Results 151 to 160 of about 29,356 (170)
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Phosphoproteins and Biomineralization

Phosphorus, Sulfur, and Silicon and the Related Elements, 1999
Phosphoproteins play multiple roles in regulating biomineralization. This paper reviews the data implicating bone and dentin phosphorylated proteins in this process, and provides data suggesting which protein domains may be important in the interaction with apatite mineral crystals.
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Phosphoproteins in dictyostelium discoideum

Journal of Supramolecular Structure and Cellular Biochemistry, 1981
AbstractThe phosphoproteins of Dictyostelium discoideum were compared at different stages of development by polyacrylamide gel electrophoresis. Certain phosphoproteins of vegetative amoebae were conserved while others appeared and disappeared during development.
Howard V. Rickenberg   +4 more
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Nuclear phosphoproteins

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
SUMMARY The effects of histones on the enzymatic phosphorylation of nuclear phosphoproteins have been extensively studied in vitro. Histones cause a 5- to Io-fold increase in the rate and extent of phosphorylation of nuclear phosphoprotein, with the lysinerich histones being the most effective at stimulation. Evidence suggests that the histones are not
Kaplowitz, Paul B.   +2 more
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Phosphoproteins in Postsynaptic Densities

1982
Publisher Summary The postsynaptic density (PSD) is a dense submembranous filamentous array located behind and in intimate contact with the postsynaptic membrane. PSDs have been isolated from synaptosomal plasma membranes and synaptosomes using various detergents.
Richard K. Carlin   +3 more
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Ribosomal phosphoproteins in Physarumpolycephalum

Biochemical and Biophysical Research Communications, 1979
Abstract Ribosomal proteins of Physarum polycephalum were labelled in vivo with 32PO4. Three acid phosphoproteins were observed in the large subunit, while two basic ones were present in the small subunit. Ribosomal phosphoprotein S3 accounted for 70% of the total radioactivity and may be equivalent to S6 from rat liver.
Gérald Lemieux   +2 more
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Chloroplast phosphoproteins: Distribution of phosphoproteins within spinach chloroplasts

Plant Science Letters, 1984
Abstract The distribution of phosphoproteins within spinach chloroplasts was studied. Intact chloroplasts with good rates of CO 2 -dependent oxygen evolution were fed [γ- 32 P]ATP and then separated into stroma and membrane fractions. Only one major labelled stroma protein was identified by gel electrophoresis/autoradiography, with a mol. wt.
John T. Christeller, William A. Laing
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Grabbing phosphoproteins

Nature, 1999
The control of complex cellular events relies on precise regulation of signalling molecules. The activity of many such proteins is controlled by adding a phosphate group to certain amino acids such as tyrosine, serine and threonine. A well-known motif -- the SH2 domain -- binds to phosphotyrosine residues.
Michael B. Yaffe, Lewis C. Cantley
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Phosphoproteins of adenovirus 2

Virology, 1978
Abstract Analysis of [ 32 P]orthophosphate-labeled extracts of adenovirus 2 (AD2)-infected HeLa cells revealed three major adenovirus-specific phosphorylated species, of molecular weights (MW) 100,000, 72,000, and 33,000. The 72,000 MW species became detectable as a phosphorylated entity at about 15 hr after infection, the 33,000 and 100,000 MW ...
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LIS1 is a microtubule‐associated phosphoprotein

European Journal of Biochemistry, 1999
Lissencephaly, a severe brain malformation, may be caused by mutations in the LIS1 gene. LIS1 encodes a microtubule‐associated protein (MAP) that is also part of the enzyme complex, platelet‐activating factor acetylhydrolase. LIS1 is also found in a complex with two protein kinases; a T‐cell Tat‐associated kinase, which contains casein‐dependant kinase
Sergei Nekhai   +4 more
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Phosphoprotein phosphatase of the human erythrocyte

Biochemical and Biophysical Research Communications, 1976
Summary Human erythrocytes contain phosphoprotein phosphatase activity that can be assayed by measurement of 32Pi release from partially purified [32P]spectrim. The activity is entirely cytoplasmic and is readily detected at very high dilution (.e.g, 10−4 relative to packed cells). Because the reaction in vitro is highly inhibited by Pi, ATP and 2,
Grant Fairbanks   +3 more
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