Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Reno Winter"'
Autor:
Anja Buttstedt, Reno Winter, Mirko Sackewitz, Gerd Hause, Franz-Xaver Schmid, Elisabeth Schwarz
Publikováno v:
PLoS ONE, Vol 5, Iss 11, p e15436 (2010)
Conversion of native proteins into amyloid fibrils is irreversible and therefore it is difficult to study the interdependence of conformational stability and fibrillation by thermodynamic analyses. Here we approached this problem by fusing amyloidoge
Externí odkaz:
https://doaj.org/article/19ad96eb79474f8eaa37aa639a63f9df
Publikováno v:
Protein Science. 24:1789-1799
The disease oculopharyngeal muscular dystrophy is caused by alanine codon trinucleotide expansions in the N-terminal segment of the nuclear poly(A) binding protein PABPN1. As histochemical features of the disease, intranuclear inclusions of PABPN1 ha
Publikováno v:
Journal of Biological Chemistry. 287:22662-22671
Oculopharyngeal muscular dystrophy is a late-onset disease caused by an elongation of a natural 10-alanine segment within the N-terminal domain of the nuclear poly(A)-binding protein 1 (PABPN1) to maximally 17 alanines. The disease is characterized b
Autor:
Jens, Liebold, Reno, Winter, Ralph, Golbik, Gerd, Hause, Christoph, Parthier, Elisabeth, Schwarz
Publikováno v:
Protein science : a publication of the Protein Society. 24(11)
The disease oculopharyngeal muscular dystrophy is caused by alanine codon trinucleotide expansions in the N-terminal segment of the nuclear poly(A) binding protein PABPN1. As histochemical features of the disease, intranuclear inclusions of PABPN1 ha
Publikováno v:
Biological chemistry. 394(8)
The prospective increase in life expectancy will be accompanied by a rise in the number of elderly people who suffer from ill health caused by old age. Many diseases caused by aging are protein misfolding diseases. The molecular mechanisms underlying
Autor:
Gerd Hause, Elisabeth Schwarz, Anja Buttstedt, Franz-Xaver Schmid, Mirko Sackewitz, Reno Winter
Publikováno v:
PLoS ONE
PLoS ONE, Vol 5, Iss 11, p e15436 (2010)
PLoS ONE, Vol 5, Iss 11, p e15436 (2010)
Conversion of native proteins into amyloid fibrils is irreversible and therefore it is difficult to study the interdependence of conformational stability and fibrillation by thermodynamic analyses. Here we approached this problem by fusing amyloidoge