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Post-translational modifications that modulate enzyme activity /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Garcia, Benjamin A. (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Cambridge, MA : Academic Press, 2019.
Colección:Methods in enzymology ; v. 626.
Temas:
Acceso en línea:Texto completo

MARC

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245 0 0 |a Post-translational modifications that modulate enzyme activity /  |c edited by Benjamin A. Garcia. 
264 1 |a Cambridge, MA :  |b Academic Press,  |c 2019. 
300 |a 1 online resource 
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 enzymology ;  |v volume 626 
588 0 |a Print version record. 
504 |a Includes bibliographical references. 
505 0 |a Crosstalk between cellular metabolism and histone acetylation / Sophie Trefely, Mary T. Doan, and Nathaniel W. Snyder -- Purification and enzymatic assay of class I histone deacetylase enzymes / Mark K. Adams, Charles A.S. Banks, Sayem Miah, Maxime Killer, and Michael P. Washburn -- Multiplexed quantitative phosphoproteomics of cell line and tissue samples / Johannes Kreuzer, Amanda Edwards, and Wilhelm Haas -- Differentiation of peptide isomers and epimers by radical-directed dissociation / Tyler R. Lambeth and Ryan R. Julian -- Biochemical analysis of protein arginylation / Junling Wang, John R. Yates III, and Anna Kashina -- Site-specific determination of lysine acetylation stoichiometries on the proteome-scale / Yue Chen and Yunan Li -- RNA modifications and the link to human disease / Amber Yanas and Kathy Fange Liu -- Isolation and characterization of glycosylated neuropeptides / Yang Liu, Qinjingwen Cao, and Lingjun Li -- Utilizing intein trans-splicing for in vivo generation of site-specifically modified proteins / Igor Maksimovic, Devin Ray, Qingfei Zheng, and Yael David -- Systematic and site-specific analysis of N-glycoproteins on the cell surface by integrating bioorthogonal chemistry and MS-based proteomics / Fangxu Sun and Ronghu Wu -- Silencing glycosaminoglycan functions in mouse embryonic stem cells with small molecule antagonists / Sourav Chatterjee, Tesia N. Stephenson, Austen L. Michalak, Kamil Godula, and Mia L. Huang -- Biochemical and structural analysis of N-terminal acetyltransferases / Leah Gottlieb and Ronen Marmorstein -- Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry / Peng Li, Yuanli Zhen, and Yonghao Yu -- Analysis of the topology of ubiquitin chains / Lucia Geis-Asteggiante, Amanda E. Lee, and Catherine Fenselau -- Analysis of cardiac troponin proteoforms by top-down mass spectrometry / Timothy N. Tiambeng, Trisha Tucholski, Zhijie Wu, Yanlong Zhu, Stanford D. Mitchell, David S. Roberts, Yutong Jin, and Ying Ge -- Assays for tyrosine phosphorylation in human cells / Monica Kruk, Naomi Widstrom, Sampreeti Jena, Nicole L. Wolter, John F. Blankenhorn, Ibrahim Abdalla, Tzu-Yi Yang, and Laurie L. Parker -- Metabolomics analysis of lipid metabolizing enzyme activity / Timothy B. Ware, Myungsun Shin, and Ku-Lung Hsu -- Simplified high yield TAILS terminomics using a new HPG-ALD 800K-2000 polymer with precipitation / Nestor Solis, Anilkumar Parambath, Srinivas Abbina, Jayachandran Kizhakkedathu, and Christopher M. Overall -- Methods for the expression, purification, and crystallization of histone deacetylase 6-inhibitor complexes / Jeremy D. Osko and David W. Christianson -- Quantitative analysis of global protein lysine methylation by mass spectrometry / Peder J. Lund, Stephanie M. Lehman, and Benjamin A. Garcia -- The roles of S-nitrosylation and S-glutathionylation in Alzheimer's disease / Ryan R. Dyer, Katarena I. Ford, Ren�a A.S. Robinson -- Expression of authentic post-translationally modified proteins in organisms with expanded genetic codes / Kyle Mohler and Jesse Rinehart -- Preparation of a new construct of human histone deacetylase 8 for the crystallization of enzyme-inhibitor complexes / Nicholas J. Porter and David W. Christianson -- Methods for characterizing protein acetylation during viral infection / Laura A. Murray, Ashton N. Combs, Pranav Rekapalli, and Ileana M. Cristea. 
650 0 |a Post-translational modification. 
650 0 |a Enzymology. 
650 0 |a Cell physiology. 
650 1 2 |a Protein Processing, Post-Translational  |0 (DNLM)D011499 
650 2 2 |a Cell Physiological Phenomena  |0 (DNLM)D002468 
650 6 |a Prot�eines  |x Modification post-traductionnelle.  |0 (CaQQLa)201-0232745 
650 6 |a Enzymologie.  |0 (CaQQLa)201-0269407 
650 6 |a Cellules  |x Physiologie.  |0 (CaQQLa)201-0005055 
650 7 |a Cell physiology.  |2 fast  |0 (OCoLC)fst00850214 
650 7 |a Enzymology.  |2 fast  |0 (OCoLC)fst00913635 
650 7 |a Post-translational modification.  |2 fast  |0 (OCoLC)fst01072761 
655 4 |a Internet Resources. 
655 4 |a Index not Present. 
700 1 |a Garcia, Benjamin A.,  |e editor. 
776 0 8 |i Print version:  |t POST-TRANSLATIONAL MODIFICATIONS THAT MODULATE ENZYME ACTIVITY.  |d [S.l.] : ELSEVIER ACADEMIC PRESS, 2019  |z 0128186690  |w (OCoLC)1089562830 
830 0 |a Methods in enzymology ;  |v v. 626. 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/626  |z Texto completo