Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein.

PloS one | 2010

The accumulation of protease resistant conformers of the prion protein (PrP(res)) is a key pathological feature of prion diseases. Polyanions, including RNA and glycosaminoglycans have been identified as factors that contribute to the propagation, transmission and pathogenesis of prion disease. Recent studies have suggested that the contribution of these cofactors to prion propagation may be species specific.

Pubmed ID: 20808809 RIS Download

Research resources used in this publication

None found

Additional research tools detected in this publication

Antibodies used in this publication

None found

Associated grants

None

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

This is a list of tools and resources that we have found mentioned in this publication.


Progen (tool)

RRID:SCR_006726

Antibody and density gradient media supplier.

View all literature mentions

RK 13 (tool)

RRID:CVCL_3155

Cell line RK 13 is a Spontaneously immortalized cell line with a species of origin Oryctolagus cuniculus

View all literature mentions

RK 13 (tool)

RRID:CVCL_3155

Cell line RK 13 is a Spontaneously immortalized cell line with a species of origin Oryctolagus cuniculus

View all literature mentions