Results 311 to 320 of about 704,733 (343)
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G PROTEIN βγ SUBUNITS

Annual Review of Pharmacology and Toxicology, 1997
▪ Abstract  Guanine nucleotide binding (G) proteins relay extracellular signals encoded in light, small molecules, peptides, and proteins to activate or inhibit intracellular enzymes and ion channels. The larger G proteins, made up of Gαβγ heterotrimers, dissociate into Gα and Gβγ subunits that separately activate intracellular effector molecules ...
Eva J. Neer, David E. Clapham
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Protein–protein interactions of a Kvβ subunit in the cochlea

Journal of Neuroscience Research, 2005
AbstractAccessory subunits associated with voltage‐gated potassium (Kv) channels can influence the biophysical properties and promote the surface expression of channel‐forming α‐subunits. Previously, we cloned several α‐subunits and a β‐subunit from a cDNA library of the chicken cochlea.
Margaret Harvey   +3 more
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Interactions of protein kinase CK2 subunits

Molecular and Cellular Biochemistry, 1999
Several approaches have been used to study the interactions of the subunits of protein kinase CK2. The inactive mutant of CK2alpha that has Asp 156 mutated to Ala (CK2alphaA156) is able to bind the CK2beta subunit and to compete effectively in this binding with wild-type subunits alpha and alpha'.
Narayanaswamy Srinivasan   +5 more
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Matrix-bound protein subunits

Biochemical and Biophysical Research Communications, 1970
Abstract A method is described for studying spatially isolated subunits by attaching them covalently to a rigid matrix and thus preventing them from re-association. Application of this method to rabbit muscle aldolase indicates that the subunits are capable of enzyme activity.
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[36] Targeting subunits for protein phosphatases

1991
Publisher Summary This chapter discusses the targeting subunits for protein phosphatases. Protein phosphatase 1 (PP1), one of the major protein-serine/threonine phosphatase catalytic subunits in eukaryotic cells, does not exist as a monomer in vivo, but as complexes with other proteins that target it to particular subcellular locations, modify its ...
Hubbard, Michael J., Cohen, Philip
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Protein Subunit-Subunit to Domain-Domain Interactions

2018
Fusion proteins often referred to as “rosetta stone” occur through an important evolutionary phenomenon called gene fusion. This results in chimeric sequences in one species compared to its unfused individual component sequences in yet another species.
Pandjassarame Kangueane   +1 more
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Dissecting subunit interfaces in homodimeric proteins

Proteins: Structure, Function, and Bioinformatics, 2003
AbstractThe subunit interfaces of 122 homodimers of known three‐dimensional structure are analyzed and dissected into sets of surface patches by clustering atoms at the interface; 70 interfaces are single‐patch, the others have up to six patches, often contributed by different structural domains.
Francis Rodier   +3 more
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Comparative immunogenicities of tobacco mosaic virus, protein subunits, and reaggregated protein subunits

Virology, 1967
Abstract When TMV protein, either dissociated subunits or reconstituted protein rods, is injected into rabbits, the amount of precipitating antibodies directed against the intact virus is 2–8 times smaller at the peak of synthesis than when similar amounts of TMV are injected.
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The protein subunit of potato virus X

Virology, 1968
Abstract The N-terminal amino acid residue of the capsid protein of potato virus X is acetylated as it is in several other plant virus proteins. On the basis of amounts of acetic acid recovered from the N-terminal residue, and amino acid analysis coupled with peptide mapping, the protein subunit of potato virus X was found to consist of about 210 ...
C.A. Knight   +3 more
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A protein subunit of bromegrass mosaic virus

Journal of Molecular Biology, 1964
The protein and RNA of bromegrass mosaic virus were separated from each other by dialysis of the virus against 1 M -calcium chloride. In this medium the virus is degraded, the RNA is quantitatively precipitated and there remains a supernatant solution of viral protein. The protein obtained in this way was soluble in various buffers in the pH range 5·5
John D. Stubbs, Paul Kaesberg
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