UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

Phototransduction: crystal clear

Trends in biochemical sciences (Amsterdam. Regular ed.), 2003-09, Vol.28 (9), p.479-487

2003

Volltextzugriff (PDF)

The Receptor-Bound “Empty Pocket” State of the Heterotrimeric G-Protein α-Subunit Is Conformationally Dynamic

Biochemistry (Easton), 2006-10, Vol.45 (43), p.12986-12997

2006

Volltextzugriff (PDF)

One-step purification of a functional, constitutively activated form of visual arrestin

Protein expression and purification, 2012-03, Vol.82 (1), p.55-60

2012

Volltextzugriff (PDF)

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein alpha -Subunit: NMR Analysis of GTP gamma S-Bound States

The Journal of biological chemistry, 2006-03, Vol.281 (11), p.7635-7648

2006

Volltextzugriff (PDF)

Building a stage for interhelical play in rhodopsin

Trends in biochemical sciences (Amsterdam. Regular ed.), 2003-08, Vol.28 (8), p.399-402

Abdulaev, Najmoutin G

2003

Volltextzugriff (PDF)

Light-Induced Exposure of the Cytoplasmic End of Transmembrane Helix Seven in Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1998-10, Vol.95 (22), p.12854-12859

1998

Volltextzugriff (PDF)

Designing Point Mutants to Detect Structural Coupling in a Heterotrimeric G Protein α-subunit by NMR Spectroscopy

Photochemistry and photobiology, 2009-03, Vol.85 (2), p.431-436

2009

Volltextzugriff (PDF)

Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein alpha-subunit

Journal of biomolecular NMR, 2005-05, Vol.32 (1), p.31-40

2005

Volltextzugriff (PDF)

Functionally Discrete Mimics of Light-activated Rhodopsin Identified through Expression of Soluble Cytoplasmic Domains

The Journal of biological chemistry, 2000-12, Vol.275 (50), p.39354-39363

2000

Volltextzugriff (PDF)

Examining Rhodopsin Folding and Assembly through Expression of Polypeptide Fragments (∗)

The Journal of biological chemistry, 1996-03, Vol.271 (13), p.7860-7867

1996

Volltextzugriff (PDF)

Grafting Segments from the Extracellular Surface of CCR5 onto a Bacteriorhodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity

Structure (London), 2002-04, Vol.10 (4), p.515-525

2002

Volltextzugriff (PDF)

Nucleoside Diphosphate Kinase from Bovine Retina: Purification, Subcellular Localization, Molecular Cloning, and Three-Dimensional Structure

Biochemistry (Easton), 1998-10, Vol.37 (40), p.13958-13967

1998

Volltextzugriff (PDF)

Folding and Assembly in Rhodopsin

The Journal of biological chemistry, 1999-07, Vol.274 (30), p.21437-21442

1999

Volltextzugriff (PDF)

Heterotrimeric G-protein α-Subunit Adopts a “Preactivated” Conformation When Associated with βγ-Subunits

The Journal of biological chemistry, 2005-11, Vol.280 (45), p.38071-38080

2005

Volltextzugriff (PDF)

Designing Point Mutants to Detect Structural Coupling in a Heterotrimeric G Protein [alpha]-subunit by NMR Spectroscopy[dagger]

Photochemistry and photobiology, 2009-03, Vol.85 (2), p.431

2009

Volltextzugriff (PDF)

Probing the molecular mechanism of heterotrimeric G‐protein signaling using high‐resolution NMR

The FASEB journal, 2007, Vol.21 (6), p.A982-A983

2007

Volltextzugriff (PDF)

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein Î±-Subunit

The Journal of biological chemistry, 2006-03, Vol.281 (11), p.7635

2006

Volltextzugriff (PDF)

Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein alpha-subunit: NMR analysis of GTPgammaS-bound states

The Journal of biological chemistry, 2006-03, Vol.281 (11), p.7635-7648

2006

Volltextzugriff (PDF)

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein α-Subunit

The Journal of biological chemistry, 2006-03, Vol.281 (11), p.7635-7648

2006

Volltextzugriff (PDF)

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein [alpha]-Subunit: NMR ANALYSIS OF GTP[gamma]S-BOUND STATES

The Journal of biological chemistry, 2006, Vol.281 (11), p.7635-7648

2006

Volltextzugriff (PDF)

Erratum to: “Phototransduction: crystal clear”[Trends Biochem. Sci. 28 (2003) 479–487]

Trends in biochemical sciences (Amsterdam. Regular ed.), 2003-10, Vol.28 (10), p.526-526

2003

Volltextzugriff (PDF)

Heterotrimeric G-protein Î±-Subunit Adopts a âPreactivatedâ Conformation When Associated with Î²Î³-Subunits

The Journal of biological chemistry, 2005-11, Vol.280 (45), p.38071

2005

Volltextzugriff (PDF)

Heterotrimeric G-protein alpha-subunit adopts a "preactivated" conformation when associated with betagamma-subunits

The Journal of biological chemistry, 2005-11, Vol.280 (45), p.38071-38080

2005

Volltextzugriff (PDF)

[4] Folding and assembly of rhodopsin from expressed fragments

Methods in Enzymology, 2000, Vol.315, p.59-70

2000

Volltextzugriff (PDF)

Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein [alpha]-subunit

Journal of biomolecular NMR, 2005-05, Vol.32 (1), p.31

2005

Volltextzugriff (PDF)

1 – 25 von 34

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(33)
Mit Volltextzugriff
(31)

Publikationsform

Artikel
(33)
Buchkapitel
(1)

Sprache

Englisch
(34)

Erscheinungsjahr

n.n

Menü

Weitere Dienste

Einstellungen

Phototransduction: crystal clear

The Receptor-Bound “Empty Pocket” State of the Heterotrimeric G-Protein α-Subunit Is Conformationally Dynamic

One-step purification of a functional, constitutively activated form of visual arrestin

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein alpha -Subunit: NMR Analysis of GTP gamma S-Bound States

Building a stage for interhelical play in rhodopsin

Light-Induced Exposure of the Cytoplasmic End of Transmembrane Helix Seven in Rhodopsin

Designing Point Mutants to Detect Structural Coupling in a Heterotrimeric G Protein α-subunit by NMR Spectroscopy

Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein alpha-subunit

Functionally Discrete Mimics of Light-activated Rhodopsin Identified through Expression of Soluble Cytoplasmic Domains

Examining Rhodopsin Folding and Assembly through Expression of Polypeptide Fragments (∗)

Grafting Segments from the Extracellular Surface of CCR5 onto a Bacteriorhodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity

Nucleoside Diphosphate Kinase from Bovine Retina: Purification, Subcellular Localization, Molecular Cloning, and Three-Dimensional Structure

Folding and Assembly in Rhodopsin

Heterotrimeric G-protein α-Subunit Adopts a “Preactivated” Conformation When Associated with βγ-Subunits

Designing Point Mutants to Detect Structural Coupling in a Heterotrimeric G Protein [alpha]-subunit by NMR Spectroscopy[dagger]

Probing the molecular mechanism of heterotrimeric G‐protein signaling using high‐resolution NMR

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein Î±-Subunit

Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein alpha-subunit: NMR analysis of GTPgammaS-bound states

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein α-Subunit

Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein [alpha]-Subunit: NMR ANALYSIS OF GTP[gamma]S-BOUND STATES

Erratum to: “Phototransduction: crystal clear”[Trends Biochem. Sci. 28 (2003) 479–487]

Heterotrimeric G-protein Î±-Subunit Adopts a âPreactivatedâ Conformation When Associated with Î²Î³-Subunits

Heterotrimeric G-protein alpha-subunit adopts a "preactivated" conformation when associated with betagamma-subunits

[4] Folding and assembly of rhodopsin from expressed fragments

Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein [alpha]-subunit

Suchergebnisse filtern