LIVIVO - Search results -

Search results

Result 1 - 10 of total 25

Search options

Article ; Online: The HisRS-like domain of GCN2 is a pseudoenzyme that can bind uncharged tRNA.

Yin, Jay Z / Keszei, Alexander F A / Houliston, Scott / Filandr, Frantisek / Beenstock, Jonah / Daou, Salima / Kitaygorodsky, Julia / Schriemer, David C / Mazhab-Jafari, Mohammad T / Gingras, Anne-Claude / Sicheri, Frank

Structure (London, England : 1993)

2024

Abstract: GCN2 is a stress response kinase that phosphorylates the translation initiation factor eIF2α to inhibit general protein synthesis when activated by uncharged tRNA and stalled ribosomes. The presence of a HisRS-like domain in GCN2, normally associated ... ...

Abstract	GCN2 is a stress response kinase that phosphorylates the translation initiation factor eIF2α to inhibit general protein synthesis when activated by uncharged tRNA and stalled ribosomes. The presence of a HisRS-like domain in GCN2, normally associated with tRNA aminoacylation, led to the hypothesis that eIF2α kinase activity is regulated by the direct binding of this domain to uncharged tRNA. Here we solved the structure of the HisRS-like domain in the context of full-length GCN2 by cryoEM. Structure and function analysis shows the HisRS-like domain of GCN2 has lost histidine and ATP binding but retains tRNA binding abilities. Hydrogen deuterium exchange mass spectrometry, site-directed mutagenesis and computational docking experiments support a tRNA binding model that is partially shifted from that employed by bona fide HisRS enzymes. These results demonstrate that the HisRS-like domain of GCN2 is a pseudoenzyme and advance our understanding of GCN2 regulation and function.
Language	English
Publishing date	2024-03-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2024.02.021
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4141: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Polycomb group-mediated histone H2A monoubiquitination in epigenome regulation and nuclear processes.

Barbour, Haithem / Daou, Salima / Hendzel, Michael / Affar, El Bachir

Nature communications

2020 Volume 11, Issue 1, Page(s) 5947

Abstract: Histone posttranslational modifications are key regulators of chromatin-associated processes including gene expression, DNA replication and DNA repair. Monoubiquitinated histone H2A, H2Aub (K118 in Drosophila or K119 in vertebrates) is catalyzed by the ... ...

Abstract	Histone posttranslational modifications are key regulators of chromatin-associated processes including gene expression, DNA replication and DNA repair. Monoubiquitinated histone H2A, H2Aub (K118 in Drosophila or K119 in vertebrates) is catalyzed by the Polycomb group (PcG) repressive complex 1 (PRC1) and reversed by the PcG-repressive deubiquitinase (PR-DUB)/BAP1 complex. Here we critically assess the current knowledge regarding H2Aub deposition and removal, its crosstalk with PcG repressive complex 2 (PRC2)-mediated histone H3K27 methylation, and the recent attempts toward discovering its readers and solving its enigmatic functions. We also discuss mounting evidence of the involvement of H2A ubiquitination in human pathologies including cancer, while highlighting some knowledge gaps that remain to be addressed.
MeSH term(s)	Animals ; Chromatin/metabolism ; Deubiquitinating Enzymes/metabolism ; Epigenesis, Genetic ; Histones/metabolism ; Humans ; Methylation ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/pathology ; Polycomb-Group Proteins/chemistry ; Polycomb-Group Proteins/genetics ; Polycomb-Group Proteins/metabolism ; Ubiquitination
Chemical Substances	Chromatin ; Histones ; Polycomb-Group Proteins ; Deubiquitinating Enzymes (EC 3.4.19.12)
Language	English
Publishing date	2020-11-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-19722-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Polycomb group-mediated histone H2A monoubiquitination in epigenome regulation and nuclear processes

Haithem Barbour / Salima Daou / Michael Hendzel / El Bachir Affar

Nature Communications, Vol 11, Iss 1, Pp 1-

2020 Volume 16

Abstract: Histone H2A monoubiquitination on lysine 119 in vertebrate and lysine 118 in Drosophila (H2Aub) is an epigenomic mark usually associated with gene repression by Polycomb group factors. Here the authors review the current knowledge on the deposition and ... ...

Abstract	Histone H2A monoubiquitination on lysine 119 in vertebrate and lysine 118 in Drosophila (H2Aub) is an epigenomic mark usually associated with gene repression by Polycomb group factors. Here the authors review the current knowledge on the deposition and removal of H2Aub, its function in transcription and other DNA-associated processes as well as its relevance to human disease.
Keywords	Science ; Q
Language	English
Publishing date	2020-11-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Vivid views of the PINK1 protein.

Daou, Salima / Sicheri, Frank

Nature

2015 Volume 552, Issue 7683, Page(s) 38–39

MeSH term(s)	Humans ; Mitochondria ; Parkinson Disease ; Protein Kinases ; Ubiquitin-Protein Ligases
Chemical Substances	Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Protein Kinases (EC 2.7.-)
Language	English
Publishing date	2015-11-03
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/d41586-017-07691-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes.

Barbour, Haithem / Nkwe, Nadine Sen / Estavoyer, Benjamin / Messmer, Clémence / Gushul-Leclaire, Mila / Villot, Romain / Uriarte, Maxime / Boulay, Karine / Hlayhel, Sari / Farhat, Bassel / Milot, Eric / Mallette, Frédérick A / Daou, Salima / Affar, El Bachir

iScience

2023 Volume 26, Issue 5, Page(s) 106276

Abstract: Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. ... ...

Abstract	Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. Much progress has been made during the last three decades in understanding how ubiquitin ligases recognize their substrates and how ubiquitination is orchestrated. Several mechanisms of regulation have evolved to prevent promiscuity including the assembly of ubiquitin ligases in multi-protein complexes with dedicated subunits and specific post-translational modifications of these enzymes and their co-factors. Here, we outline another layer of complexity involving the coordinated access of E3 ligases to substrates. We provide an extensive inventory of ubiquitination crosstalk with multiple PTMs including SUMOylation, phosphorylation, methylation, acetylation, hydroxylation, prolyl isomerization, PARylation, and O-GlcNAcylation. We discuss molecular mechanisms by which PTMs orchestrate ubiquitination, thus increasing its specificity as well as its crosstalk with other signaling pathways to ensure cell homeostasis.
Language	English
Publishing date	2023-02-26
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.106276
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones.

Masclef, Louis / Maxime, Uriarte / Ahmed, Oumaima / Sen Nkwe, Nadine / Barbour, Haithem / Iannantuono, Nicholas V G / Boubekeur, Amina / Daou, Salima / Affar, El Bachir

Journal of visualized experiments : JoVE

2019 , Issue 149

Abstract: Ubiquitination is a post-translational modification that plays important roles in various signaling pathways and is notably involved in the coordination of chromatin function and DNA-associated processes. This modification involves a sequential action of ...

Abstract	Ubiquitination is a post-translational modification that plays important roles in various signaling pathways and is notably involved in the coordination of chromatin function and DNA-associated processes. This modification involves a sequential action of several enzymes including E1 ubiquitin-activating, E2 ubiquitin-conjugating and E3 ubiquitin-ligase and is reversed by deubiquitinases (DUBs). Ubiquitination induces degradation of proteins or alteration of protein function including modulation of enzymatic activity, protein-protein interaction and subcellular localization. A critical step in demonstrating protein ubiquitination or deubiquitination is to perform in vitro reactions with purified components. Effective ubiquitination and deubiquitination reactions could be greatly impacted by the different components used, enzyme co-factors, buffer conditions, and the nature of the substrate. Here, we provide step-by-step protocols for conducting ubiquitination and deubiquitination reactions. We illustrate these reactions using minimal components of the mouse Polycomb Repressive Complex 1 (PRC1), BMI1, and RING1B, an E3 ubiquitin ligase that monoubiquitinates histone H2A on lysine 119. Deubiquitination of nucleosomal H2A is performed using a minimal Polycomb Repressive Deubiquitinase (PR-DUB) complex formed by the human deubiquitinase BAP1 and the DEUBiquitinase ADaptor (DEUBAD) domain of its co-factor ASXL2. These ubiquitination/deubiquitination assays can be conducted in the context of either recombinant nucleosomes reconstituted with bacteria-purified proteins or native nucleosomes purified from mammalian cells. We highlight the intricacies that can have a significant impact on these reactions and we propose that the general principles of these protocols can be swiftly adapted to other E3 ubiquitin ligases and deubiquitinases.
MeSH term(s)	Animals ; HEK293 Cells ; Histones/metabolism ; Humans ; Mice ; Nucleosomes/chemistry ; Ubiquitination
Chemical Substances	Histones ; Nucleosomes
Language	English
Publishing date	2019-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/59385
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.

Myers, Samuel A / Daou, Salima / Affar, El Bachir / Burlingame, Al

Proteomics

2013 Volume 13, Issue 6, Page(s) 982–991

Abstract: The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment. The field of ... ...

Abstract	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment. The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures. Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs. Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1). HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression. ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells. These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Chromatography, High Pressure Liquid ; Glycopeptides/chemistry ; Glycopeptides/isolation & purification ; Glycosylation ; HEK293 Cells ; Host Cell Factor C1/chemistry ; Host Cell Factor C1/isolation & purification ; Host Cell Factor C1/metabolism ; Humans ; Mice ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Peptide Fragments/isolation & purification ; Protein Processing, Post-Translational ; Spectrometry, Mass, Electrospray Ionization/methods ; Tandem Mass Spectrometry/methods
Chemical Substances	Glycopeptides ; HCFC1 protein, human ; Host Cell Factor C1 ; Peptide Fragments
Language	English
Publishing date	2013-01-18
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2032093-0
ISSN	1615-9861 ; 1615-9853
ISSN (online)	1615-9861
ISSN	1615-9853
DOI	10.1002/pmic.201200332
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5386: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.A 1868: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A potent nuclear export mechanism imposes USP16 cytoplasmic localization during interphase.

Sen Nkwe, Nadine / Daou, Salima / Uriarte, Maxime / Gagnon, Jessica / Iannantuono, Nicholas Victor / Barbour, Haithem / Yu, Helen / Masclef, Louis / Fernández, Erlinda / Zamorano Cuervo, Natalia / Mashtalir, Nazar / Binan, Loïc / Sergeev, Mikhail / Bélanger, François / Drobetsky, Elliot / Milot, Eric / Wurtele, Hugo / Costantino, Santiago / Affar, El Bachir

Journal of cell science

2020 Volume 133, Issue 4

Abstract: USP16 (also known as UBP-M) has emerged as a histone H2AK119 deubiquitylase (DUB) implicated in the regulation of chromatin-associated processes and cell cycle progression. Despite this, available evidence suggests that this DUB is also present in the ... ...

Abstract	USP16 (also known as UBP-M) has emerged as a histone H2AK119 deubiquitylase (DUB) implicated in the regulation of chromatin-associated processes and cell cycle progression. Despite this, available evidence suggests that this DUB is also present in the cytoplasm. How the nucleo-cytoplasmic transport of USP16, and hence its function, is regulated has remained elusive. Here, we show that USP16 is predominantly cytoplasmic in all cell cycle phases. We identified the nuclear export signal (NES) responsible for maintaining USP16 in the cytoplasm. We found that USP16 is only transiently retained in the nucleus following mitosis and then rapidly exported from this compartment. We also defined a non-canonical nuclear localization signal (NLS) sequence that plays a minimal role in directing USP16 into the nucleus. We further established that this DUB does not accumulate in the nucleus following DNA damage. Instead, only enforced nuclear localization of USP16 abolishes DNA double-strand break (DSB) repair, possibly due to unrestrained DUB activity. Thus, in contrast to the prevailing view, our data indicate that USP16 is actively excluded from the nucleus and that this DUB might indirectly regulate DSB repair.This article has an associated First Person interview with the first author of the paper.
MeSH term(s)	Active Transport, Cell Nucleus ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Cytoplasm/genetics ; Cytoplasm/metabolism ; Interphase ; Nuclear Export Signals/genetics ; Nuclear Localization Signals/genetics ; Nuclear Localization Signals/metabolism
Chemical Substances	Nuclear Export Signals ; Nuclear Localization Signals
Language	English
Publishing date	2020-02-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.239236
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A phenolic small molecule inhibitor of RNase L prevents cell death from ADAR1 deficiency.

Daou, Salima / Talukdar, Manisha / Tang, Jinle / Dong, Beihua / Banerjee, Shuvojit / Li, Yize / Duffy, Nicole M / Ogunjimi, Abiodun A / Gaughan, Christina / Jha, Babal K / Gish, Gerald / Tavernier, Nicolas / Mao, Daniel / Weiss, Susan R / Huang, Hao / Silverman, Robert H / Sicheri, Frank

Proceedings of the National Academy of Sciences of the United States of America

2020 Volume 117, Issue 40, Page(s) 24802–24812

Abstract: The oligoadenylate synthetase (OAS)-RNase L system is an IFN-inducible antiviral pathway activated by viral infection. Viral double-stranded (ds) RNA activates OAS isoforms that synthesize the second messenger 2-5A, which binds and activates the ... ...

Abstract	The oligoadenylate synthetase (OAS)-RNase L system is an IFN-inducible antiviral pathway activated by viral infection. Viral double-stranded (ds) RNA activates OAS isoforms that synthesize the second messenger 2-5A, which binds and activates the pseudokinase-endoribonuclease RNase L. In cells, OAS activation is tamped down by ADAR1, an adenosine deaminase that destabilizes dsRNA. Mutation of
MeSH term(s)	2',5'-Oligoadenylate Synthetase/genetics ; 2',5'-Oligoadenylate Synthetase/metabolism ; Adenine Nucleotides/metabolism ; Adenosine Deaminase/deficiency ; Adenosine Deaminase/genetics ; Autoimmune Diseases of the Nervous System/enzymology ; Autoimmune Diseases of the Nervous System/genetics ; Autoimmune Diseases of the Nervous System/physiopathology ; Cell Death/drug effects ; Endoribonucleases/antagonists & inhibitors ; Endoribonucleases/genetics ; Endoribonucleases/metabolism ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Humans ; Nervous System Malformations/enzymology ; Nervous System Malformations/genetics ; Nervous System Malformations/physiopathology ; Oligoribonucleotides/metabolism ; Phenol/chemistry ; Phenol/pharmacology ; RNA-Binding Proteins/genetics
Chemical Substances	Adenine Nucleotides ; Enzyme Inhibitors ; Oligoribonucleotides ; RNA-Binding Proteins ; Phenol (339NCG44TV) ; 2',5'-oligoadenylate (61172-40-5) ; 2',5'-Oligoadenylate Synthetase (EC 2.7.7.84) ; Endoribonucleases (EC 3.1.-) ; 2-5A-dependent ribonuclease (EC 3.1.26.-) ; ADAR protein, human (EC 3.5.4.37) ; Adenosine Deaminase (EC 3.5.4.4)
Keywords	covid19
Language	English
Publishing date	2020-09-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2006883117
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: In vitro ubiquitination and deubiquitination assays of nucleosomal histones

Masclef, Louis / Affar, El Bachir / Ahmed, Oumaima / Barbour, Haithem / Boubekeur, Amina / Daou, Salima / Iannantuono, Nicholas V.G / Maxime, Uriarte / Sen Nkwe, Nadine

Journal of visualized experiments. 2019 July 25, , no. 149

2019

Abstract	Ubiquitination is a post-translational modification that plays important roles in various signaling pathways and is notably involved in the coordination of chromatin function and DNA-associated processes. This modification involves a sequential action of several enzymes including E1 ubiquitin-activating, E2 ubiquitin-conjugating and E3 ubiquitin-ligase and is reversed by deubiquitinases (DUBs). Ubiquitination induces degradation of proteins or alteration of protein function including modulation of enzymatic activity, protein-protein interaction and subcellular localization. A critical step in demonstrating protein ubiquitination or deubiquitination is to perform in vitro reactions with purified components. Effective ubiquitination and deubiquitination reactions could be greatly impacted by the different components used, enzyme co-factors, buffer conditions, and the nature of the substrate. Here, we provide step-by-step protocols for conducting ubiquitination and deubiquitination reactions. We illustrate these reactions using minimal components of the mouse Polycomb Repressive Complex 1 (PRC1), BMI1, and RING1B, an E3 ubiquitin ligase that monoubiquitinates histone H2A on lysine 119. Deubiquitination of nucleosomal H2A is performed using a minimal Polycomb Repressive Deubiquitinase (PR-DUB) complex formed by the human deubiquitinase BAP1 and the DEUBiquitinase ADaptor (DEUBAD) domain of its co-factor ASXL2. These ubiquitination/deubiquitination assays can be conducted in the context of either recombinant nucleosomes reconstituted with bacteria-purified proteins or native nucleosomes purified from mammalian cells. We highlight the intricacies that can have a significant impact on these reactions and we propose that the general principles of these protocols can be swiftly adapted to other E3 ubiquitin ligases and deubiquitinases.
Keywords	enzyme activity ; histones ; humans ; lysine ; mice ; nucleosomes ; protein-protein interactions ; signal transduction ; ubiquitination ; ubiquitin-protein ligase ; ubiquitinyl hydrolase 1
Language	English
Dates of publication	2019-0725
Size	p. e59385.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/59385
Database	NAL-Catalogue (AGRICOLA)

Order via subito

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito