UB Paderborn / Katalog / Suche / in CDI

1 – 25 von 55

Sortiert nach

Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils

International journal of molecular sciences, 2021-05, Vol.22 (9), p.4349

2021

Volltextzugriff (PDF)

Detection of Fibril Nucleation in Micrometer-Sized Protein Condensates and Suppression of Sup35NM Fibril Nucleation by Liquid–Liquid Phase Separation

Analytical chemistry (Washington), 2023-07, Vol.95 (26), p.9855-9862

2023

Volltextzugriff (PDF)

Short disordered protein segment regulates cross-species transmission of a yeast prion

Nature chemical biology, 2020-07, Vol.16 (7), p.756

2020

Volltextzugriff (PDF)

Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin

The Journal of biological chemistry, 2005-09, Vol.280 (38), p.32843-32848

2005

Volltextzugriff (PDF)

Molecular basis for diversification of yeast prion strain conformation

Proceedings of the National Academy of Sciences - PNAS, 2018-03, Vol.115 (10), p.2389-2394

2018

Volltextzugriff (PDF)

Growth of β2-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

Biochemical journal, 2008-12, Vol.416 (2), p.307-315

2008

Volltextzugriff (PDF)

The Intrachain Disulfide Bond of β2-Microglobulin Is Not Essential for the Immunoglobulin Fold at Neutral pH, but Is Essential for Amyloid Fibril Formation at Acidic pH

Journal of biochemistry (Tokyo), 2002-01, Vol.131 (1), p.45-52

2002

Volltextzugriff (PDF)

Amyloidogenic synthetic peptides of β2-microglobulin—a role of the disulfide bond

Biochemical and biophysical research communications, 2003-04, Vol.304 (1), p.101-106

2003

Volltextzugriff (PDF)

Conformational Dynamics of β2-Microglobulin Analyzed by Reduction and Reoxidation of the Disulfide Bond

Journal of biochemistry (Tokyo), 2003-06, Vol.133 (6), p.731-736

2003

Volltextzugriff (PDF)

The Anti-Amyloidogenic Effect Is Exerted against Alzheimer's β-Amyloid Fibrils in Vitro by Preferential and Reversible Binding of Flavonoids to the Amyloid Fibril Structure

Biochemistry (Easton), 2007-02, Vol.46 (7), p.1888-1899

2007

Volltextzugriff (PDF)

2PT113 アミロイド構造の決定におけるタンパク質揺らぎの役割の解析(日本生物物理学会第50回年会(2012年度))

生物物理, 2012/08/15, Vol.52(supplement), pp.S123

2012

Volltextzugriff (PDF)

2PT113 NMR study on the role of protein fluctuation in determining the amyloid conformation(The 50th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2012/08/15, Vol.52(supplement), pp.S123

2012

Volltextzugriff (PDF)

Lysophospholipids induce the nucleation and extension of β2-microglobulin-related amyloid fibrils at a neutral pH

Nephrology, dialysis, transplantation, 2008-10, Vol.23 (10), p.3247-3255

2008

Volltextzugriff (PDF)

Optimum Amyloid Fibril Formation of a Peptide Fragment Suggests the Amyloidogenic Preference of β2-Microglobulin under Physiological Conditions

The Journal of biological chemistry, 2004-03, Vol.279 (11), p.10814-10821

2004

Volltextzugriff (PDF)

2SC1444 Structure of yeast prion Sup35NM oligomer determines prion strain phenotype(2SC Advanced Insight into Protein Motions-in silico, in vitro and in vivo Studies,The 48th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2010/08/15, Vol.50(supplement2), pp.S11

2010

Volltextzugriff (PDF)

1P051 Differences in prion strain conformations result from nonnative interactions in a nucleus.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2010/08/15, Vol.50(supplement2), pp.S28

2010

Volltextzugriff (PDF)

1P051 酵母プリオンSup35の高感染性凝集体を誘導するオリゴマー中間体(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)

生物物理, 2010/08/15, Vol.50(supplement2), pp.S28

2010

Volltextzugriff (PDF)

Growth of beta(2)-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

Biochemical journal, 2008-12, Vol.416 (2), p.307-315

2008

Volltextzugriff (PDF)

Radically Different Amyloid Conformations Dictate the Seeding Specificity of a Chimeric Sup35 Prion

Journal of molecular biology, 2011-04, Vol.408 (1), p.1-8

2011

Volltextzugriff (PDF)

2P-072 Molecular basis of prion strain phenotypes in the yeast prion [PSI+] system(The 46th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2008/10/25, Vol.48(supplement), pp.S86

2008

Volltextzugriff (PDF)

2P-072 酵母プリオン系におけるプリオン株形成の分子機構(蛋白質・物性(2),第46回日本生物物理学会年会)

生物物理, 2008/10/25, Vol.48(supplement), pp.S86

2008

Volltextzugriff (PDF)

The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH

Journal of biochemistry (Tokyo), 2002-01, Vol.131 (1), p.45-52

2002

Volltextzugriff (PDF)

Ultrasonication-induced Amyloid Fibril Formation of Î²2-Microglobulin

The Journal of biological chemistry, 2005-09, Vol.280 (38), p.32843

2005

Volltextzugriff (PDF)

Ultrasonication-induced amyloid fibril formation of beta2-microglobulin

The Journal of biological chemistry, 2005-09, Vol.280 (38), p.32843-32848

2005

Volltextzugriff (PDF)

Lysophospholipids induce the nucleation and extension of 2-microglobulin-related amyloid fibrils at a neutral pH

Nephrology, dialysis, transplantation, 2008-06, Vol.23 (10), p.3247-3255

2008

Volltextzugriff (PDF)

1 – 25 von 55

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(54)
Mit Volltextzugriff
(50)

Publikationsform

Artikel
(55)

Sprache

Englisch
(52)
Japanisch
(19)

Erscheinungsjahr

n.n

Thema

15 weitere anzeigen...

Weniger anzeigen...

Menü

Weitere Dienste

Einstellungen

Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils

Detection of Fibril Nucleation in Micrometer-Sized Protein Condensates and Suppression of Sup35NM Fibril Nucleation by Liquid–Liquid Phase Separation

Short disordered protein segment regulates cross-species transmission of a yeast prion

Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin

Molecular basis for diversification of yeast prion strain conformation

Growth of β2-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

The Intrachain Disulfide Bond of β2-Microglobulin Is Not Essential for the Immunoglobulin Fold at Neutral pH, but Is Essential for Amyloid Fibril Formation at Acidic pH

Amyloidogenic synthetic peptides of β2-microglobulin—a role of the disulfide bond

Conformational Dynamics of β2-Microglobulin Analyzed by Reduction and Reoxidation of the Disulfide Bond

The Anti-Amyloidogenic Effect Is Exerted against Alzheimer's β-Amyloid Fibrils in Vitro by Preferential and Reversible Binding of Flavonoids to the Amyloid Fibril Structure

2PT113 アミロイド構造の決定におけるタンパク質揺らぎの役割の解析(日本生物物理学会第50回年会(2012年度))

2PT113 NMR study on the role of protein fluctuation in determining the amyloid conformation(The 50th Annual Meeting of the Biophysical Society of Japan)

Lysophospholipids induce the nucleation and extension of β2-microglobulin-related amyloid fibrils at a neutral pH

Optimum Amyloid Fibril Formation of a Peptide Fragment Suggests the Amyloidogenic Preference of β2-Microglobulin under Physiological Conditions

2SC1444 Structure of yeast prion Sup35NM oligomer determines prion strain phenotype(2SC Advanced Insight into Protein Motions-in silico, in vitro and in vivo Studies,The 48th Annual Meeting of the Biophysical Society of Japan)

1P051 Differences in prion strain conformations result from nonnative interactions in a nucleus.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

1P051 酵母プリオンSup35の高感染性凝集体を誘導するオリゴマー中間体(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)

Growth of beta(2)-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

Radically Different Amyloid Conformations Dictate the Seeding Specificity of a Chimeric Sup35 Prion

2P-072 Molecular basis of prion strain phenotypes in the yeast prion [PSI+] system(The 46th Annual Meeting of the Biophysical Society of Japan)

2P-072 酵母プリオン系におけるプリオン株形成の分子機構(蛋白質・物性(2),第46回日本生物物理学会年会)

The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH

Ultrasonication-induced Amyloid Fibril Formation of Î²2-Microglobulin

Ultrasonication-induced amyloid fibril formation of beta2-microglobulin

Lysophospholipids induce the nucleation and extension of 2-microglobulin-related amyloid fibrils at a neutral pH

Suchergebnisse filtern