Mutation biochemical

Kwon, B. S., Halaban, R., and Chintamaneni, C. (1989a). Molecular basis of mouse Himalayan mutation. Biochem. Biophys. Res. Commun. 161 252-260. 

Yen, C.-J., Beamer, B. A., Negri, C., Silver, K., Brown, K. A., Yarnell, D. P., Burns, D. K., Roth, J., and Shuldiner, A. R. (1997). Molecular Scanning of the Human Peroxisome Proliferator Activated Receptor y Gene in Diabetic Caucasians Identification of a Prol2Ala PPARy2 Missense Mutation. Biochem. Biophys. Res. Commun. 241, 270-274. 

Folkesson R, MaUdewicz K, Kloskowska E, Nilsson T, Popova E, Bogdanovic N, Ganten U, Ganten D, Bader M, Winblad B, Benedikz E (2007) A transgenic rat expressing human APP with the Swedish Alzheimer s disease mutation. Biochem Biophys Res Commun 358 777-782 Foster AC, CoUins JF, Schwarcz R (1983) On the excitotoxic properties of quinolinic acid, 2,3-piperidine dicarboxylic adds and structurally related compounds. Neuropharmacology 22 1331-1342... 

Parfait B, Rustin P, Munnich A, Rotig A. Coamplification of nuclear pseudogenes and assessment of heteroplasmy of mitochondrial DNA mutations. Biochem Biophys Res Commun 1998 247 57-9. 

Brown DR (2000) Altered toxicity of the prion protein peptide PrP106-126 carrying the Ala (117) -> Val mutation. Biochem J 346 785... 

Suganami T, Mieda T, Itoh M, Shimoda Y, Kamei Y, Ogawa Y. Attenuation of obesity-induced inflammation in C3H/HeJ miee earrying a Toll-like receptor4 mutation. Biochem Biophys Res Commun. 2007, 354 45-9. 

Salama I, Hinderlich S, Shlomai Z et al. (2005) No overall hyposialylation in hereditary inclusion body myopathy myoblasts carrying the homozygous M712T GNB mutation. Biochem Biophys Res Commun 328, 221-226. 

Equations (5)-(8) assume that the energy functions (7 and Ub operate on the same conformation space i.e., A and B must have the same number N of degrees of freedom. In practice, this almost always implies that A and B have the same number of atoms or particles. Most biochemical changes of interest (e.g., point mutations of a protein) do not obey this requirement, but they can often be made to do so artificially through the use of dummy atoms (see below). 

Alber, T. Mutational effects on protein stability. Annu. Rev. Biochem. 58 765-798, 1989. 

The biflagellate unicellular green alga Chlamydomonas reinhardtii is prone to spontaneous mutations that produce deficiencies in flagellar proteins and MT assembly, substructure, and function. Viable mutants that are either nonmotile or slow moving can be isolated and analyzed biochemically and morphologically, thereby establishing structure-function correlations. Electron microscopic analysis... 

Kitchin KT, Brown JL, Kulkami AP. 1992. Predictive assay for rodent carcinogenicity using in vivo biochemical parameters Operational characteristics and complementarity. Mutat Res 266 253-272. 

Myal Y., Blanchard A., Watson P., CoRRiN M., Shiu R., Iwasiow B. Detection of genetic point mutations by peptide nucleic acid-mediated polymerase chain reaction clamping using paraffin-embedded specimens. Anal. Biochem. 2000 285 169-172. 

Dewald G, Bork K Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal Cl inhibitor. Biochem Biophys Res Commun 2006 343 1286-1289. 

Hayakawa, M., Hattori, K., Sugiyama, S. and Ozawa, T. (1992). Age-associated oxygen damage and mutations in mitochondria] DNA in human hearts. Biochem. Biophys. Res. Commun. 189, 979-985. 

To date, 15 GPI variants have been analyzed at the molecular level, and 16 mis-sense mutations, 1 nonsense mutation, and 1 splicing mutation due to a four-nucleotide deletion have been reported (Fig. 7) (B9, F13, K14, Wl, XI). The GPI gene mutations were heterogeneous, although most GPI variants had common biochemical characteristics such as heat instability and normal kinetic properties. We have determined the molecular abnormalities of four homozygous variants, GPI Matsumoto, GPI Iwate, GPI Narita, and GPI Fukuoka (K14). GPI Narita has a homozygous mutation from A to G at position 1028 (343 Gin to Arg), and the same mutation was reported in an Italian patient, GPI Moscone (B9). The substituted Gin is adjacent to the reported active site residue, 341 Asp. Homozygous missense mutations, C to T at position 14 (5 Thr to lie) and C to T at position 671 (224 Thr to Met) have been identified in GPI Matsumoto and GPI Iwate, respectively. GPI... 

Acatalasemia is a rare hereditary deficiency of tissue catalase and is inherited as an autosomal recessive trait (03). This enzyme deficiency was discovered in 1948 by Takahara and Miyamoto (Tl). Two different types of acatalasemia can be distinguished clinically and biochemically. The severe form, Japanese-type acatalasemia, is characterized by nearly total loss of catalase activity in the red blood cells and is often associated with an ulcerating lesion of the oral cavity. The asymptomatic Swiss-type acatalasemia is characterized by residual catalase activity with aberrant biochemical properties. In four unrelated families with Japanese-type acatalasemia, a splicing mutation due to a G-to-A transition at the fifth nucleotide in intron 4 was elucidated (K20, W5). We have also determined a single base deletion resulting in the frameshift and premature translational termination in the Japanese patient (HI6). 

M5. Maekawa, M Sudo, K., Kanno, T., and Li, S. S.-L., Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency. Biochem. Biophys. Res. Commun. 168, 677-682 (1990). 

Ookawara, T., Dave, V., Willems, P Martin, J.-J., de Barsy, T., Matthys, E., and Yoshida, A., Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant. Arch. Biochem. Biophys. 327, 35-40 (1996). 

Ul. Uenaka, R., Nakajima, H., Noguchi, T., Imamura, K Hamagauchi, T Tomita, K Yamada, K., Kuwajima, M Kono, N Tanaka, T and Matsuzawa, Y., Compound heterozygous mutations affecting both hepatic and erythrocyte isozymes of pyruvate kinase. Biochem. Biophys. Res. Commun. 208,991-998 (1995). 

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