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Artikel ; Online: Protein lipidation in cancer: mechanisms, dysregulation and emerging drug targets.

Tate, Edward W / Soday, Lior / de la Lastra, Ana Losada / Wang, Mei / Lin, Hening

2024 Band 24, Heft 4, Seite(n) 240–260

Abstract: Protein lipidation describes a diverse class of post-translational modifications (PTMs) that is regulated by over 40 enzymes, targeting more than 1,000 substrates at over 3,000 sites. Lipidated proteins include more than 150 oncoproteins, including ... ...

Abstract	Protein lipidation describes a diverse class of post-translational modifications (PTMs) that is regulated by over 40 enzymes, targeting more than 1,000 substrates at over 3,000 sites. Lipidated proteins include more than 150 oncoproteins, including mediators of cancer initiation, progression and immunity, receptor kinases, transcription factors, G protein-coupled receptors and extracellular signalling proteins. Lipidation regulates the physical interactions of its protein substrates with cell membranes, regulating protein signalling and trafficking, and has a key role in metabolism and immunity. Targeting protein lipidation, therefore, offers a unique approach to modulate otherwise undruggable oncoproteins; however, the full spectrum of opportunities to target the dysregulation of these PTMs in cancer remains to be explored. This is attributable in part to the technological challenges of identifying the targets and the roles of protein lipidation. The early stage of drug discovery for many enzymes in the pathway contrasts with efforts for drugging similarly common PTMs such as phosphorylation and acetylation, which are routinely studied and targeted in relevant cancer contexts. Here, we review recent advances in identifying targetable protein lipidation pathways in cancer, the current state-of-the-art in drug discovery, and the status of ongoing clinical trials, which have the potential to deliver novel oncology therapeutics targeting protein lipidation.
Mesh-Begriff(e)	Humans ; Protein Processing, Post-Translational ; Neoplasms/drug therapy ; Phosphorylation ; Transcription Factors ; Oncogene Proteins
Chemische Substanzen	Transcription Factors ; Oncogene Proteins
Sprache	Englisch
Erscheinungsdatum	2024-02-29
Erscheinungsland	England
Dokumenttyp	Journal Article ; Review
ZDB-ID	2062767-1
ISSN	1474-1768 ; 1474-175X
ISSN (online)	1474-1768
ISSN	1474-175X
DOI	10.1038/s41568-024-00666-x
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Rapid Degradation Pathways of Host Proteins During HCMV Infection Revealed by Quantitative Proteomics.

Lin, Kai-Min / Nightingale, Katie / Soday, Lior / Antrobus, Robin / Weekes, Michael P

Frontiers in cellular and infection microbiology

2021 Band 10, Seite(n) 578259

Abstract: Human cytomegalovirus (HCMV) is an important pathogen in immunocompromised individuals and neonates, and a paradigm for viral immune evasion. We previously developed a quantitative proteomic approach that identified 133 proteins degraded during the early ...

Abstract	Human cytomegalovirus (HCMV) is an important pathogen in immunocompromised individuals and neonates, and a paradigm for viral immune evasion. We previously developed a quantitative proteomic approach that identified 133 proteins degraded during the early phase of HCMV infection, including known and novel antiviral factors. The majority were rescued from degradation by MG132, which is known to inhibit lysosomal cathepsins in addition to the proteasome. Global definition of the precise mechanisms of host protein degradation is important both to improve our understanding of viral biology, and to inform novel antiviral therapeutic strategies. We therefore developed and optimized a multiplexed comparative proteomic analysis using the selective proteasome inhibitor bortezomib in addition to MG132, to provide a global mechanistic view of protein degradation. Of proteins rescued from degradation by MG132, 34-47 proteins were also rescued by bortezomib, suggesting both that the predominant mechanism of protein degradation employed by HCMV is
Mesh-Begriff(e)	Cytomegalovirus ; Humans ; Immune Evasion ; Infant, Newborn ; Proteins ; Proteolysis ; Proteomics
Chemische Substanzen	Proteins
Sprache	Englisch
Erscheinungsdatum	2021-01-27
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2020.578259
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Selective modulation of cell surface proteins during vaccinia infection: A resource for identifying viral immune evasion strategies.

Depierreux, Delphine M / Altenburg, Arwen F / Soday, Lior / Fletcher-Etherington, Alice / Antrobus, Robin / Ferguson, Brian J / Weekes, Michael P / Smith, Geoffrey L

PLoS pathogens

2022 Band 18, Heft 6, Seite(n) e1010612

Abstract: The interaction between immune cells and virus-infected targets involves multiple plasma membrane (PM) proteins. A systematic study of PM protein modulation by vaccinia virus (VACV), the paradigm of host regulation, has the potential to reveal not only ... ...

Abstract	The interaction between immune cells and virus-infected targets involves multiple plasma membrane (PM) proteins. A systematic study of PM protein modulation by vaccinia virus (VACV), the paradigm of host regulation, has the potential to reveal not only novel viral immune evasion mechanisms, but also novel factors critical in host immunity. Here, >1000 PM proteins were quantified throughout VACV infection, revealing selective downregulation of known T and NK cell ligands including HLA-C, downregulation of cytokine receptors including IFNAR2, IL-6ST and IL-10RB, and rapid inhibition of expression of certain protocadherins and ephrins, candidate activating immune ligands. Downregulation of most PM proteins occurred via a proteasome-independent mechanism. Upregulated proteins included a decoy receptor for TRAIL. Twenty VACV-encoded PM proteins were identified, of which five were not recognised previously as such. Collectively, this dataset constitutes a valuable resource for future studies on antiviral immunity, host-pathogen interaction, poxvirus biology, vector-based vaccine design and oncolytic therapy.
Mesh-Begriff(e)	Communicable Diseases ; Humans ; Immune Evasion ; Membrane Proteins/metabolism ; Poxviridae ; Vaccinia ; Vaccinia virus
Chemische Substanzen	Membrane Proteins
Sprache	Englisch
Erscheinungsdatum	2022-06-21
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010612
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Comprehensive cell surface proteomics defines markers of classical, intermediate and non-classical monocytes.

Ravenhill, Benjamin J / Soday, Lior / Houghton, Jack / Antrobus, Robin / Weekes, Michael P

Scientific reports

2020 Band 10, Heft 1, Seite(n) 4560

Abstract: Monocytes are a critical component of the cellular innate immune system, and can be subdivided into classical, intermediate and non-classical subsets on the basis of surface CD14 and CD16 expression. Classical monocytes play the canonical role of ... ...

Abstract	Monocytes are a critical component of the cellular innate immune system, and can be subdivided into classical, intermediate and non-classical subsets on the basis of surface CD14 and CD16 expression. Classical monocytes play the canonical role of phagocytosis, and account for the majority of circulating cells. Intermediate and non-classical cells are known to exhibit varying levels of phagocytosis and cytokine secretion, and are differentially expanded in certain pathological states. Characterisation of cell surface proteins expressed by each subset is informative not only to improve understanding of phenotype, but may also provide biological insights into function. Here we use highly multiplexed Tandem-Mass-Tag (TMT)-based mass spectrometry with selective cell surface biotinylation to characterise the classical monocyte surface proteome, then interrogate the phenotypic differences between each monocyte subset to identify novel protein markers.
Mesh-Begriff(e)	Biomarkers/metabolism ; Chromatography, Liquid ; Gene Expression Regulation ; Healthy Volunteers ; Humans ; Immunity, Cellular ; Mass Spectrometry ; Membrane Proteins/metabolism ; Monocytes/metabolism ; Phenotype ; Proteomics/methods
Chemische Substanzen	Biomarkers ; Membrane Proteins
Sprache	Englisch
Erscheinungsdatum	2020-03-12
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-61356-w
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Ribosome profiling of porcine reproductive and respiratory syndrome virus reveals novel features of viral gene expression.

Cook, Georgia M / Brown, Katherine / Shang, Pengcheng / Li, Yanhua / Soday, Lior / Dinan, Adam M / Tumescheit, Charlotte / Mockett, A P Adrian / Fang, Ying / Firth, Andrew E / Brierley, Ian

eLife

2022 Band 11

Abstract: The arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) causes significant economic losses to the swine industry worldwide. Here we apply ribosome profiling (RiboSeq) and parallel RNA sequencing (RNASeq) to characterise the ... ...

Abstract	The arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) causes significant economic losses to the swine industry worldwide. Here we apply ribosome profiling (RiboSeq) and parallel RNA sequencing (RNASeq) to characterise the transcriptome and translatome of both species of PRRSV and to analyse the host response to infection. We calculated programmed ribosomal frameshift (PRF) efficiency at both sites on the viral genome. This revealed the nsp2 PRF site as the second known example where temporally regulated frameshifting occurs, with increasing -2 PRF efficiency likely facilitated by accumulation of the PRF-stimulatory viral protein, nsp1β. Surprisingly, we find that PRF efficiency at the canonical ORF1ab frameshift site also increases over time, in contradiction of the common assumption that RNA structure-directed frameshift sites operate at a fixed efficiency. This has potential implications for the numerous other viruses with canonical PRF sites. Furthermore, we discovered several highly translated additional viral ORFs, the translation of which may be facilitated by multiple novel viral transcripts. For example, we found a highly expressed 125-codon ORF overlapping nsp12, which is likely translated from novel subgenomic RNA transcripts that overlap the 3' end of ORF1b. Similar transcripts were discovered for both PRRSV-1 and PRRSV-2, suggesting a potential conserved mechanism for temporally regulating expression of the 3'-proximal region of ORF1b. We also identified a highly translated, short upstream ORF in the 5' UTR, the presence of which is highly conserved amongst PRRSV-2 isolates. These findings reveal hidden complexity in the gene expression programmes of these important nidoviruses.
Mesh-Begriff(e)	Animals ; Codon/metabolism ; Frameshifting, Ribosomal/genetics ; Gene Expression Profiling ; Porcine respiratory and reproductive syndrome virus/genetics ; Ribosomes/genetics ; Ribosomes/metabolism ; Swine ; Transcriptome
Chemische Substanzen	Codon
Sprache	Englisch
Erscheinungsdatum	2022-02-28
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.75668
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Quantitative Temporal Proteomic Analysis of Vaccinia Virus Infection Reveals Regulation of Histone Deacetylases by an Interferon Antagonist.

Soday, Lior / Lu, Yongxu / Albarnaz, Jonas D / Davies, Colin T R / Antrobus, Robin / Smith, Geoffrey L / Weekes, Michael P

Cell reports

2019 Band 27, Heft 6, Seite(n) 1920–1933.e7

Abstract: Vaccinia virus (VACV) has numerous immune evasion strategies, including multiple mechanisms of inhibition of interferon regulatory factor 3 (IRF-3), nuclear factor κB (NF-κB), and type I interferon (IFN) signaling. Here, we use highly multiplexed ... ...

Abstract	Vaccinia virus (VACV) has numerous immune evasion strategies, including multiple mechanisms of inhibition of interferon regulatory factor 3 (IRF-3), nuclear factor κB (NF-κB), and type I interferon (IFN) signaling. Here, we use highly multiplexed proteomics to quantify ∼9,000 cellular proteins and ∼80% of viral proteins at seven time points throughout VACV infection. A total of 265 cellular proteins are downregulated >2-fold by VACV, including putative natural killer cell ligands and IFN-stimulated genes. Two-thirds of these viral targets, including class II histone deacetylase 5 (HDAC5), are degraded proteolytically during infection. In follow-up analysis, we demonstrate that HDAC5 restricts replication of both VACV and herpes simplex virus type 1. By generating a protein-based temporal classification of VACV gene expression, we identify protein C6, a multifunctional IFN antagonist, as being necessary and sufficient for proteasomal degradation of HDAC5. Our approach thus identifies both a host antiviral factor and a viral mechanism of innate immune evasion.
Mesh-Begriff(e)	Cytomegalovirus/metabolism ; Down-Regulation ; Gene Expression Regulation, Viral ; Herpesvirus 1, Human/metabolism ; Histone Deacetylases/metabolism ; Host-Pathogen Interactions ; Humans ; Immune Evasion ; Interferons/antagonists & inhibitors ; Interferons/metabolism ; Membrane Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Proteomics ; Time Factors ; Vaccinia/metabolism ; Vaccinia/virology ; Vaccinia virus/genetics ; Vaccinia virus/immunology ; Vaccinia virus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemische Substanzen	Membrane Proteins ; Viral Proteins ; Interferons (9008-11-1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Histone Deacetylases (EC 3.5.1.98)
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2019-05-07
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2019.04.042
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Comparative Cell Surface Proteomic Analysis of the Primary Human T Cell and Monocyte Responses to Type I Interferon.

Soday, Lior / Potts, Martin / Hunter, Leah M / Ravenhill, Benjamin J / Houghton, Jack W / Williamson, James C / Antrobus, Robin / Wills, Mark R / Matheson, Nicholas J / Weekes, Michael P

Frontiers in immunology

2021 Band 12, Seite(n) 600056

Abstract: The cellular response to interferon (IFN) is essential for antiviral immunity, IFN-based therapy and IFN-related disease. The plasma membrane (PM) provides a critical interface between the cell and its environment, and is the initial portal of entry for ... ...

Abstract	The cellular response to interferon (IFN) is essential for antiviral immunity, IFN-based therapy and IFN-related disease. The plasma membrane (PM) provides a critical interface between the cell and its environment, and is the initial portal of entry for viruses. Nonetheless, the effect of IFN on PM proteins is surprisingly poorly understood, and has not been systematically investigated in primary immune cells. Here, we use multiplexed proteomics to quantify IFNα2a-stimulated PM protein changes in primary human CD14+ monocytes and CD4+ T cells from five donors, quantifying 606 and 482 PM proteins respectively. Comparison of cell surface proteomes revealed a remarkable invariance between donors in the overall composition of the cell surface from each cell type, but a marked donor-to-donor variability in the effects of IFNα2a. Furthermore, whereas only 2.7% of quantified proteins were consistently upregulated by IFNα2a at the surface of CD4+ T cells, 6.8% of proteins were consistently upregulated in primary monocytes, suggesting that the magnitude of the IFNα2a response varies according to cell type. Among these differentially regulated proteins, we found the viral target Endothelin-converting enzyme 1 (ECE1) to be an IFNα2a-stimulated protein exclusively upregulated at the surface of CD4+ T cells. We therefore provide a comprehensive map of the cell surface of IFNα2a-stimulated primary human immune cells, including previously uncharacterized interferon stimulated genes (ISGs) and candidate antiviral factors.
Mesh-Begriff(e)	CD4-Positive T-Lymphocytes/cytology ; CD4-Positive T-Lymphocytes/immunology ; Endothelin-Converting Enzymes/immunology ; Humans ; Interferon-alpha/pharmacology ; Monocytes/cytology ; Monocytes/immunology ; Proteomics
Chemische Substanzen	IFNA2 protein, human ; Interferon-alpha ; ECE1 protein, human (EC 3.4.24.71) ; Endothelin-Converting Enzymes (EC 3.4.24.71)
Sprache	Englisch
Erscheinungsdatum	2021-02-08
Erscheinungsland	Switzerland
Dokumenttyp	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.600056
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Human cytomegalovirus interactome analysis identifies degradation hubs, domain associations and viral protein functions.

Nobre, Luis V / Nightingale, Katie / Ravenhill, Benjamin J / Antrobus, Robin / Soday, Lior / Nichols, Jenna / Davies, James A / Seirafian, Sepehr / Wang, Eddie Cy / Davison, Andrew J / Wilkinson, Gavin Wg / Stanton, Richard J / Huttlin, Edward L / Weekes, Michael P

eLife

2019 Band 8

Abstract: Human cytomegalovirus (HCMV) extensively modulates host cells, downregulating >900 human proteins during viral replication and degrading ≥133 proteins shortly after infection. The mechanism of degradation of most host proteins remains unresolved, and the ...

Abstract	Human cytomegalovirus (HCMV) extensively modulates host cells, downregulating >900 human proteins during viral replication and degrading ≥133 proteins shortly after infection. The mechanism of degradation of most host proteins remains unresolved, and the functions of many viral proteins are incompletely characterised. We performed a mass spectrometry-based interactome analysis of 169 tagged, stably-expressed canonical strain Merlin HCMV proteins, and two non-canonical HCMV proteins, in infected cells. This identified a network of >3400 virus-host and >150 virus-virus protein interactions, providing insights into functions for multiple viral genes. Domain analysis predicted binding of the viral UL25 protein to SH3 domains of NCK Adaptor Protein-1. Viral interacting proteins were identified for 31/133 degraded host targets. Finally, the uncharacterised, non-canonical ORFL147C protein was found to interact with elements of the mRNA splicing machinery, and a mutational study suggested its importance in viral replication. The interactome data will be important for future studies of herpesvirus infection.
Mesh-Begriff(e)	Adaptor Proteins, Signal Transducing/genetics ; Cytomegalovirus/genetics ; Cytomegalovirus/pathogenicity ; Cytomegalovirus Infections/genetics ; Cytomegalovirus Infections/virology ; Gene Expression Regulation, Viral/genetics ; Host-Pathogen Interactions/genetics ; Humans ; Oncogene Proteins/genetics ; Proteomics ; RNA Splicing/genetics ; RNA, Messenger/genetics ; Viral Proteins/genetics ; Virus Replication/genetics
Chemische Substanzen	Adaptor Proteins, Signal Transducing ; Nck protein ; Oncogene Proteins ; RNA, Messenger ; Viral Proteins
Sprache	Englisch
Erscheinungsdatum	2019-12-24
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.49894
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: A Temporal Proteomic Map of Epstein-Barr Virus Lytic Replication in B Cells.

Ersing, Ina / Nobre, Luis / Wang, Liang Wei / Soday, Lior / Ma, Yijie / Paulo, Joao A / Narita, Yohei / Ashbaugh, Camille W / Jiang, Chang / Grayson, Nicholas E / Kieff, Elliott / Gygi, Steven P / Weekes, Michael P / Gewurz, Benjamin E

Cell reports

2017 Band 19, Heft 7, Seite(n) 1479–1493

Abstract: Epstein-Barr virus (EBV) replication contributes to multiple human diseases, including infectious mononucleosis, nasopharyngeal carcinoma, B cell lymphomas, and oral hairy leukoplakia. We performed systematic quantitative analyses of temporal changes in ... ...

Abstract	Epstein-Barr virus (EBV) replication contributes to multiple human diseases, including infectious mononucleosis, nasopharyngeal carcinoma, B cell lymphomas, and oral hairy leukoplakia. We performed systematic quantitative analyses of temporal changes in host and EBV proteins during lytic replication to gain insights into virus-host interactions, using conditional Burkitt lymphoma models of type I and II EBV infection. We quantified profiles of >8,000 cellular and 69 EBV proteins, including >500 plasma membrane proteins, providing temporal views of the lytic B cell proteome and EBV virome. Our approach revealed EBV-induced remodeling of cell cycle, innate and adaptive immune pathways, including upregulation of the complement cascade and proteasomal degradation of the B cell receptor complex, conserved between EBV types I and II. Cross-comparison with proteomic analyses of human cytomegalovirus infection and of a Kaposi-sarcoma-associated herpesvirus immunoevasin identified host factors targeted by multiple herpesviruses. Our results provide an important resource for studies of EBV replication.
Mesh-Begriff(e)	B-Lymphocytes/metabolism ; B-Lymphocytes/virology ; Cell Cycle ; Cell Membrane/metabolism ; Complement System Proteins/metabolism ; Down-Regulation ; Herpesvirus 4, Human/physiology ; Humans ; Proteolysis ; Proteomics/methods ; Receptors, Antigen, B-Cell/metabolism ; Time Factors ; Transcription Factors/metabolism ; Up-Regulation ; Virus Replication
Chemische Substanzen	Receptors, Antigen, B-Cell ; Transcription Factors ; Complement System Proteins (9007-36-7)
Sprache	Englisch
Erscheinungsdatum	2017-05-11
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2017.04.062
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: High-Definition Analysis of Host Protein Stability during Human Cytomegalovirus Infection Reveals Antiviral Factors and Viral Evasion Mechanisms.

Cell host & microbe

2018 Band 24, Heft 3, Seite(n) 447–460.e11

Abstract: Human cytomegalovirus (HCMV) is an important pathogen with multiple immune evasion strategies, including virally facilitated degradation of host antiviral restriction factors. Here, we describe a multiplexed approach to discover proteins with innate ... ...

Abstract	Human cytomegalovirus (HCMV) is an important pathogen with multiple immune evasion strategies, including virally facilitated degradation of host antiviral restriction factors. Here, we describe a multiplexed approach to discover proteins with innate immune function on the basis of active degradation by the proteasome or lysosome during early-phase HCMV infection. Using three orthogonal proteomic/transcriptomic screens to quantify protein degradation, with high confidence we identified 35 proteins enriched in antiviral restriction factors. A final screen employed a comprehensive panel of viral mutants to predict viral genes that target >250 human proteins. This approach revealed that helicase-like transcription factor (HLTF), a DNA helicase important in DNA repair, potently inhibits early viral gene expression but is rapidly degraded during infection. The functionally unknown HCMV protein UL145 facilitates HLTF degradation by recruiting the Cullin4 E3 ligase complex. Our approach and data will enable further identifications of innate pathways targeted by HCMV and other viruses.
Mesh-Begriff(e)	Cytomegalovirus/genetics ; Cytomegalovirus/immunology ; Cytomegalovirus/physiology ; Cytomegalovirus Infections/genetics ; Cytomegalovirus Infections/immunology ; Cytomegalovirus Infections/virology ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/immunology ; Humans ; Immune Evasion ; Protein Stability ; Proteins/chemistry ; Proteins/genetics ; Proteins/immunology ; Proteomics ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/immunology ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/immunology
Chemische Substanzen	DNA-Binding Proteins ; HLTF protein, human ; Proteins ; Transcription Factors ; Viral Proteins
Sprache	Englisch
Erscheinungsdatum	2018-08-16
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2018.07.011
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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