Library Efficiency™ DH5α Competent Cells - Citations

Library Efficiency™ DH5α Competent Cells - Citations

View additional product information for Library Efficiency™ DH5α Competent Cells - Citations (18263012)

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Citations & References
Abstract
Changes in the mechanism of DNA integration in vitro induced by base substitutions in the HIV-1 U5 and U3 terminal sequences.
Authors Brin Elena; Leis Jonathan;
JournalJ Biol Chem
PubMed ID11788585
'We have reconstituted concerted human immunodeficiency virus type 1 (HIV-1) integration with specially designed mini-donor DNA, a supercoiled plasmid acceptor, purified bacterial-derived HIV-1 integrase (IN), and host HMG-I(Y) protein (Hindmarsh, P., Ridky, T., Reeves, R., Andrake, M., Skalka, A. M., and Leis, J. (1999) J. Virol. 73, 2994-3003). Integration in ... More
Identification and characterization of two cation binding sites in the integrin beta 3 subunit.
Authors Cierniewska-Cieslak Aleksandra; Cierniewski Czeslaw S; Blecka Kamila; Papierak Malgorzata; Michalec Lidia; Zhang Li; Haas Thomas A; Plow Edward F;
JournalJ Biol Chem
PubMed ID11796735
'The midsegment of the beta(3) subunit has been implicated in the ligand and cation binding functions of the beta(3) integrins. This region may contain a metal ion-dependent adhesion site (MIDAS) and fold into an I domain-like structure. Two recombinant fragments, beta(3)-(95-373) and beta(3)-(95-301), were expressed and found to bind fibrinogen. ... More
Requirement for either a host- or pectin-induced pectate lyase for infection of pisum sativum by nectriahematococca.
AuthorsRogers LM, Kim YK, Guo W, Gonzalez-Candelas L, Li D, Kolattukudy PE
JournalProc Natl Acad Sci U S A
PubMed ID10931947
Fungal pathogens usually have multiple genes that encode extracellular hydrolytic enzymes that may degrade the physical barriers in their hosts during the invasion process. Nectria hematococca, a plant pathogen, has two inducible pectate lyase (PL) genes (pel) encoding PL that can help degrade the carbohydrate barrier in the host. pelA ... More
Molecular determinants of high affinity binding to group III metabotropic glutamate receptors.
Authors Rosemond Erica; Peltekova Vanya; Naples Mark; Thøgersen Henning; Hampson David R;
JournalJ Biol Chem
PubMed ID11744707
The amino-terminal domain containing the ligand binding site of the G protein-coupled metabotropic glutamate receptors (mGluRs) consists of two lobes that close upon agonist binding. In this study, we explored the ligand binding pocket of the Group III mGluR4 receptor subtype using site-directed mutagenesis and radioligand binding. The selection of ... More