Ubiquitin-proteasome protocols /
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| Imprint: | Totowa, N.J. : Humana Press, ©2005. |
|---|---|
| Description: | 1 online resource (xi, 381 pages) : illustrations |
| Language: | English |
| Series: | Methods in molecular biology, 1064-3745 ; 301 Methods in molecular biology (Clifton, N.J.) ; v. 301. |
| Subject: | |
| Format: | E-Resource Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/11137239 |
MARC
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| 072 | 7 | |a SCI |x 007000 |2 bisacsh | |
| 072 | 7 | |a PSB. |2 bicssc | |
| 245 | 0 | 0 | |a Ubiquitin-proteasome protocols / |c edited by Cam Patterson, Douglas M. Cyr. |
| 260 | |a Totowa, N.J. : |b Humana Press, |c ©2005. | ||
| 300 | |a 1 online resource (xi, 381 pages) : |b illustrations | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a Methods in molecular biology, |x 1064-3745 ; |v 301 | |
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | |a Small-molecule inhibitors of proteasome activity / Maria Gaczynska and Pawel A. Osmulski -- Purification of E1 and E1-like enzymes / Arthur L. Haas -- Assays for RING family ubiquitin ligases / Manabu Furukawa, Paul S. Andrews, and Yue Xiong -- Ubiquitin chain synthesis / Shahri Raasi and Cecile M. Pickart -- Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast / David S. Leggett, Michael H. Glickman, and Daniel Finley -- Recognition and processing of misfolded proteins by PA700, the 19S regulatory complex of the 26S proteasome / Chang-Wei Liu [and others] -- Cell-free assay for ubiquitin-independent proteasomal protein degradation / Chaim Kahana and Yuval Reiss. | |
| 505 | 0 | |a Assays of proteasome-dependent cleavage products / Stefan Tenzer and Hansjörg Schild -- Identification of components of protein complexes / Carol E. Parker [and others] -- Mass spectrometric determination of protein ubiqitination / Carol E. Parker [and others] -- Reconstitution of endoplasmic reticulum-associated degradation using yeast membranes and cytosol / Robert J. Lee, Ardythe A. McCracken, and Jeffrey L. Brodsky -- Reticulocyte lysate as a model system to study endoplasmic reticulum membrane protein degradation / Eric Carlson [and others] -- Deubiquitinating enzyme purifucation, assay inhibitors, and characterization / Nathaniel S. Russell and Keith D. Wilkinson -- Measuring ubiquitin conjugation in cells / Edward G. Mimnaugh and Leonard M. Neckers -- Assays for proteasome assembly and maturation / R. Jürgen Dohmen [and others]. | |
| 505 | 0 | |a N-terminal ubiquitination / Aaron Ciechanover -- Quantitating defective ribosome products / Shu-Bing Qian, Jack R. Bennink, and Jonathan W. Yewdell --endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis / Antje Schäfer and Dieter H. Wolf -- Endoplasmic reticulum-associated protein quality control and degradation: genome wide screen for ERAD components / Antje Schäfer and Dieter H. Wolf -- Cystic fibrosis transmembrane conductance regulator as a model substrate to study endoplasmic reticulum protein quality control in mammalian cells / J. Michael Younger [and others] -- Aggresome formation / Michael J. Corboy, Philip J. Thomas, and W. Christian Wigley -- Detection of sumoylated proteins / Roland S. Hilgarth and Kevin D. Sarge -- Proteasome inhibitors in cancer therapy / Robert Z. Orlowski -- Parkinson's disease: assays for the ubiquitin ligase activity of neural parkin / Michael G. Schlossmacher and Hideki Shimura. | |
| 588 | 0 | |a Print version record. | |
| 520 | 8 | |a Annotation |b A collection of cutting-edge techniques for studying ubiquitin-dependent protein degradation via the proteasome. The topics covered range broadly from basic biochemistry to cellular assays to discovery techniques using mass spectrometric analysis. These biochemical and cellular methods are necessary to explore the ubiquitin-proteasome system and ubiquitin-proteasome-dependent functions. State-of-the-art and user-friendly, Ubiquitin-Proteasome Protocols offers novice and experienced bench scientists alike a thorough compendium of readily reproducible techniques that will accelerate discovery, enhance productivity, and permit manipulation of the system for varied research purposes. | |
| 546 | |a English. | ||
| 650 | 0 | |a Ubiquitin |v Laboratory manuals. | |
| 650 | 0 | |a Proteolytic enzymes |v Laboratory manuals. | |
| 650 | 0 | |a Cysteine proteinases. |0 http://id.loc.gov/authorities/subjects/sh86007065 | |
| 650 | 0 | |a Multienzyme complexes. | |
| 650 | 1 | 2 | |a Ubiquitin |x metabolism |
| 650 | 2 | 2 | |a Cysteine Endopeptidases |
| 650 | 2 | 2 | |a Multienzyme Complexes |
| 650 | 6 | |a Ubiquitine |v Manuels de laboratoire. | |
| 650 | 6 | |a Enzymes protéolytiques |v Manuels de laboratoire. | |
| 650 | 6 | |a Peptidases à cystéine. | |
| 650 | 6 | |a Complexes multienzymatiques. | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Multienzyme complexes |2 fast | |
| 650 | 7 | |a Cysteine proteinases |2 fast | |
| 650 | 7 | |a Proteolytic enzymes |2 fast | |
| 650 | 7 | |a Ubiquitin |2 fast | |
| 653 | 0 | 0 | |a ubiquitine |
| 653 | 0 | 0 | |a ubiquitin |
| 653 | 0 | 0 | |a eiwitafbraak |
| 653 | 0 | 0 | |a protein degradation |
| 653 | 1 | 0 | |a Proteins and Enzymes |
| 653 | 1 | 0 | |a Eiwitten en enzymen |
| 655 | 2 | |a Laboratory Manual |0 https://id.nlm.nih.gov/mesh/D020484 | |
| 655 | 7 | |a Laboratory manuals |2 fast | |
| 655 | 7 | |a Laboratory manuals. |2 lcgft |0 http://id.loc.gov/authorities/genreForms/gf2014026120 | |
| 655 | 7 | |a Manuels de laboratoire. |2 rvmgf | |
| 700 | 1 | |a Patterson, Cam. |0 http://id.loc.gov/authorities/names/n2004121689 | |
| 700 | 1 | |a Cyr, Douglas M. |0 http://id.loc.gov/authorities/names/n2004122364 | |
| 776 | 0 | 8 | |i Print version: |t Ubiquitin-proteasome protocols. |d Totowa, N.J. : Humana Press, ©2005 |z 1588292525 |z 1592598951 |w (DLC) 2004017480 |w (OCoLC)56066486 |
| 830 | 0 | |a Methods in molecular biology (Clifton, N.J.) ; |v v. 301. | |
| 856 | 4 | 0 | |u https://link.springer.com/10.1385/1592598951 |y Springer Nature |
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