraries of peptides and proteins have been constructed that include a linkage between each polypeptide and the encoding DNA. Library members can be selected by virtue of a particular binding specificity, and their protein sequence can be deduced from the sequence of the cognate DNA.
J, Pelletier, S, Sidhu
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Novel approaches to map protein interactions

Current Opinion in Biotechnology, 2003
Although we now have the sequence of the human genome at hand, we face the challenge of assigning function to the identified genes. Genes usually ascribe their function through proteins, and the role of proteins is to interact with other molecules. Therefore, if we could map the interactions of proteins we would be able to understand protein function ...
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The protein–protein interaction map of Helicobacter pylori

Nature, 2001
With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function. As elementary constituents of cellular protein complexes and pathways, protein-protein interactions are key ...
J C, Rain, L, Selig, H, De Reuse, V, Battaglia, C, Reverdy, S, Simon, G, Lenzen, F, Petel, J, Wojcik, V, Schächter, Y, Chemama, A, Labigne, P, Legrain   +12 more
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Transcriptome-Wide Mapping of Protein–RNA Interactions

2020
RNA and RNA-binding proteins (RBPs) control multiple biological processes. The spatial and temporal arrangement of RNAs and RBPs underlies the delicate regulation of these processes. The strategy called CLIP-seq (cross-linking and immunoprecipitation) has been developed to capture endogenous protein-RNA interactions with UV cross-linking followed by ...
Xianju, Bi, Xiaohua, Shen
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Proteolytic DNA for Mapping Protein−DNA Interactions

Biochemistry, 2002
We describe a technique to determine sites on proteins involved in protein-DNA interactions. DNA was synthesized via polymerase chain reaction (PCR) to produce four polynucleotide products with phosphorothioate nucleotides at the A, T, G, or C residues.
Brian D, Schmidt, Claude F, Meares
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Mapping Protein–DNA Interactions Using ChIP-Sequencing

2011
Chromatin immunoprecipitation (ChIP) allows enrichment of genomic regions which are associated with specific transcription factors, histone modifications, and indeed any other epitopes which are present on chromatin. The original ChIP methods used site-specific PCR and Southern blotting to confirm which regions of the genome were enriched, on a ...
Massie, Charles E, Mills, Ian G
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Mapping RNA–Protein Interactions Using Iodine Footprinting

Cold Spring Harbor Protocols, 2014
Footprinting methods are used to determine the binding site of a protein on an RNA. They are based on the fact that a protein bound to an RNA protects the RNA from cleavage by chemicals or nucleases. The footprinting method described here relies on the ability of iodoethanol to cleave the backbone of RNA when a phosphodiester bond contains sulfur in ...
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Construction and Prediction of Protein-Protein Interaction Maps

2002
With the completion of full genome sequence for several model organisms, new approaches are emerging to comprehensively characterize the function of gene products. In these so-called functional proteomics approaches, large-scale assays on the complete set of proteins of a given organism — the proteome — enable the study of the function of proteins in ...
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Mapping protein-protein interactions with alkaline phosphatase fusion proteins

2001
Publisher Summary This chapter describes a convenient and versatile method for determining the molecular recognition properties of SH3 domains, using bacterial alkaline phosphatase as a fusion protein. A variety of proteins or peptides have been fused to the N terminus of alkaline phosphatase (AP) by genetic engineering, including antibody chains and
M, Yamabhai, B K, Kay
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