Differences in the Molecular Structure of β2-Microglobulin between Two Morphologically Different Amyloid Fibrils-Reference-Cited by-同舟云学术

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Differences in the Molecular Structure of β2-Microglobulin between Two Morphologically Different Amyloid Fibrils

Published:2010-01-05 Issue:4 Volume:49 Page:742-751
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hiramatsu Hirotsugu¹,Lu Ming¹,Matsuo Koichi²,Gekko Kunihiko²,Goto Yuji³,Kitagawa Teizo¹

Affiliation:

1. Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki 444-8787, Japan

2. Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan

3. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi901536j

Reference75 articles.

1. Structure of the human class I histocompatibility antigen, HLA-A2

2. Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation

3. A native to amyloidogenic transition regulated by a backbone trigger

4. Low Concentrations of Sodium Dodecyl Sulfate Induce the Extension of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH

5. Collagen Plays an Active Role in the Aggregation of β2-Microglobulin under Physiopathological Conditions of Dialysis-related Amyloidosis

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1. Conformational fingerprinting of tau variants and strains by Raman spectroscopy;RSC Advances;2021

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3. Early mechanisms of amyloid fibril nucleation in model and disease-related proteins;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2019-11

4. Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation;ACS Chemical Neuroscience;2019-09-06

5. Ultraviolet/persulfate (UV/PS) pretreatment of typical natural organic matter (NOM): Variation of characteristics and control of membrane fouling;Chemosphere;2019-01

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