نتایج جستجو برای: P22

تعداد نتایج: 1939  

Delavar Shahbaz-Zadelf, Mostafa Saadat,

The gene encoding alpha fetoprotein (locus symbol Afp) was assigned to rat chromosome 14 at band p21-p22 using fluorescence in situ hybridization method. The present result suggests that there is a conserved syntenic group between human 4q11-q13, mouse 5F-G, and rat 14p21-p22.

Journal: :The Biochemical journal 2004
Josefa Andrade Sandy Timm Pearce Hu Zhao Margarida Barroso

Previously, we have shown that p22, an EF-hand Ca2+-binding protein, interacts indirectly with microtubules in an N-myristoylation-dependent and Ca2+-independent manner. In the present study, we report that N-myristoylated p22 interacts with several microtubule-associated proteins within the 30-100 kDa range using overlay blots of microtubule pellets containing cytosolic proteins. One of those ...

Journal: :Journal of molecular biology 1978
E N Jackson H I Miller M L Adams

‘l’l~e SWYW EcoKI restriction endonuclease cleavage sites in bacteriophage P%d DNA have been mapped. The cleavage site map of circularly permut.ed P22 linear DNA is a circle. The positions of EcoRI sites in the early region of the P22 genomc were determined by comparing products of EcoRI digestion of maturtx liaear P22 chromosomes with the EcoRI cleavage fragments of DNA of three XimmP22 hybrid...

Journal: :Virology 1972
R K Chan D Botstein T Watanabe Y Ogata

A high-frequency-transducing (HFT) lysate for tetracycline resistance (Lets) was obtained by inducing an unusual tets P22 lysogen which had been made by transducing Salmonella typhimurium LT.2 to letR with P22 phage grown on an LT-2 strain carrying the R factor 222. The HFT lysate contains defective P22 particles, called P22 Tc-10, which cannot grow or lysogenize (i.e., transduce tetn) upon sin...

1996
Margarida R. Barroso Karen K. Bernd Natalie D. DeWitt Andrea Chang Ken Mills Elizabeth S. Sztul

We have identified a novel protein, p22, required for “constitutive” exocytic membrane traffic. p22 belongs to the EF-hand superfamily of Ca-binding proteins and shows extensive similarity to the regulatory subunit of protein phosphatase 2B, calcineurin B. p22 is a cytosolic N-myristoylated protein that undergoes conformational changes upon binding of Ca. Antibodies against a p22 peptide block ...

Journal: :Molecular biology of the cell 1999
S Timm B Titus K Bernd M Barroso

Proteins containing the EF-hand Ca(2+)-binding motif, such as calmodulin and calcineurin B, function as regulators of various cellular processes. Here we focus on p22, an N-myristoylated, widely expressed EF-hand Ca(2+)-binding protein conserved throughout evolution, which was shown previously to be required for membrane traffic. Immunofluorescence studies show that p22 distributes along microt...

Journal: :Journal of virology 1977
J M Pipas R H Reeves

Two peaks of RNA synthesis (early and late) are directed by bacteriophage P22 in lytic infections of Salmonella typhimurium. Late RNA synthesis is not seen in P22 23- infections; neither early nor late RNA synthesis occurs in P22 24- infections. Genes 23 and 24 of P22 appear to be analogous to genes Q and N of lambda, respectively.

Journal: :Journal of bacteriology 2008
Yoshihiro Yamaguchi Yumiko Takatsuka Yoshiyuki Kamio

In Selenomonas ruminantium, a strictly anaerobic and gram-negative bacterium, the degradation of lysine/ornithine decarboxylase (LDC/ODC) by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain. Amino acid sequence alignment of S. ruminantium P22 with the L10 ribosomal proteins of gram-positive and -negative bacteria showed that P22 has a 5...

Journal: :Nucleic acids research 2001
M L Hayman M M Miller D M Chandler C C Goulah L K Read

RBP16 is a guide RNA (gRNA)-binding protein that was shown through immunoprecipitation experiments to interact with approximately 30% of total gRNAs in Trypanosoma brucei mitochondria. To gain insight into the biochemical function of RBP16, we used affinity chromatography and immunoprecipitation to identify RBP16 protein binding partners. By these methods, RBP16 does not appear to stably intera...

Journal: :FEBS letters 2003
María U Moreno Gorka San José Josune Orbe José A Páramo Oscar Beloqui Javier Díez Guillermo Zalba

The p22(phox) subunit is an essential protein in the activation of NAD(P)H oxidase. Here we report the preliminary characterisation of the human p22(phox) gene promoter. The p22(phox) promoter contains TATA and CCAC boxes and Sp1, gamma-interferon and nuclear factor kappaB sites. We screened for mutations in the p22(phox) promoter and identified a new polymorphism, localised at position -930 fr...

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