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Protein function modulation

Phosphorylation is the reversible process of introducing a phosphate group onto a protein. Phosphorylation occurs on the hydroxyamino acids serine and threonine or on tyrosine residues targeted by Ser/Thr kinases and tyrosine kinases respectively. Dephosphorylation is catalyzed by phosphatases. Phosphorylation is a key mechanism for rapid posttranslational modulation of protein function. It is widely exploited in cellular processes to control various aspects of cell signaling, cell proliferation, cell differentiation, cell survival, cell metabolism, cell motility, and gene transcription. [Pg.976]

The functioning of heterotrimeric G proteins is modulated by other proteins 340... [Pg.335]

How does PARP-Fs role as a nucleosome-binding protein and modulator of chromatin structure, which is evident under normal physiological conditions, impact PARP-1-dependent DNA repair, cell death, and inflammatory response pathways, which occur under pathophysiological conditions A number of different scenarios are possible. For example, PARP-l s chromatin-dependent activities may be critical for its function as a DNA repair protein, since the repair of genomic DNA must occur in the context of chromatin. In addition, nucleosome-stimulated autoPARylation may play a role in depleting cellular NAD+ pools in response to cellular stresses. Furthermore, PARP-Fs chromatin-dependent activities may help to regulate the expression of immune and inflammatory response genes. These possibilities will need to be examined in the future. [Pg.61]

In chemogenomics and drug discovery, the most challenging task is to find small molecule modulators of protein function that specifically modulate the protein function of interest. Combinatorial chemistry has emerged as a powerful tool to address this problem by generation of large compound... [Pg.59]

Compound libraries as sources for small molecule modulators of protein function... [Pg.60]

The ligand binding or catalytic sites are the most relevant parts of a protein domain for the development of small molecules as modulators of protein function. There is evidence that proteins with conserved folds often also have their functional sites on the same topological location. In some cases a remarkable conservatism in functional sites can be observed. This is true for the example described later in this review on similarity of Cdc25A phosphatase, acetylcholinesterase (AChE) and 1 Ifl-hydroxysteroid dehydrogenases (1 l HSD) (Fig. 9). Nevertheless, it should be stressed that the correlation patterns of amino acid sequence, protein fold and protein function remain a matter of debate. Moreover, a vast number of specific functions can be carried out by the limited number of protein domains due to the high amino acid diversity of proteins with similar folds. " ... [Pg.70]

Newton AC, Johnson JE (1998) Protein kinase C a paradigm for regulation of protein function by two membrane-targeting modules. Biochim Biophys Acta 1376 155-172... [Pg.84]

An alternative way to validate the critical function eliciting the disease-relevant phenotype is the use of tool modulators these can be small molecules, peptides, or antibodies that may not have the properties to be considered a drug, but may display sufficient potency and selectivity to be used to interrogate the specific protein function in the relevant system. Such tools, however, are rarely available with the required characteristics to allow for a robust interpretation of the experiment. The exception is represented by the... [Pg.10]

Table 5.7. Cytokines for which soluble receptors have been detected in biological fluids. The exact functional role played by these binding proteins, in modulating cytokine activity, remains to be elucidated in most cases... Table 5.7. Cytokines for which soluble receptors have been detected in biological fluids. The exact functional role played by these binding proteins, in modulating cytokine activity, remains to be elucidated in most cases...
Sandanaraj BS, Vutukuri DR, Simard JM, Klaikherd A, Hong R, Rotello VM, Thayumanavan S. Noncovalent modification of chymotrypsin surface using an amphiphilic polymer scaffold implications in modulating protein function. J Am Chem Soc 2005 127 10693-10698. [Pg.35]

Fig. 3 A AGS proteins isolated in yeast-based functional screen G-protein signaling modulator (GPSM) as named by the Human Genome Nomenclature Committee. The major sites of action of AGS proteins in the context of the G-protein activation-deactivation cycle are indicated B on the right. (GPR G-protein regulatory, GEF guanine nucleotide exchange factor, GDI guanine nucleotide dissociation inhibitor, GPCR G-protein coupled receptor)... Fig. 3 A AGS proteins isolated in yeast-based functional screen G-protein signaling modulator (GPSM) as named by the Human Genome Nomenclature Committee. The major sites of action of AGS proteins in the context of the G-protein activation-deactivation cycle are indicated B on the right. (GPR G-protein regulatory, GEF guanine nucleotide exchange factor, GDI guanine nucleotide dissociation inhibitor, GPCR G-protein coupled receptor)...
As discussed for N-myristoylation and S-prenylation, even S-acylation of proteins with a fatty acid which in the vast majority of cases is the C16 0 palmitic acid, plays a fundamental role in the cellular signal-transduction process (Table l). 2-5 14 While N-myristoylation and S-prenylation are permanent protein modifications due to the amide- and sulfide-type linkage, the thioester bond between palmitic acid and the peptide chain is rather labile and palmi-toylation is referred to as a dynamic modification. 64 This reversibility plays a crucial role in the modulation of protein functions since the presence or absence of a palmitoyl chain can determine the membrane localization of the protein and can also be used to regulate the interactions of these proteins with other proteins. Furthermore, a unique consensus sequence for protein palmitoylation has not been found, in contrast to the strict consensus sequences required for N-myristoylation and S-prenylation. Palmitoylation can occur at N- or C-terminal parts of the polypeptide chain depending on the protein family and often coexists with other types of lipidation (see Section 6.4.1.4). Given the diversity of protein sequences... [Pg.341]


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Functional Module

Functional protein-functionalized

Functionality protein

Modulating function

Modulation functions

Module function

Protein modulating

Protein module

Protein, proteins modulation

Proteins functioning

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