205 records matched your query       

05100aam a2200361 i 4500
001 04EB3190ECCF11E5A64DF5B3DAD10320
003 SILO
005 20160318010059
008 160115t20162015nyua     b    001 0deng d
010    $a 2015949999
020    $a 1493929771 (hd.bd.)
020    $a 9781493929771 (hd.bd.)
035    $a (OCoLC)935107875
040    $a OHX $b eng $c OHX $d OCLCO $d NUI $d SILO
245 00 $a Protein amyloid aggregation : $b methods and protocols / $c editoed by David Eliezer.
264  1 $a New York : $b Springer, $c [2015]
300    $a xiv, 314 pages : $b illustrations (some color) ; $c 27 cm
490 1  $a Methods in molecular biology, $x 1064-3745 ; $v volume 1345
490 1  $a Springer protocols, $x 1949-2448
504    $a Includes bibliographical references and index.
505 80 $t Analyzing tau aggregation with electron microscopy / $r Joseph D. Handen and Igor K. Lednev -- $t Isotope-labeled amyloids via synthesis, expression, and chemical ligation for use in FTIR, 2D IR, and NMR studies / $r Tianqi O. Zhang [and others] -- $t Intermolecular paramagnetic relaxation enhancement (PRE) studies of transient complexes in intrinsically disordered proteins / $r Maria K. Janowska and Jean Baum -- $t Detection of helical intermediates during amyloid formation by intrinsically disordered polypeptides and proteins / $r Andisheh Abedini, Ping Cao, and Daniel P. Raleigh -- $t Fluorescence correlation spectroscopy : a tool to study protein oligomerization and aggregation in vitro and in vivo / $r Bankanidhi Sahoo, Kenneth W. Drombosky, and Ronald Wetzel -- $t Deep UV resonance raman spectroscopy for characterizing amyloid aggregation / $r Joseph D. Handen and Igor K. Lednev -- $t Analyzing tau aggregation with electron microscopy /
505 80 $r Andrei T. Alexandrescu -- $t Quenched hydrogen exchange NMR of amyloid fibrils / $r Charlotte A. Scarff, Alison E. Ashcroft, and Sheena E. Radford -- $t Formation and characterization of α-Synuclein oligomers / $r Wojciech Paslawski, Nikolai Lorenzen, and Daniel E. Otzen -- $t Fluorescence methods for unraveling oligomeric amyloid intermediates / $r Niels Zijlstra, Nathalie Schilderink, and Vinod Subramaniam -- $t Preparation of amyloid fibrils for magic-angle spinning solid-state NMR spectroscopy / $r Marcus D. Tuttle [and others] -- $t Spin labeling and characterization of tau fibrils using electron paramagnetic resonance (EPR) / $r Virginia Meyer and Martin Margittai -- $t Preparation of crystalline samples of amyloid fibrils and oligomers / $r Asher Moshe, Meytal Landau, and David Eisenberg -- $t Quenched hydrogen exchange NMR of amyloid fibrils / $r Andrei T. Alexandrescu --
505 80 $t Preparation of amyloid fibrils seeded from brain and meninges / $r Kathryn P. Scherpel [and others]. $t Computational methods for structural and functional studies of Alzheimer's amyloid ion channels / $r Hyunbum Jang [and others] -- $t Analyzing ensembles of amyloid proteins using Bayesian statistics / $r Thomas Gurry [and others] -- $t In vitro studies of membrane permeability induced by amyloidogenic polypeptides using large unilamellar vesicles / $r Ping Cao and Daniel P. Raleigh -- $t Cell models to study cell-to-cell transmission of α-Synuclein / $r Eun-Jin Bae, He-Jin Lee, and Seung-Jae Lee -- $t Preparation of amyloid fibrils seeded from brain and meninges / $r Kathryn P. Scherpel [and others].
520    $a This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils, and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists, and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.
650  0 $a Life sciences $v Laboratory manuals.
650  0 $a Proteins $v Laboratory manuals.
700 1  $a Eliezer, David, $e editor.
710 2  $a Springer Science+Business Media, $e copyright holder.
830  0 $a Methods in molecular biology (Clifton, N.J.) ; $v v. 1345, $x 1064-3745
830  0 $a Springer protocols (Series), $x 1949-2448
941    $a 1
952    $l OVUX522 $d 20180124032506.0
956    $a http://locator.silo.lib.ia.us/search.cgi?index_0=id&term_0=04EB3190ECCF11E5A64DF5B3DAD10320