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11 results for author:"Yerbury J.J." in Literature citations

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Clusterin facilitates in vivo clearance of extracellular misfolded proteins.

Wyatt A.R., Yerbury J.J., Berghofer P., Greguric I., Katsifis A., Dobson C.M., Wilson M.R.

Cell. Mol. Life Sci. 68:3919-3931(2011) · UniProtKB (1) · Mapped (8)

ANS binding reveals common features of cytotoxic amyloid species.

Bolognesi B., Kumita J.R., Barros T.P., Esbjorner E.K., Luheshi L.M., Crowther D.C., Wilson M.R., Dobson C.M., Favrin G., Yerbury J.J.

ACS Chem. Biol. 5:735-740(2010) · Mapped (10)

Structural characterization of clusterin-chaperone client protein complexes.

Wyatt A.R., Yerbury J.J., Wilson M.R.

J. Biol. Chem. 284:21920-21927(2009) · UniProtKB (1) · Mapped (4)

Extracellular chaperones modulate the effects of Alzheimer's patient cerebrospinal fluid on Abeta(1-42) toxicity and uptake.

Yerbury J.J., Wilson M.R.

Cell Stress Chaperones 15:115-121(2010) · Mapped (7)

alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species.

Yerbury J.J., Kumita J.R., Meehan S., Dobson C.M., Wilson M.R.

J. Biol. Chem. 284:4246-4254(2009) · Mapped (7)

Clusterin interacts with Paclitaxel and confer Paclitaxel resistance in ovarian cancer.

Park D.C., Yeo S.G., Wilson M.R., Yerbury J.J., Kwong J., Welch W.R., Choi Y.K., Birrer M.J., Mok S.C., Wong K.K.

Neoplasia 10:964-972(2008) · Mapped (5)

Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.

French K., Yerbury J.J., Wilson M.R.

Biochemistry 47:1176-1185(2008) · Mapped (2)

Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity.

Wilson M.R., Yerbury J.J., Poon S.

Mol Biosyst 4:42-52(2008) · Mapped (7)

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.

Yerbury J.J., Poon S., Meehan S., Thompson B., Kumita J.R., Dobson C.M., Wilson M.R.

FASEB J. 21:2312-2322(2007) · UniProtKB (1) · Mapped (4)

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

Kumita J.R., Poon S., Caddy G.L., Hagan C.L., Dumoulin M., Yerbury J.J., Stewart E.M., Robinson C.V., Wilson M.R., Dobson C.M.

J. Mol. Biol. 369:157-167(2007) · UniProtKB (1) · Mapped (6)

The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin.

Yerbury J.J., Rybchyn M.S., Easterbrook-Smith S.B., Henriques C., Wilson M.R.

Biochemistry 44:10914-10925(2005) · Mapped (5)

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