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Title Protein misfolding diseases : methods and protocols / editor Cláudio M. Gomes.
Imprint New York, NY : Humana Press : Springer, ©2018.


 Internet  Electronic Book    AVAILABLE
Description 1 online resource (xiii, 338 pages) : illustrations (some color)
Series Methods in Molecular Biology, 1940-3745 ; volume 1873
Methods in molecular biology (Clifton, N.J.) ; v. 1873. 1064-3745
Bibliog. Includes bibliographical references and index.
Note Available only to authorized UTEP users.
Online resource; title from PDF title page (SpringerLink, viewed October 19, 2018).
Subject Protein folding.
Proteostasis Deficiencies.
Genre Laboratory Manual.
Contents Intro; Preface; Contents; Contributors; Part I: Protein Biophysics Assays; Chapter 1: Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation; 1 Introduction; 1.1 Protein Misfolding and Aggregation in Disease; 1.2 Circular Dichroism; 1.3 Fourier-Transform Infrared Spectroscopy; 1.4 Fluorescence Spectroscopy; 1.5 Dynamic Light Scattering; 2 Materials; 2.1 SOD1 Expression and Purification; 2.2 Demetallation of SOD1; 2.3 CD; 2.4 ATR-FTIR; 2.5 1,8-ANS Fluorescence; 2.6 ThT Fluorescence Kinetics; 2.7 DLS; 3 Methods; 3.1 SOD1 Expression and Purification
Biophysical and spectroscopic methods for monitoring protein misfolding and amyloid / Joana S. Cristóvão, Bárbara J. Henriques, and Cláudio M. Gomes -- Ultrasensitive RT-QuIC seed amplification assays for disease-associated tau, α-Synuclein, and prion aggregates / Eri Saijo, Bradley R. Groveman, Allison Kraus, Michael Metrick, Christina D. Orrù, Andrew G. Hughson, and Byron Caughey -- Vesicle-based assays to study membrane interactions of amyloid peptides / Ravit Malishev, Sofiya Kolusheva, and Raz Jelinek -- Differential scanning fluorimetry and hydrogen deuterium exchange mass spectrometry to monitor the conformational dynamics of NBD1 in cystic fibrosis / Naoto Soya, Ariel Roldan, and Gergely L. Lukacs -- Multipronged method for unveiling subtle structural-functional defects of mutant chaperone molecules causing human chaperonopathies / Donatella Bulone, Pier Luigi San Biagio, Tatiana Quiñones-Ruiz, Manuel Rosario-Alomar, Igor K. Lednev, Frank T. Robb, Everly Conway de Macario, and Alberto J.L. Macario -- High-throughput microplate-based fluorescence assays for studying stochastic aggregation of superoxide Ddsmutase-1 / Alireza Abdolvahabi, Sanaz Rasouli, Corbin M. Croom, and Devon L. Plewman -- Methods for structural analysis of amyloid fibrils in misfolding diseases / Devkee M. Vadukul, Youssra K. Al-Hilaly, and Louise C. Serpell -- Assays for light chain amyloidosis formation and cytotoxicity / Luis M. Blancas-Mejia, Pinaki Misra, Christopher J. Dick, Marta Marin-Argany, Keely R. Redhage, Shawna A. Cooper, and Marina Ramirez-Alvarado -- Monitoring aggregate clearance and formation in cell-based assays / Evelien Eenjes, Young Joo Yang-Klingler, and Ai Yamamoto -- Monitoring proteome stress in live cells using halotag-based fluorogenic sensor / Yu Liu, Matthew Fares, and Xin Zhang -- Quantification of protein aggregates using bimolecular fluorescence complementation / Vibha Prasad and Aaron Voigt -- Screening protein aggregation in cells using fluorescent labels coupled to flow cytometry / Salvador Ventura and Susanna Navarro -- Induction of Cu/Zn superoxide dismutase (SOD1) aggregation in living cells / Edward Pokrishevsky, Jeremy Nan, and Neil R. Cashman -- Cell model for HSP60 deficiencies : modeling different levels of chaperonopathies leading to oxidative stress and mitochondrial dysfunction / Cagla Cömert, Paula Fernandez-Guerra, and Peter Bross -- Superresolution fluorescence imaging of mutant huntingtin aggregation in cells / Steffen J. Sahl and Willianne I.M. Vonk -- Thermal shift and stability assays of disease-related misfolded proteins using differential scanning fluorimetry / Tânia G. Lucas, Cláudio M. Gomes, and Bárbara J. Henriques -- Methods to screen compounds against mutant p53 misfolding and aggregation for cancer therapeutics / Giulia Diniz da Silva Ferretti, Danielly C. Ferraz da Costa, Jerson L. Silva, and Luciana Pereira Rangel -- Early stage discovery and validation of pharmacological chaperones for the correction of protein misfolding diseases / Oscar Aubi, Per M. Knappskog, and Aurora Martinez -- Constructing kinetically controlled denaturation isotherms of folded proteins using denaturant-pulse chaperonin binding / Pierce T. O'Neil, Alexandra J. Machen, Jackie A. Thompson, Wei Wang, Quyen Q. Hoang, Michael R. Baldwin, Karen R. Khar, John Karanicolas, and Mark T. Fisher -- In vitro prion amplification methodology for inhibitor screening / Tuane Cristine R.G. Vieira and Jerson L. Silva -- SolubiS : optimizing protein solubility by minimal point mutations / Rob van der Kant, Joost van Durme, Frederic Rousseau, and Joost Schymkowitz.
3.2.1 Stock Solutions3.2.2 Prepreparation; 3.2.3 Multilamellar Dispersion (MLD); 3.2.4 Small Unilamellar Vesicles (SUVs), Size Range 1000 nm; 3.3 Fluorescence Measurements; 3.3.1 Förster Resonance Energy Transfer (FRET); 3.3.2 Fluorescence Anisotropy; 3.3.3 Fluorescence Quenching; 3.3.4 Vesicle Leakage Assay; 3.4 Calorimetric Measurements; 3.4.1 Differential Scanning Calorimetry (DSC); 3.4.2 Isothermal Titration Calorimetry (ITC); 3.5 Electron Spin Resonance (ESR); 3.6 Microscopy; 4 Notes
Other Author Gomes, Cláudio M., 1970- editor.
Other Title Print version: Protein misfolding diseases. New York, NY : Humana Press : Springer, ©2018 9781493988198