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Functional analysis of the human CDC5L complex
Functional analysis of the human CDC5L complex

... stably associated with snRNPs. Therefore, snRNP proteins were puri®ed by af®nity chromatography on an anti-2,2,7trimethylguanosine cap column as described (Bach et al., 1990). Puri®ed snRNP proteins were separated by SDS±PAGE, transferred onto a nitrocellulose membrane and probed with both anti-CDC5 ...
The retinal pigment epithelium: a versatile partner in vision
The retinal pigment epithelium: a versatile partner in vision

... et al., 1987). This retinoid isom er is bound by yet another intracellular binding protein nam ed cellular retinal binding protein (CRA LBP, Futterm an et al., 1977). It presents the retinoid to an oxidoreductase (Saari and Bredberg, 1982), w hich converts it to the final product, 11 -cis retinaldeh ...
Interactions of liposomes and lipid-based carrier systems with blood
Interactions of liposomes and lipid-based carrier systems with blood

... clearance properties in the biological milieu. ...
Bacterial tail anchors can target to the mitochondrial outer
Bacterial tail anchors can target to the mitochondrial outer

... mitochondrial OM that would allow full integration of mitochondria within the ancestral ...
Diverse Effects of Mutations in the Signal Sequence on the Secretion of b-lactamase in Salmonella typhimurium.
Diverse Effects of Mutations in the Signal Sequence on the Secretion of b-lactamase in Salmonella typhimurium.

... latter mutants does produce mature protein, but at a very reduced rate. It thus appears that signalsequence mutations can affect more than one step in the secretion process, and that processing of the signal peptide is not required for the protein to be translocated (at least partially) across the i ...
Article A Model of Substitution Trajectories in
Article A Model of Substitution Trajectories in

... model of sequence evolution, which investigates the impact of interactions of sites across the protein sequence. An exhaustive description of all possible interactions is impossible for a sequence even of moderate length (L) as it requires to consider all 20L sequences in sequence space. This vast n ...
View Full Page PDF
View Full Page PDF

... Cys-Val-Ile-Met (231), is an example. When a protein carrying this signal is added to cells in the presence of radioactive mevalonate, a precursor of the farnesyl group, the protein will only be labeled if it reaches the cytosol or the nucleoplasm in the living cell (Fig. 1). PKC is also found only ...
SM-20, EGL-9, and the EGLN Family of Hypoxia
SM-20, EGL-9, and the EGLN Family of Hypoxia

... discovery of a novel family of prolyl hydroxylases, proline hydroxylation has emerged as an important component in the signaling pathway that regulates how cells adapt to changes in oxygen (O2) levels. When exposed to abnormally low O2 concentrations (i.e., hypoxia), multicellular organisms respond ...
The bacterial divisome: ready for its close-up
The bacterial divisome: ready for its close-up

... approximately 3 mm long by 1 mm wide, this represents at least 50 mass doublings, all the while continuing to extend the cell wall and membrane continuously, as well as replicate and segregate their nucleoids as visualized with DAPI staining. These multinucleate filaments indicated that the fts gene ...
A Nascent Membrane Protein Is Located Adjacent to
A Nascent Membrane Protein Is Located Adjacent to

... designated the signal sequence receptor by Wiedmann et al. (1987b) after being crosslinked using a short nascent chain (the arrested fragment, •70 amino acids long) with photoprobes located only in the signal sequence. Recent experiments have confirmed that nascent chains longer than the arrested fr ...
A Nascent Membrane Protein Is Located Adjacent to ER Membrane
A Nascent Membrane Protein Is Located Adjacent to ER Membrane

... designated the signal sequence receptor by Wiedmann et al. (1987b) after being crosslinked using a short nascent chain (the arrested fragment, •70 amino acids long) with photoprobes located only in the signal sequence. Recent experiments have confirmed that nascent chains longer than the arrested fr ...
Heterochromatin silencing at p53 target genes by a small viral protein.
Heterochromatin silencing at p53 target genes by a small viral protein.

... global transcriptional changes that drive oncogenic cellular and viral replication. ...
PROTEINS IN NUCLEOCYTOPLASMIC INTERACTIONS III
PROTEINS IN NUCLEOCYTOPLASMIC INTERACTIONS III

... isolated, and these amcbae had to be discarded. The latter amebac scrved to demonstrate that a good degree of synchrony between sisters was present. In the light of this synchrony, the remaining 19 undivided amebae were considered to have been in a late part of the G2 stage at the time of nuclear is ...
Proteomic analysis of nipple aspirate fluid from women with early
Proteomic analysis of nipple aspirate fluid from women with early

... Despite the widespread adoption of screening mammography, many breast cancers still escape detection at an early stage [1,2]. Identifying relevant biologic markers could improve our ability to diagnose early-stage breast cancer [3-7]. Compared with DNA analysis (genomics) and RNA analysis (expressio ...
WAVE/Scars in platelets
WAVE/Scars in platelets

... proteins, platelets express WASP, which becomes strongly tyrosine phosphorylated upon stimulation by collagen or following crosslinking of CD32, a low-affinity Fc receptor for immunoglobulin G (IgG).16 However, despite the very small size of platelets from patients with WAS, these small platelets un ...
Memory consolidation of Pavlovian fear conditioning: a cellular and
Memory consolidation of Pavlovian fear conditioning: a cellular and

... the capacity to become ‘autophosphorylated’, or persistently active in the absence of Ca2+ for a period of time following LTP induction53,54. While activated, αCaMKII and PKC can, in turn, phosphorylate a variety of target proteins. Autophosphorylation of αCaMKII on Thr286, for example, leads to α-a ...
Protein secretion and surface display in Gram
Protein secretion and surface display in Gram

... peptidoglycan associated polymers of proteins, polysaccharides or teichoic acids provide a barrier to protein translocation has not been studied. Using electron microscopy and immunogold labelling techniques in S. pyogenes, Rosch & Caparon [55,56] reported the accumulation of immune-reactive signals ...
Regulation of Heat Shock Response in Yeast and - E
Regulation of Heat Shock Response in Yeast and - E

... regulation of components of the heat shock response, a cellular stress defense mechanism present in all eukaryotes. The hallmark of the heat shock response is an increase in heat shock protein expression, which results from transcriptional activation accomplished by heat shock transcription factors. ...
PROTEINS IN NUCLEOCYTOPLASMIC
PROTEINS IN NUCLEOCYTOPLASMIC

... isolated, and these amcbae had to be discarded. The latter amebac scrved to demonstrate that a good degree of synchrony between sisters was present. In the light of this synchrony, the remaining 19 undivided amebae were considered to have been in a late part of the G2 stage at the time of nuclear is ...
Positive Regulation of IκB Kinase Signaling by Protein
Positive Regulation of IκB Kinase Signaling by Protein

... These functional results, together with data shown, further reinforce the model that PP2A binds to IKK, facilitating the induction of IκB kinase activity, targeted degradation of IκB, and release of NF-κB to its nuclear site of action. Instead, our studies support the idea that this region of IKKγ i ...
Small-molecule binding sites to explore new targets in the cancer
Small-molecule binding sites to explore new targets in the cancer

... The transcription factor HNF4A forms a homodimer complex to interact with DNA to control the expression of other genes. In the monomer structure, two binding sites were detected on the protein surface (Fig. S5D). One of these two sites is bound to a saturated fatty acid in multiple superimposed crys ...
The Plant Cell - Utrecht University Repository
The Plant Cell - Utrecht University Repository

... Progression through the eukaryotic cell cycle requires the coordinated destruction of essential cell cycle regulatory proteins by the ubiquitin-dependent pathway (reviewed by King et al., 1996). Protein ubiquitylation is a multistep enzymatic process (reviewed by Ciechanover et al., 2000) that invol ...
Bluetongue Virus Capsid Assembly and Maturation
Bluetongue Virus Capsid Assembly and Maturation

... following low-pH shock [25]. Following membrane destabilization, it is during this stage that the dissociation of VP5 from VP7 occurs, signifying the loss of the two outer protein layers and the completion of the uncoating process, releasing the core into the cytoplasm (Figure 2). These released cor ...
M6PRs are found in a subset of PC12 cell ISGs
M6PRs are found in a subset of PC12 cell ISGs

... controversy and the precise mechanisms involved in secretory granule formation are not yet known. Regarding the selection of secretory granule content proteins experimental data has been obtained, using endocrine and neuroendocrine cell systems, which supports two disparate, but not mutually exclusi ...
Theoretical studies of Membrane Proteins
Theoretical studies of Membrane Proteins

... Helix bundle membrane proteins are the class that has been studied most in this thesis. These proteins are present in the plasma membrane of prokaryotes and in all membranes of eukaryotic cells. In the rest of this thesis they will be referred to simply as membrane proteins. A helix bundle integral ...
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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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