scholarly journals Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

2011 ◽  
Vol 59 (8) ◽  
pp. 965-971 ◽  
Author(s):  
Aya Kojima ◽  
Yasunori Mabuchi ◽  
Motomi Konishi ◽  
Rika Okihara ◽  
Makoto Nagano ◽  
...  
Keyword(s):  
Prion Protein ◽  
Metal Binding ◽  
Protein Fragment ◽  
Binding Ability ◽  
Human Prion Protein ◽  
Metal Binding Ability

scholarly journals Multinuclear metal-binding ability of a carotene

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Shinnosuke Horiuchi ◽  
Yuki Tachibana ◽  
Mitsuki Yamashita ◽  
Koji Yamamoto ◽  
Kohei Masai ◽  
...  
Keyword(s):  
Metal Binding ◽  
Binding Ability ◽  
Metal Binding Ability

Metal binding ability of microbial natural metal chelators and potential applications

2020 ◽  
Vol 37 (9) ◽  
pp. 1262-1283 ◽  
Author(s):  
Marika Hofmann ◽  
Gerardo Retamal-Morales ◽  
Dirk Tischler
Keyword(s):  
Metal Binding ◽  
Metal Chelators ◽  
Binding Ability ◽  
Potential Applications ◽  
Metal Binding Ability

Metallophores can chelate many different metal and metalloid ions next to iron, make them valuable for many applications.

Novel insights into the metal binding ability of ZinT periplasmic protein from Escherichia coli and Salmonella enterica

2020 ◽  
Vol 49 (27) ◽  
pp. 9393-9403
Author(s):  
Denise Bellotti ◽  
Magdalena Rowińska-Żyrek ◽  
Maurizio Remelli
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
Salmonella Enterica ◽  
Periplasmic Protein ◽  
Binding Ability ◽  
Primary Metal ◽  
Metal Binding Ability

The characterization of Zn(ii) and Cu(ii) complexes with periplasmic protein ZinT suggests that the N-terminal histidine-rich loop plays a role as a primary metal scavenger and that ZinT can possibly transfer a Zn(ii) ion to ZnuA.

scholarly journals Sulphated glycosaminoglycans prevent the neurotoxicity of a human prion protein fragment

1998 ◽  
Vol 335 (2) ◽  
pp. 369-374 ◽  
Author(s):  
Mar PÉREZ ◽  
Francisco WANDOSELL ◽  
Camilo COLAÇO ◽  
Jesús AVILA
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Transmissible Spongiform Encephalopathies ◽  
Therapeutic Effects ◽  
Protein Fragment ◽  
Spongiform Encephalopathies ◽  
Sulphated Polysaccharides ◽  
Human Prion Protein ◽  
Sulphated Glycosaminoglycans

Although a number of features distinguish the disease isoform of the prion protein (PrPSc) from its normal cellular counterpart (PrPC) in the transmissible spongiform encephalopathies (TSEs), the neuropathogenesis of these diseases remains an enigma. The amyloid fibrils formed by fragments of human PrP have, however, been shown to be directly neurotoxic in vitro. We show here that sulphated polysaccharides (heparin, keratan and chondroitin) inhibit the neurotoxicity of these amyloid fibrils and this appears to be mediated via inhibition of the polymerization of the PrP peptide into fibrils. This provides a rationale for the therapeutic effects of sulphated polysaccharides and suggests a rapid in vitro functional screen for TSE therapeutics.

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