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...

Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin

PloS one, 2016-04, Vol.11 (4), p.e0153495-e0153495

2016

Volltextzugriff (PDF)

Refolding Increases the Chaperone-like Activity of αH-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin

International journal of molecular sciences, 2023-08, Vol.24 (17), p.13473

2023

Volltextzugriff (PDF)

Fenton Reaction in vivo and in vitro. Possibilities and Limitations

Biochemistry (Moscow), 2024, Vol.89 (Suppl 1), p.S112-S126

Muranov, Konstantin O.

2024

Volltextzugriff (PDF)

Quantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albumin

PloS one, 2013-09, Vol.8 (9), p.e74367

2013

Volltextzugriff (PDF)

Biochemistry of Eye Lens in the Norm and in Cataractogenesis

Biochemistry (Moscow), 2022-02, Vol.87 (2), p.106-120

2022

Volltextzugriff (PDF)

Correction: Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

PloS one, 2014-01, Vol.9 (1)

2014

Volltextzugriff (PDF)

Oxidative damage to βL-crystallin in vitro by iron compounds formed in physiological buffers

Biophysical chemistry, 2023-03, Vol.294, p.106963-106963, Article 106963

2023

Volltextzugriff (PDF)

3D structure of the native α-crystallin from bovine eye lens

International journal of biological macromolecules, 2018-10, Vol.117, p.1289-1298

2018

Volltextzugriff (PDF)

Structural and functional alteration of human αA-crystallin after exposure to full spectrum solar radiation and preventive role of lens antioxidants

International journal of biological macromolecules, 2018-10, Vol.118, p.1120-1130

2018

Volltextzugriff (PDF)

Natural Dipeptides as Mini-Chaperones: Molecular Mechanism of Inhibition of Lens βL-Crystallin Aggregation

Current aging science, 2013-02, Vol.5 (3), p.236-241

2013

Volltextzugriff (PDF)

Does the Crowded Cell-like Environment Reduce the Chaperone-like Activity of α-Crystallin?

Biochemistry (Easton), 2011-12, Vol.50 (49), p.10607-10623

2011

Volltextzugriff (PDF)

Quantification of anti-aggregation activity of UV-irradiated α-crystallin

International journal of biological macromolecules, 2015-02, Vol.73, p.84-91

2015

Volltextzugriff (PDF)

Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones

Biopolymers, 2014-05, Vol.101 (5), p.504-516

2014

Volltextzugriff (PDF)

Effect of crowding and chaperones on self-association, aggregation and reconstitution of apophosphorylase b

International journal of biological macromolecules, 2013-09, Vol.60, p.69-76

2013

Volltextzugriff (PDF)

Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity

Biophysical chemistry, 2012-04, Vol.163-164, p.11-20

2012

Volltextzugriff (PDF)

Mechanism of aggregation of UV-irradiated β(L)-crystallin

Experimental eye research, 2011-01, Vol.92 (1), p.76-86

2011

Volltextzugriff (PDF)

Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin

Biophysical chemistry, 2010-02, Vol.146 (2), p.108-117

2010

Volltextzugriff (PDF)

Mechanism of thermal aggregation of yeast alcohol dehydrogenase I: role of intramolecular chaperone

Biochimica et biophysica acta, 2008-09, Vol.1784 (9), p.1286-1293

2008

Volltextzugriff (PDF)

Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of α-crystallin

European biophysics journal, 2009-06, Vol.38 (5), p.547-556

2009

Volltextzugriff (PDF)

Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Biophysical chemistry, 2007-02, Vol.125 (2), p.521-531

2007

Volltextzugriff (PDF)

Refolding Increases the Chaperone-like Activity of α[sub.H]-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin

International journal of molecular sciences, 2023-08, Vol.24 (17)

2023

Volltextzugriff (PDF)

Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase

International journal of biological macromolecules, 2009-06, Vol.44 (5), p.441-446

2009

Volltextzugriff (PDF)

Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

The Protein Journal, 2010, Vol.29 (1), p.11-25

2010

Volltextzugriff (PDF)

Mechanism of aggregation of UV-irradiated βL-crystallin

Experimental eye research, 2011-01, Vol.92 (1), p.76-86

2011

Volltextzugriff (PDF)

Mechanism of Chaperone-like Activity. Suppression of Thermal Aggregation of βL-Crystallin by α-Crystallin

Biochemistry (Easton), 2005-11, Vol.44 (47), p.15480-15487

2005

Volltextzugriff (PDF)

1 – 25 von 32

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(30)
Mit Volltextzugriff
(29)

Publikationsform

Artikel
(32)

Sprache

Englisch
(32)

Erscheinungsjahr

n.n

Thema

15 weitere anzeigen...

Weniger anzeigen...

Menü

Weitere Dienste

Einstellungen

Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin

Refolding Increases the Chaperone-like Activity of αH-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin

Fenton Reaction in vivo and in vitro. Possibilities and Limitations

Quantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albumin

Biochemistry of Eye Lens in the Norm and in Cataractogenesis

Correction: Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

Oxidative damage to βL-crystallin in vitro by iron compounds formed in physiological buffers

3D structure of the native α-crystallin from bovine eye lens

Structural and functional alteration of human αA-crystallin after exposure to full spectrum solar radiation and preventive role of lens antioxidants

Natural Dipeptides as Mini-Chaperones: Molecular Mechanism of Inhibition of Lens βL-Crystallin Aggregation

Does the Crowded Cell-like Environment Reduce the Chaperone-like Activity of α-Crystallin?

Quantification of anti-aggregation activity of UV-irradiated α-crystallin

Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones

Effect of crowding and chaperones on self-association, aggregation and reconstitution of apophosphorylase b

Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity

Mechanism of aggregation of UV-irradiated β(L)-crystallin

Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin

Mechanism of thermal aggregation of yeast alcohol dehydrogenase I: role of intramolecular chaperone

Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of α-crystallin

Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Refolding Increases the Chaperone-like Activity of α[sub.H]-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin

Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase

Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

Mechanism of aggregation of UV-irradiated βL-crystallin

Mechanism of Chaperone-like Activity. Suppression of Thermal Aggregation of βL-Crystallin by α-Crystallin

Suchergebnisse filtern