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11 results for author:"Doucette P.A." in Literature citations

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Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R.

Seetharaman S.V., Winkler D.D., Taylor A.B., Cao X., Whitson L.J., Doucette P.A., Valentine J.S., Schirf V., Demeler B., Carroll M.C. et al.

Biochemistry 49:5714-5725(2010) · Mapped (3)

Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.

Oztug Durer Z.A., Cohlberg J.A., Dinh P., Padua S., Ehrenclou K., Downes S., Tan J.K., Nakano Y., Bowman C.J., Hoskins J.L. et al.

PLoS ONE 4:e5004-e5004(2009) · Mapped (2)

Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.

Cao X., Antonyuk S.V., Seetharaman S.V., Whitson L.J., Taylor A.B., Holloway S.P., Strange R.W., Doucette P.A., Valentine J.S., Tiwari A. et al.

J. Biol. Chem. 283:16169-16177(2008) · UniProtKB (1)

Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein.

Potter S.Z., Zhu H., Shaw B.F., Rodriguez J.A., Doucette P.A., Sohn S.H., Durazo A., Faull K.F., Gralla E.B., Nersissian A.M. et al.

J. Am. Chem. Soc. 129:4575-4583(2007) · Mapped (2)

Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.

Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A., Valentine J.S., Hasnain S.S.

J. Mol. Biol. 356:1152-1162(2006) · UniProtKB (1)

Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.

Rodriguez J.A., Shaw B.F., Durazo A., Sohn S.H., Doucette P.A., Nersissian A.M., Faull K.F., Eggers D.K., Tiwari A., Hayward L.J. et al.

Proc. Natl. Acad. Sci. U.S.A. 102:10516-10521(2005) · Mapped (2)

Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.

Doucette P.A., Whitson L.J., Cao X., Schirf V., Demeler B., Valentine J.S., Hansen J.C., Hart P.J.

J. Biol. Chem. 279:54558-54566(2004) · Mapped (2)

Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants.

Hough M.A., Grossmann J.G., Antonyuk S.V., Strange R.W., Doucette P.A., Rodriguez J.A., Whitson L.J., Hart P.J., Hayward L.J., Valentine J.S. et al.

Proc. Natl. Acad. Sci. U.S.A. 101:5976-5981(2004) · UniProtKB (1)

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.

Elam J.S., Taylor A.B., Strange R., Antonyuk S., Doucette P.A., Rodriguez J.A., Hasnain S.S., Hayward L.J., Valentine J.S., Yeates T.O. et al.

Nat. Struct. Biol. 10:461-467(2003) · UniProtKB (1) · Mapped (1)

The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis.

Strange R.W., Antonyuk S., Hough M.A., Doucette P.A., Rodriguez J.A., Hart P.J., Hayward L.J., Valentine J.S., Hasnain S.S.

J. Mol. Biol. 328:877-891(2003) · Mapped (2)

An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate.

Elam J.S., Malek K., Rodriguez J.A., Doucette P.A., Taylor A.B., Hayward L.J., Cabelli D.E., Valentine J.S., Hart P.J.

J. Biol. Chem. 278:21032-21039(2003) · Mapped (2)

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