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Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A

Biochemistry (Easton), 2017-06, Vol.56 (24), p.3029-3048

2017

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The domain 2 of the HCV NS5A protein is intrinsically unstructured

Protein and peptide letters, 2010-08, Vol.17 (8), p.1012-1018

2010

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Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B

The Journal of biological chemistry, 2009-05, Vol.284 (20), p.13589-13601

2009

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Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic α-Helical Propensity and Is a Substrate of Cyclophilin A

The Journal of biological chemistry, 2011-06, Vol.286 (23), p.20441-20454

2011

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Structural Studies of Self‐Assembled Subviral Particles: Combining Cell‐Free Expression with 110 kHz MAS NMR Spectroscopy

Angewandte Chemie International Edition, 2018-04, Vol.57 (17), p.4787-4791

International ed. in English, 2018

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Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins

Methods in molecular biology (Clifton, N.J.), 2017-01, Vol.1635, p.91

2017

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Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded

Biochemical and biophysical research communications, 2009-04, Vol.381 (4), p.634-638

2009

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Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus

Journal of biomolecular NMR, 2016-06, Vol.65 (2), p.87-98

2016

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Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins

Protein expression and purification, 2015-01, Vol.105, p.39-46

2015

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Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus

Protein expression and purification, 2015-12, Vol.116, p.1-6

2015

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Domain 3 of NS5A protein from the hepatitis C virus has intrinsic {alpha}-helical propensity and is a substrate of Cyclophilin A

The Journal of biological chemistry, 2011-04

2011

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The Domain 2 of the HCV NS5A Protein is Intrinsically Unstructured

Protein and peptide letters, 2010-05, Vol.999 (999), p.1-7

2010

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Strukturelle Untersuchung subviraler Partikel durch die Kombination von zellfreier Proteinherstellung mit 110 kHz MAS‐NMR‐Spektroskopie

Angewandte Chemie, 2018-04, Vol.130 (17), p.4877-4882

2018

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Glycosaminoglycans: major biological players

Glycoconjugate journal, 2017-06, Vol.34 (3), p.275-276

2017

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Strukturelle Untersuchung subviraler Partikel durch die Kombination von zellfreier Proteinherstellung mit 110 kHz MAS‐NMR‐Spektroskopie

Angewandte Chemie, 2018-04, Vol.130 (17), p.4877-4882

2018

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Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and BS

The Journal of biological chemistry, 2009-05, Vol.284 (20), p.13589-13601

2009

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Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A

The domain 2 of the HCV NS5A protein is intrinsically unstructured

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B

Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic α-Helical Propensity and Is a Substrate of Cyclophilin A

Structural Studies of Self‐Assembled Subviral Particles: Combining Cell‐Free Expression with 110 kHz MAS NMR Spectroscopy

Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded

Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus

Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins

Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic {alpha}-helical propensity and is a substrate of Cyclophilin A

The Domain 2 of the HCV NS5A Protein is Intrinsically Unstructured

Strukturelle Untersuchung subviraler Partikel durch die Kombination von zellfreier Proteinherstellung mit 110 kHz MAS‐NMR‐Spektroskopie

Glycosaminoglycans: major biological players

Strukturelle Untersuchung subviraler Partikel durch die Kombination von zellfreier Proteinherstellung mit 110 kHz MAS‐NMR‐Spektroskopie

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and BS

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