Diameter of the vial plays a crucial role in the amyloid fibril formation: Role of interface area between hydrophilic-hydrophobic surfaces

Role of Post-translational Chemical Modifications in Amyloid Fibril Formation

Amyloid Proteins ◽

10.1002/9783527619344.ch5 ◽

2008 ◽

pp. 81-109 ◽

Cited By ~ 3

Author(s):

Melanie R. Nilsson

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Chemical Modifications ◽

Amyloid fibril formation by bovine α1-acid glycoprotein in a reducing environment: The role of disulfide bridges on the observed aggregation kinetics

Biochimie ◽

10.1016/j.biochi.2015.09.026 ◽

2015 ◽

Vol 118 ◽

pp. 244-252 ◽

Cited By ~ 2

Author(s):

Maurizio Baldassarre ◽

Beatrice Maggiore ◽

Andrea Scirè ◽

Fabio Tanfani

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Aggregation Kinetics ◽

Disulfide Bridges ◽

Acid Glycoprotein ◽

Reducing Environment

Role of the intrachain disulfide bond of beta2-microglobulin on its amyloid fibril formation.

Seibutsu Butsuri ◽

10.2142/biophys.41.s169_1 ◽

2001 ◽

Vol 41 (supplement) ◽

pp. S169

Author(s):

Y Ohashi ◽

Y Hagihara ◽

Kozhukh Gennadiy ◽

M Hoshino ◽

K Hasegawa ◽

...

Keyword(s):

Disulfide Bond ◽

Amyloid Fibril ◽

Fibril Formation ◽

Intrachain Disulfide Bond

The role of protein stability, solubility, and net charge in amyloid fibril formation

Protein Science ◽

10.1110/ps.03152903 ◽

2009 ◽

Vol 12 (10) ◽

pp. 2374-2378 ◽

Cited By ~ 106

Author(s):

Jason P. Schmittschmitt ◽

J. Martin Scholtz

Keyword(s):

Protein Stability ◽

Amyloid Fibril ◽

Fibril Formation ◽

Net Charge ◽

The role of conformational flexibility in β 2 ‐microglobulin amyloid fibril formation at neutral pH

Rapid Communications in Mass Spectrometry ◽

10.1002/rcm.6282 ◽

2012 ◽

Vol 26 (16) ◽

pp. 1783-1792 ◽

Cited By ~ 22

Author(s):

John P. Hodkinson ◽

Sheena E. Radford ◽

Alison E. Ashcroft

Keyword(s):

Amyloid Fibril ◽

Conformational Flexibility ◽

Fibril Formation ◽

Neutral Ph ◽

The role of apo E in amyloid fibril formation

Neurobiology of Aging ◽

10.1016/0197-4580(94)93041-4 ◽

1994 ◽

Vol 15 ◽

pp. S143

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Apo E

The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II

Advances in Experimental Medicine and Biology - Lipids in Protein Misfolding ◽

10.1007/978-3-319-17344-3_7 ◽

2015 ◽

pp. 157-174 ◽

Cited By ~ 6

Author(s):

Timothy M. Ryan ◽

Yee-Foong Mok ◽

Geoffrey J. Howlett ◽

Michael D. W. Griffin

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Apolipoprotein C

The role of the acidic domain of α-synuclein in amyloid fibril formation: a molecular dynamics study

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.2015.1033016 ◽

2015 ◽

Vol 34 (2) ◽

pp. 376-383 ◽

Cited By ~ 13

Author(s):

SeongByeong Park ◽

Jeseong Yoon ◽

Soonmin Jang ◽

Kyunghee Lee ◽

Seokmin Shin

Keyword(s):

Molecular Dynamics ◽

Amyloid Fibril ◽

Fibril Formation ◽

Acidic Domain ◽

Role of the C-Terminal 28 Residues of β2-Microglobulin in Amyloid Fibril Formation†

Biochemistry ◽

10.1021/bi0301486 ◽

2003 ◽

Vol 42 (46) ◽

pp. 13536-13540 ◽

Cited By ~ 26

Author(s):

Magdalena I. Ivanova ◽

Mari Gingery ◽

Lisa J. Whitson ◽

David Eisenberg

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Β2 Microglobulin ◽

Role of disulfide bond in the amyloid fibril formation of beta2-microglobulin by NMR

Seibutsu Butsuri ◽

10.2142/biophys.41.s169_3 ◽

2001 ◽

Vol 41 (supplement) ◽

pp. S169

Author(s):

H Katou ◽

M Hoshino ◽

Kozhukh Gennadiy ◽

K Hasegawa ◽

H Naiki ◽

...

Keyword(s):

Disulfide Bond ◽

Amyloid Fibril ◽

Fibril Formation ◽