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Protein mutations

Wilcox, S. K. Cavey, G. S. Pearson, J. D. Single ribosomal protein mutations in antibiotic-resistant bacteria analyzed by mass spectrometry. Antimicrob. Agents Chemother. 2001,45,3046-3055. [Pg.201]

Presen m genes encode enzymes involved in cleaving BAPP protein mutations produce early onset fonn... [Pg.343]

Novel PS-related famihes of proteins (IMPAS/PSH/signal peptide peptidases [SPSs]) have been identified (163). Intramembrane protease-associated or intramembrane protease aspartic protein Impas 1 (1MP1)/SPS induces intramembranous cleavage of PSl holoprotein in cultured cells coexpressing these proteins. Mutations in evolutionary invariant sites in hlMPl or specific y-secretase inhibitors abolish the hlMPl-mediated endoproteolysis of PSl. In contrast, AD-like mutations in neither hlMPl nor PSl substrate abridge the PSl cleavage (163). [Pg.239]

Much that is occurring with genes, proteins, mutations, chain folding, and other important molecular biology-related efforts is polymer chemistry applied to natural systems, and we have much to offer to assist in these ventures. [Pg.355]

The LI loop winds aroimd the P and y phosphates it is also know as the P loop. Glyl2 is located in the LI loop this amino acid is frequently mutated in oncogenic mutants of Ras protein (mutation hotspot ). [Pg.329]

The ATM protein has been identified as an important member of a reaction chain that leads from detection of DNA damage to activation of the p53 protein. Mutations of the ATM protein are causally associated with the disease ataxia telangiectasia, thus the name ATM (ataxia telangiectasia mutated). The ATM protein has protein kinase activity and is counted as a member of the PI3-kinase family, due to sequence homologies (review Canman et al., 1998). The p53 protein is phosphorylated at Serl5 by ATM kinase (Canman et al., 1998) and it is assumed that this phosphorylation contributes to activation of the p53 protein. The ATM protein is preceded by other protein kinases that are directly or indirectly activated by DNA damage and pass this signal on to the p53 protein via the ATM protein. [Pg.448]

Genetic engineering. The X-ray structures are known for many hydrolases, allowing for modeling of the substrate in the active site as well as structurally based, random or rational protein mutation to magnify or invert enantioselectivity. An example of the latter is provided by the rational design of a mutant of Candida antarctica lipase (CALB), which, instead of the wild-type R-selectivity, displayed... [Pg.82]

Fig. 4.5.4 Identification of mutations in the transferrin protein by neuraminidase treatment. Unusual patterns in the IEF of serum transferrin might lead to pitfalls in CDG diagnostics. These varying patterns are often due to mutations of charged amino acids in the protein backbone of the transferrin molecule, which might lead, for example, to an accumulation of trisialo transferrin bands (lane 3, indicated by a question mark). Further investigations are carried out by cleaving off charged sialic acid monosaccharide moieties from transferrin-linked oligosaccharides by neuraminidase treatment, followed by IEF and transferrin antibody staining. In the case of protein mutations, additional bands below (lane 4) or above (not shown) the desialylated transferrin form appear... Fig. 4.5.4 Identification of mutations in the transferrin protein by neuraminidase treatment. Unusual patterns in the IEF of serum transferrin might lead to pitfalls in CDG diagnostics. These varying patterns are often due to mutations of charged amino acids in the protein backbone of the transferrin molecule, which might lead, for example, to an accumulation of trisialo transferrin bands (lane 3, indicated by a question mark). Further investigations are carried out by cleaving off charged sialic acid monosaccharide moieties from transferrin-linked oligosaccharides by neuraminidase treatment, followed by IEF and transferrin antibody staining. In the case of protein mutations, additional bands below (lane 4) or above (not shown) the desialylated transferrin form appear...
Drury, L.S. Buxton, R.S. Identification and sequencing of the Escherichia coli cet gene which codes for an inner membrane protein, mutation of which causes tolerance to colicin E2. Mol. Microbiol., 2, 109-119 (1988)... [Pg.460]

Smith SJ, Li Y, Whitley R, et al. Molecular epidemiology of p53 protein mutations in workers exposed to vinyl chloride. Am J Epidemiol 1998 147 302-308. [Pg.404]

Palek, J., and Jarolim, P. (1993). Clinical expression and laboratory detection of red blood cell membrane protein mutations. Semin. Hematol. 30, 249-283. [Pg.242]

Errico, A., Ballabio, A., and Rugarli, E. I. (2002). Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics. Hum. Mol. Genet. 11, 153-163. [Pg.292]

Chartier-Harlin, M. C., Crawford, R, Hamandi, K., Mullan, M., Goate, A., et al. (1991) Screening for the beta-amyloid precursor protein mutation (APP717 Val— lie) in extended pedigrees with early onset Alzheimer s disease. Neurosci Lett 129, 134-135. [Pg.341]

Fig. 1. Putative location of podocyte proteins mutated in different types of familial nephrotic syndrome. Fig. 1. Putative location of podocyte proteins mutated in different types of familial nephrotic syndrome.
Gene a.k.a. Full name (Predicted) protein Mutation Reference... [Pg.654]


See other pages where Protein mutations is mentioned: [Pg.201]    [Pg.1284]    [Pg.181]    [Pg.263]    [Pg.137]    [Pg.301]    [Pg.69]    [Pg.672]    [Pg.321]    [Pg.334]    [Pg.63]    [Pg.723]    [Pg.45]    [Pg.246]    [Pg.94]    [Pg.371]    [Pg.48]    [Pg.738]    [Pg.23]    [Pg.805]    [Pg.574]    [Pg.1690]    [Pg.619]    [Pg.612]    [Pg.457]    [Pg.458]    [Pg.268]    [Pg.17]    [Pg.361]    [Pg.265]    [Pg.376]   


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Amyloid precursor protein mutations

Ataxia telangiectasia mutated proteins

Ataxia-telangiectasia-mutated protein kinase

Frameshift mutations, protein

Frameshift mutations, protein synthesis

Genes mutations encoding proteins

Human prion protein pathogenic mutations

Insertions protein synthesis mutations

Mechanisms of protein mutation

Missense mutations, protein

Missense mutations, protein synthesis

Mitochondrial membrane proteins, mutations

Mutational studies, protein aggregation

Mutations protein synthesis

Myelin sheath protein mutations

Nonsense mutations, protein

Nonsense mutations, protein synthesis

Point mutations protein synthesis

Prion protein human disease-associated mutations

Prion proteins genetic mutations

Protein Engineering mutations

Protein point mutation

Protein-Ligand Interactions mutated

Protein-Ligand Interactions mutations

Protein-based machines mutations

Proteins mutation probability matrices

Repair proteins mutated mismatched

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