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tag yeast two hybrid analysis evolution

The Yeast Two-hybrid Assay
Mark Greener(mgreener@the-scientist.com) | Aug 28, 2005 | 8 min read
No protein is an island.
Yeast Genome Doubling
Amanda B. Keener | Aug 10, 2015 | 1 min read
The results of a computational genetic analysis suggest Saccharomyces cerevisiae doubled its genome through species hybridization.
An Alternative to Two-Hybrid
Aileen Constans | Oct 28, 2001 | 2 min read
Researchers most often use techniques such as coimmunoprecipitation and yeast two-hybrid screening to study protein-protein interactions. These methods are time-consuming-the yeast two-hybrid technique can take several months to perform-and prone to false positive results. Millbury, Mass.-based Hypromatrix recently introduced AntibodyArray™ technology to combat these problems. Hypromatrix developed the AntibodyArray for the study of protein-protein interactions and protein phosphorylation,
Green and red fluorescent proteins in a zebrafish outline the animal’s vasculature in red and lymphatic system in green in a fluorescent image. Where the two overlap along the bottom of the animal is yellow.
Serendipity, Happenstance, and Luck: The Making of a Molecular Tool
Shelby Bradford, PhD | Dec 4, 2023 | 10+ min read
The common fluorescent marker GFP traveled a long road to take its popular place in molecular biology today.
The Two Body Problem
Laura Defrancesco | Apr 11, 1999 | 10+ min read
Two-Hybrid Systems Studying a biological phenomenon? Which field? Well, it really doesn't matter. Whatever the area of interest, rest assured that protein-protein interactions are somehow, somewhere involved--if not directly, then as part of a structural or regulatory apparatus. Two-hybrid systems, pioneered by Fields and Song,1 are powerful systems for detecting interactions between and among macromolecules. The first systems described were for protein-protein interactions; later, the basic
Systematic proteomics in yeast
Jonathan Weitzman(jonathanweitzman@hotmail.com) | Jan 9, 2002 | 1 min read
Large-scale purification and mass spectrometry has been used to characterize hundreds of multiprotein complexes in yeast.
Yeast: An Attractive, Yet Simple Model
Gregory Smutzer | Sep 16, 2001 | 9 min read
Yeast possesses many characteristics that make it especially useful as a model system in the laboratory, including an entirely sequenced genome. Recently, a number of researchers published studies detailing the transition from genome sequencing to functional genomics. Notably, these scientists have developed new high-throughput approaches to the characterization of large numbers of yeast genes. In aggregate, these studies make yeast one of the most well-characterized eukaryotic organisms known.
bacteria inside a biofilm
How Bacterial Communities Divvy up Duties
Holly Barker, PhD | Jun 1, 2023 | 10+ min read
Biofilms are home to millions of microbes, but disrupting their interactions could produce more effective antibiotics.
Finding a Mate
Barbara Cunningham | Apr 1, 2001 | 9 min read
Available Two-hybrid Systems Graphic: Leza BerardoneGenome sequencing has produced a vast supply of proteins in need of a functional identity. One way to identify a protein's function is to identify its interacting partners, because proteins often work in pairs or as part of large complexes. Scientists traditionally have used biophysical or biochemical methods (such as affinity chromatography or co-immunoprecipitation) to study protein-protein interactions. More recently, two-hybrid and phage-d
Playing Protein Hide and Seek
Mignon Fogarty | Apr 11, 2004 | 6 min read
LIGHTING THEIR LOCATIONS:© 2002 Cold Spring Harbor PressImmunolocalization of epitope-tagged proteins. (A-E) represent cells containing HAT-tagged proteins stained with the DNA dye, DAPI, and a monoclonal antibody against hemagluttinin, α-HA. At right the images are merged. (F-J) indicates cells carrying V5 tagged proteins. The bar equals 2 μm.Aliens sifting through the remains of a lost human civilization might puzzle over the function of a ladle. But if found in a room associate

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