Results 31 to 40 of about 33,090 (271)

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett, Daggett, Valerie, van der Kamp, Marc W, Marc W. van der Kamp   +3 more
core   +1 more source

Evolutionary descent of prion genes from the ZIP family of metal ion transporters. [PDF]

PLoS ONE, 2009
In the more than twenty years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
Gerold Schmitt-Ulms, Sepehr Ehsani, Joel C Watts, David Westaway, Holger Wille   +4 more
doaj   +1 more source

Prion Protein Gene‐Deficient Cell Lines: Powerful Tools for Prion Biology [PDF]

Microbiology and Immunology, 2007
AbstractPrion diseases are zoonotic infectious diseases commonly transmissible among animals via prion infections with an accompanying deficiency of cellular prion protein (PrPC) and accumulation of an abnormal isoform of prion protein (PrPSc), which are observed in neurons in the event of injury and disease.
Akikazu, Sakudo, Takashi, Onodera, Kazuyoshi, Ikuta   +2 more
openaire   +2 more sources

Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]

, 2011
Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Valerie Daggett, Daggett, Valerie, van der Kamp, Marc W, Marc W. van der Kamp   +3 more
core   +1 more source

Absence of single nucleotide polymorphisms (SNPs) in the open reading frame (ORF) of the prion protein gene (PRNP) in a large sampling of various chicken breeds

BMC Genomics, 2019
Background Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP ...
Yong-Chan Kim, Sae-Young Won, Byung-Hoon Jeong   +2 more
doaj   +1 more source

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]

, 2003
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C., Weiss, S., Riley, M. L., Gauczynski, S., Leucht, C.   +4 more
core   +1 more source

Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells

Journal of General Virology, 2003
The susceptibility of prion protein gene (Prnp)-null cells to coxsackievirus B3 (CVB3) was investigated. Primary cultures of murinePrnp−/−brain cells were more sensitive to CVBs than corresponding cells from wild-type mice. The viral susceptibility of aPrnp-null cell line (HpL3-4) derived from the murine hippocampus was compared with that of two ...
NAKAMURA Y, SAKUDO A, SAEKI K, KANEKO T, MATSUMOTO Y, TONIOLO, ANTONIO, ITOHARA S, ONODERA T.   +7 more
openaire   +3 more sources

A novel protective prion protein variant that colocalizes with kuru exposure. [PDF]

, 2009
BACKGROUND: Kuru is a devastating epidemic prion disease that affected a highly restricted geographic area of the Papua New Guinea highlands; at its peak, it predominantly affected adult women and children of both sexes.
Whittaker, John, Mein, C., Shah, Paresh, Campbell, T., Whitfield, Jerome, Mein, Charles A, Whittaker, J., Alpers, Michael Philip, Hummerich, H., Collinge, J., Hummerich, Holger, Collinge, John, Uphill, J., Poulter, Mark, Beck, Jon, Al-Dujaily, Huda, Mead, S., Al-Dujaily, H., Alpers, Michael P, Beck, J., Verzilli, C., Mead, Simon, Verzilli, Claudio, Shah, P., Uphill, James, Poulter, M., Campbell, Tracy   +26 more
core   +1 more source

Loss of Octarepeats in Two Processed Prion Pseudogenes in the Red Squirrel, Sciurus vulgaris [PDF]

, 2010
The N-terminal region of the mammalian prion protein (PrP) contains an 'octapeptide' repeat which is involved in copper binding. This eight- or nine-residue peptide is repeated four to seven times, depending on the species, and polymorphisms in repeat ...
Rheede, T., Marlinda Hupkes, Timothy T. Kortum, Wilfried W. de Jong, Ole Madsen, de Jong, W.W., Kohlen, W., Madsen, O., Jong, W.W., de, Kortum, T.T., Wouter Kohlen, Teun van Rheede, Hupkes, H.   +12 more
core   +1 more source

Polymorphisms of the prion protein gene (PRNP) in a Korean population [PDF]

Journal of Human Genetics, 2004
Human prion protein gene (PRNP) has been considered to be involved in the susceptibility of humans to prion diseases. Polymorphisms of methionine (Met)/valine (Val) at codon 129 and of glutamic acid (Glu)/lysine (Lys) at codon 219 are thought to play an important role in susceptibility to sporadic, iatrogenic and variant Creutzfeldt-Jakob disease (CJD).
Byung-Hoon, Jeong, Jae-Hwan, Nam, Yun-Jung, Lee, Kyung-Hee, Lee, Myoung-Kuk, Jang, Richard I, Carp, Ho-Dong, Lee, Young-Ran, Ju, Sangmee, Ahn Jo, Keun-Yong, Park, Yong-Sun, Kim   +10 more
openaire   +2 more sources