UNIVERSI
TÄ
TS-
BIBLIOTHEK
P
ADERBORN
Anmelden
Menü
Menü
Start
Hilfe
Blog
Weitere Dienste
Neuerwerbungslisten
Fachsystematik Bücher
Erwerbungsvorschlag
Bestellung aus dem Magazin
Fernleihe
Einstellungen
Sprache
Deutsch
Deutsch
Englisch
Farbschema
Hell
Dunkel
Automatisch
Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist
gegebenenfalls
nur via VPN oder Shibboleth (DFN-AAI) möglich.
mehr Informationen...
Universitätsbibliothek
Katalog
Suche
Details
Zur Ergebnisliste
Ergebnis 5 von 5
Datensatz exportieren als...
BibTeX
A cell adhesion peptide from foot-and-mouth disease virus can direct cell targeted delivery of a functional enzyme
Biotechnology and bioengineering, 1998-08, Vol.59 (3), p.294-301
Villaverde, Antonio
Feliu, Jordi X.
Arís, Anna
Harbottle, Richard P.
Benito, Antoni
Coutelle, Charles
1998
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Villaverde, Antonio
Feliu, Jordi X.
Arís, Anna
Harbottle, Richard P.
Benito, Antoni
Coutelle, Charles
Titel
A cell adhesion peptide from foot-and-mouth disease virus can direct cell targeted delivery of a functional enzyme
Ist Teil von
Biotechnology and bioengineering, 1998-08, Vol.59 (3), p.294-301
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
1998
Quelle
Wiley Online Library - AutoHoldings Journals
Beschreibungen/Notizen
The G‐H loop of foot‐and‐mouth disease virus is a disordered protrusion of the VP1 protein exposed on the virion surface. This short stretch includes an arginine‐glycine‐aspartic acid tripeptide, a recognized integrin‐binding motif, which is responsible for cell attachment and infection. Eight copies of a peptide reproducing the amino acid sequence of this FMDV ligand have been displayed in solvent‐exposed regions on an enzymatically active recombinant β‐galactosidase. This viral peptide segment enables the chimeric enzyme to bind mammalian cell lines with different efficiencies, probably depending on the number of suitable cell receptors present on each of them. Moreover, it also promotes the internalization of the attached enzyme, which is transiently active inside the cells. These results suggest further exploration of the potential use of short adhesion peptides of viral origin as cell attachment tags to direct the targeted delivery of both genes and enzymes, instead of whole, infectious viruses. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:294–301, 1998.
Sprache
Englisch
Identifikatoren
ISSN: 0006-3592
eISSN: 1097-0290
DOI: 10.1002/(SICI)1097-0290(19980805)59:3<294::AID-BIT5>3.0.CO;2-6
Titel-ID: cdi_proquest_miscellaneous_69186230
Format
–
Schlagworte
Amino Acid Sequence
,
Aphthovirus
,
beta-Galactosidase - biosynthesis
,
beta-Galactosidase - genetics
,
beta-Galactosidase - metabolism
,
Biological and medical sciences
,
Bioreactors
,
Biotechnology
,
Capsid - biosynthesis
,
Capsid - chemistry
,
Capsid Proteins
,
Cell Adhesion
,
cell binding
,
Escherichia coli - enzymology
,
FMDV
,
Fundamental and applied biological sciences. Psychology
,
Genetic engineering
,
Genetic Engineering - methods
,
Genetic technics
,
Genetic Vectors
,
integrins
,
internalization
,
Ligands
,
Methods. Procedures. Technologies
,
Miscellaneous
,
Models, Molecular
,
Molecular Sequence Data
,
Protein Conformation
,
Recombinant Fusion Proteins - biosynthesis
,
Recombinant Fusion Proteins - chemistry
,
Recombinant Fusion Proteins - metabolism
,
Recombinant Proteins
,
RGD
,
Synthetic digonucleotides and genes. Sequencing
,
β-galactosidase
Weiterführende Literatur
Empfehlungen zum selben Thema automatisch vorgeschlagen von
bX