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1

Prions - the new infectious agent

100%
Gogiel T.
Biotechnologia
|
1998
|
issue 3
35-51
EN
Prions are devoid of nucleic acids and they are composed mainly or exclusively of protein PrPSC, that is a conformational variant of the normal cellular prion protein PrPC, encoded by a chromosomal gene. Conversion of PrPC into PrPSC is a posttranslational process which is accompanied by the acquisition of high b-sheet content. Human prion diseases may be of sporadic, genetic or infectious origin. Human activity caused a 'mad cow disease' epidemic, iatrogenic Creutzfeldt-Jakob disease (CJD), and lately, a new variant of CJD, which is thought to be a result of transmission of bovine prions to humans. Prion diseases are always fatal, and there is a need to develop effective methods of prevention and therapy for these disorders.
2

New collagenous proteins: FACITs, transmembrane collagens and multiplexins

63%
Gogiel T., Bankowski E.
Postępy Higieny i Medycyny Doświadczalnej
|
2001
|
vol. 55
|
issue 1
133-156
EN
Collagens are the main components of the extracellular matrix and they constitute about 30% of total body protein. Each collagen molecule consists of three polypeptide chains that intertwine in one or more places into triple helical domains, a very rare structure in other proteins. Nineteen collagen types have been described to date and those forming banded fibrils are the most abundant. In the last decade new collagenous proteins were discovered that have been classified into three distinct groups: fibril-associated collagens with interrupted triple helices (FACITs), transmembrane collagens and multiplexins. FACITs appear to connect collagen fibrils to other matrix components or cells. Transmembrane collagens have intracellular domains and they participate in cell adhesion and probably in signal transduction. Multiplexins are situated mainly in basement membranes and contain sequences, which demonstrate features of angiogenesis inhibitors reducing the growth of neoplasmatic tumours.
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