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Functional interaction between a novel protein phosphatase 2A
Functional interaction between a novel protein phosphatase 2A

... inhibit PP2A, but not PP1 (Cohen et al., 1989; Honkanan et al., 1994). Figure 3c shows that the phosphatase activity in immunoprecipitates of the HAPR65 and the HA-PP2Ac-transfected cells could be inhibited by this concentration of okadaic acid, strongly suggesting that the phosphatase activity seen ...
eXtra Botany - Journal of Experimental Botany
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... 2009). Consequently, current data from genetic and biochemical approaches suggest a model in which development of specific plant cells and tissues is characterized by the expression of distinct tubulin genes and, consequently, by the use of distinct tubulin isotypes, which are post-translationally m ...
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... intracellular receptor proteins. These receptors function as ligandactivated transcription factors, switching on or off networks of genes in response to a specific hormone signal. The receptor proteins have a conserved domain organization, comprising a C-terminal LBD (ligand-binding domain), a hinge ...
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... 4. Describe how prokaryotes carry out cellular respiration when they lack compartmentalized organelles such as mitochondria. 5. List the three domains of life. 6. Describe the structure, composition, and functions of prokaryotic cell walls. 7. Distinguish the structure and staining properties of gra ...
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... various strategies to spread from one cell to another. Animal viruses commonly use vesicular transport machineries in the se­ cretory and endocytosis/exocytosis pathways for entry and exit (Pelkmans et al., 2001; Sieczkarski and Whittaker, 2002; Smith and Helenius, 2004; Greber and Way, 2006). Howev ...
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The Case of Protein Kinase CK2

... CK2β seems to interact directly with more than 40 different proteins, including other protein kinases such as A-Raf, Chk1, Chk2, PKC-ζ, Mos and p90rsk (Bibby & Lichfield, 2005; BolanosGarcia et al., 2006; Olsen & Guerra, 2008). It was shown that association of the human protein kinases Chk1, Mos, an ...
Dual targeting of aminoacyl-tRNA synthetases to the mitochondrion
Dual targeting of aminoacyl-tRNA synthetases to the mitochondrion

... Accepted 18 September 2012 Journal of Cell Science 125, 6176–6184 ß 2012. Published by The Company of Biologists Ltd doi: 10.1242/jcs.116533 ...
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... Fis1p TA by up to three amino acids did not inhibit mitochondrial targeting, arguing against a model in which TA length directs insertion of TAs to distinct organelles. Most importantly, positively charged residues were more acceptable at several positions within the membrane-associated domain of th ...
Interactions of Virus Proteins Within the Host Cell
Interactions of Virus Proteins Within the Host Cell

... Bacteria and Archaea. Viruses usually specifically infect a determined cell type, largely defined by the receptors they recognise. Canine parvovirus is a small, non-enveloped animal virus that infects cells in dividing cells, especially in puppies. PRD1 is a bacteriophage infecting a wide range of G ...
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... e) Janus family of non-receptor TK s also bind some receptors receptors i) growth hormone receptors ii) prola ctin receptors iii) some cytokine receptors ...
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Protein quality control and elimination of protein waste: The role of

... denatured proteins to keep them in a folding-competent state. Further folding is finally exerted by the Hsp70 system [68,69]. The cytosol also possesses small heat shock proteins (sHsps) belonging to the class of ATP-independent chaperones. In yeast, the two most prominent members are Hsp42 and Hsp26 ...
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Palmitoylation of influenza virus proteins

... the enzymology of acylation of HA. Members of the DHHC family, polytopic membrane proteins containing a DHHC (Asp-His-His-Cys) motif within one of their cytoplasmic domains, were shown to palmitoylate cellular proteins [17], but a DHHC protein that acylates influenza HA (or other viral proteins) has ...
The Plant Journal
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HER2

... • Connects the αC helix with the A-loop, stabilizing the helix in the active site • Bond is conserved among ErbB family members: K851-E734 (EGFR), K856-E739 (ErbB4) ...
Protein dynamics and proteolysis in plant vacuoles
Protein dynamics and proteolysis in plant vacuoles

... Plant cells cannot live without their vacuoles. The tissues and organs of a plant contain a wide variety of differentiated and specialized vacuoles—even a single plant cell can possess two or more types of vacuoles. Vacuolar proteins are encoded by nuclear genes and synthesized in the cytoplasm. The ...
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Protein phosphorylation



Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
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