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FEBS Letters–384 journal homepage: www.FEBSLetters.org Polyglutamine shows a urea-like affinity for unfolded cytosolic protein Jeremy L. England a,⇑, Daniel Kaganovich b
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Document Date: 2011-07-05 13:31:24

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Morimoto / Bence / Khare / /

Company

Bevivino A.E. / Carl Icahn Laboratory / M.J. and Bottomley S.P. / Hasenbank / K.N. and Dokholyan N.V. / Elsevier B.V. / /

Country

United States / United Kingdom / Israel / /

Currency

pence / USD / /

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Facility

Princeton University / Hebrew University of Jerusalem / Sigler Institute / Alexander Silberman Institute of Life Sciences / Lewis-Sigler Institute / /

IndustryTerm

urea solutions / polyQ chain / chemical-induced denaturation / free energy / free energy difference / online version / quality control machinery / urea solution / disease gene product / polyQ chains / chemical denaturant / chemical denaturant urea / concentrated urea solution / toxic polyQexpanded gene product / /

MedicalCondition

disease / VHL tumor / Huntington’s disease / diseases / polyglutamine diseases / neurodegenerative diseases / truncated Machado-Joseph disease / /

Organization

Lewis-Sigler Institute / National Institute of Health / Lewis-Sigler Institute for Integrative Genomics / National Science Foundation / United States Department of Cell and Developmental Biology / Federation of European Biochemical Societies / Hebrew University of Jerusalem / Jerusalem / Princeton University / Alexander Silberman Institute of Life Sciences / /

Person

Scott / Miguel De la Rosa Keywords / Daniel Kaganovich / Lehrach / /

Position

G.P. / DG =RT / DGu =RT / Corresponding author / /

Product

IPOD / /

ProvinceOrState

South Dakota / New Jersey / N.F. / M.B. / Rhode Island / /

Technology

Genomics / molecular evolution / /

URL

www.FEBSLetters.org / /