LIVIVO - Search results -

Search results

Result 1 - 10 of total 15

Search options

Article ; Online: CRISPR/Cas9-based inactivation of human papillomavirus oncogenes E6 or E7 induces senescence in cervical cancer cells.

Inturi, Raviteja / Jemth, Per

2021 Volume 562, Page(s) 92–102

Abstract: Human papillomaviruses (HPVs) such as HPV16 and HPV18 can cause cancers of the cervix, anogenital and oropharyngeal sites. Continuous expression of the HPV oncoproteins E6 and E7 are essential for transformation and maintenance of cancer cells. Therefore, ...

Abstract	Human papillomaviruses (HPVs) such as HPV16 and HPV18 can cause cancers of the cervix, anogenital and oropharyngeal sites. Continuous expression of the HPV oncoproteins E6 and E7 are essential for transformation and maintenance of cancer cells. Therefore, therapeutic targeting of E6 or E7 genes can potentially treat HPV-related cancers. Here we report that CRISPR/Cas9-based knockout of E6 or E7 can trigger cellular senescence in HPV18 immortalized HeLa cells. Specifically, E6 or E7-inactivated HeLa cells exhibited characteristic senescence markers like enlarged cell surface area, increased β-galactosidase expression and loss of lamin B1. Since E6 and E7 are bicistronic transcripts, inactivation of HPV18 E6 resulted in knockout of both E6 and E7 and increasing levels of p53/p21 and pRb/p21, respectively. Knockout of HPV18 E7 resulted in decreased E6 expression with activation of pRb/p21 pathway. Taken together, our study demonstrates cellular senescence as an alternative outcome of HPV oncogene inactivation by CRISPR/Cas9.
MeSH term(s)	CRISPR-Associated Protein 9/metabolism ; CRISPR-Cas Systems ; Cellular Senescence/genetics ; Cyclin-Dependent Kinase Inhibitor p21/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Female ; Gene Editing ; HeLa Cells ; Humans ; Lamin Type B/metabolism ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/metabolism ; Retinoblastoma Protein/metabolism ; Signal Transduction ; Tumor Suppressor Protein p53/metabolism ; Uterine Cervical Neoplasms/genetics ; Uterine Cervical Neoplasms/metabolism ; Uterine Cervical Neoplasms/pathology ; beta-Galactosidase/metabolism
Chemical Substances	CDKN1A protein, human ; Cyclin-Dependent Kinase Inhibitor p21 ; DNA-Binding Proteins ; E6 protein, Human papillomavirus type 18 ; E7 protein, Human papillomavirus type 18 ; Lamin Type B ; Oncogene Proteins, Viral ; Retinoblastoma Protein ; TP53 protein, human ; Tumor Suppressor Protein p53 ; CRISPR-Associated Protein 9 (EC 3.1.-) ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2021-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.07.005
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.172: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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: CRISPR/Cas9-based inactivation of human papillomavirus oncogenes E6 or E7 induces senescence in cervical cancer cells

Inturi, Raviteja / Jemth, Per

Virology. 2021 Oct., v. 562

2021

Abstract	Human papillomaviruses (HPVs) such as HPV16 and HPV18 can cause cancers of the cervix, anogenital and oropharyngeal sites. Continuous expression of the HPV oncoproteins E6 and E7 are essential for transformation and maintenance of cancer cells. Therefore, therapeutic targeting of E6 or E7 genes can potentially treat HPV-related cancers. Here we report that CRISPR/Cas9-based knockout of E6 or E7 can trigger cellular senescence in HPV18 immortalized HeLa cells. Specifically, E6 or E7-inactivated HeLa cells exhibited characteristic senescence markers like enlarged cell surface area, increased β-galactosidase expression and loss of lamin B1. Since E6 and E7 are bicistronic transcripts, inactivation of HPV18 E6 resulted in knockout of both E6 and E7 and increasing levels of p53/p21 and pRb/p21, respectively. Knockout of HPV18 E7 resulted in decreased E6 expression with activation of pRb/p21 pathway. Taken together, our study demonstrates cellular senescence as an alternative outcome of HPV oncogene inactivation by CRISPR/Cas9.
Keywords	CRISPR-Cas systems ; Papillomaviridae ; cell senescence ; humans ; oncogene proteins ; oncogenes ; surface area ; therapeutics ; uterine cervical neoplasms ; virology
Language	English
Dates of publication	2021-10
Size	p. 92-102.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.07.005
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 3686: Show issues

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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Determinants of affinity, specificity, and phase separation in a supramodule from Post-synaptic density protein 95.

Laursen, Louise / Inturi, Raviteja / Østergaard, Søren / Jemth, Per

iScience

2022 Volume 25, Issue 10, Page(s) 105069

Abstract: The post-synaptic density (PSD) is a phase-separated membraneless compartment of proteins including PSD-95 that undergoes morphological alteration in response to synaptic activity. Here, we investigated the interactome of a three-domain supramodule, PDZ3- ...

Abstract	The post-synaptic density (PSD) is a phase-separated membraneless compartment of proteins including PSD-95 that undergoes morphological alteration in response to synaptic activity. Here, we investigated the interactome of a three-domain supramodule, PDZ3-SH3-GK (PSG) from PSD-95 using bioinformatics to identify potential binding partners, and biophysical methods to characterize the interaction with peptides from these proteins. PSG and the single PDZ3 domain bound similar peptides, but with different specificity. Furthermore, we found that the protein ADGRB1 formed liquid droplets with the PSG supramodule, extending the model for PSD formation. Moreover, certain mutations, introduced outside of the binding pocket in PDZ3, increased the affinity and specificity of the interaction and the size of liquid droplets. Other mutations within the ligand binding pocket lead to a new binding motif specificity. Our results show how the context in terms of supertertiary structure modulates affinity, specificity, and phase separation, and how these properties can evolve by point mutation.
Language	English
Publishing date	2022-09-05
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.105069
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: Structural Insights into Human Adenovirus Type 4 Virus-Associated RNA I.

Bergquist, Helen / Inturi, Raviteja / Zain, Rula / Punga, Tanel

International journal of molecular sciences

2022 Volume 23, Issue 6

Abstract: RNA molecules can adopt specific RNA triplex structures to execute critical biological functions. Human adenoviruses (HAdVs) are abundant pathogens encoding the essential, noncoding virus-associated RNA I (VA RNAI). Here, we employ a triplex-specific ... ...

Abstract	RNA molecules can adopt specific RNA triplex structures to execute critical biological functions. Human adenoviruses (HAdVs) are abundant pathogens encoding the essential, noncoding virus-associated RNA I (VA RNAI). Here, we employ a triplex-specific probing assay, based on the intercalating and cleaving agent benzoquinoquinoxaline 1, 10-phenanthroline (BQQ-OP), to unravel a potential RNA triplex formation in VA RNAI. The BQQ-OP cleavage of the pathogenic HAdV type 4 (HAdV-4) VA RNAI indicates that a potential triplex is formed involving the highly conserved stem 4 of the central domain and side stem 7. Further, the integrity of the HAdV-4 VA RNAI side stem 7 contributes to a potential triplex formation in vitro and virus growth in vivo. Collectively, we propose that the HAdV-4 VA RNAI can potentially form a biologically relevant triplex structure.
MeSH term(s)	Adenoviruses, Human/genetics ; Humans ; RNA, Bacterial
Chemical Substances	RNA I ; RNA, Bacterial
Language	English
Publishing date	2022-03-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23063103
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Structural Characterization of a Thorarchaeota Profilin Indicates Eukaryotic-Like Features but with an Extended N-Terminus.

Inturi, Raviteja / Lara, Sandra / Derweesh, Mahmoud / Chi, Celestine N

Advanced biology

2022 Volume 6, Issue 7, Page(s) e2101323

Abstract: The emergence of the first eukaryotic cell is preceded by evolutionary events, which are still highly debatable. Clues of the exact sequence of events are beginning to emerge. Recent metagenomics analyses has uncovered the Asgard super-phylum as the ... ...

Abstract	The emergence of the first eukaryotic cell is preceded by evolutionary events, which are still highly debatable. Clues of the exact sequence of events are beginning to emerge. Recent metagenomics analyses has uncovered the Asgard super-phylum as the closest yet known archaea host of eukaryotes. Some of these have been tested and confirmed experimentally. However, the bulk of eukaryotic signature proteins predicted to be encoded by the Asgard super-phylum have not been studied, and their true functions, at least in the context of a eukaryotic cell, are still elusive. For example, there are several different variants of the profilin within each Asgardian Achaea, and there are some conflicting results of their actual roles. Here, the 3D structure of profilin from Thorarchaeota is determined by nuclear magnetic resonance spectroscopy and shows that this profilin has a eukaryotic-like profilin with a rigid core and an extended N-terminus previously implicated in polyproline binding. In addition, it is also shown that Thorarchaeota Profilin co-localizes with eukaryotic actin in cultured HeLa cells. This finding reaffirms the notion that Asgardian encoded proteins possess eukaryotic-like characteristics and strengthen the likely existence of a complex cytoskeleton already in a last eukaryotic common ancestor.
MeSH term(s)	Archaea/chemistry ; Archaeal Proteins/chemistry ; Eukaryota ; Genome, Archaeal ; HeLa Cells ; Humans ; Profilins/chemistry
Chemical Substances	Archaeal Proteins ; Profilins
Language	English
Publishing date	2022-04-15
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2701-0198
ISSN (online)	2701-0198
DOI	10.1002/adbi.202101323
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

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.

Details ▾
- Full text online
- Order with fees

Article ; Online: Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets.

Mihalič, Filip / Benz, Caroline / Kassa, Eszter / Lindqvist, Richard / Simonetti, Leandro / Inturi, Raviteja / Aronsson, Hanna / Andersson, Eva / Chi, Celestine N / Davey, Norman E / Överby, Anna K / Jemth, Per / Ivarsson, Ylva

Nature communications

2023 Volume 14, Issue 1, Page(s) 5636

Abstract: The virus life cycle depends on host-virus protein-protein interactions, which often involve a disordered protein region binding to a folded protein domain. Here, we used proteomic peptide phage display (ProP-PD) to identify peptides from the ... ...

Abstract	The virus life cycle depends on host-virus protein-protein interactions, which often involve a disordered protein region binding to a folded protein domain. Here, we used proteomic peptide phage display (ProP-PD) to identify peptides from the intrinsically disordered regions of the human proteome that bind to folded protein domains encoded by the SARS-CoV-2 genome. Eleven folded domains of SARS-CoV-2 proteins were found to bind 281 peptides from human proteins, and affinities of 31 interactions involving eight SARS-CoV-2 protein domains were determined (K
MeSH term(s)	Humans ; Antiviral Agents/pharmacology ; Protein Domains ; SARS-CoV-2 ; Ligands ; Proteomics ; COVID-19 ; Peptides/pharmacology
Chemical Substances	Antiviral Agents ; Ligands ; Peptides
Language	English
Publishing date	2023-09-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-41312-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Human Adenovirus Infection Causes Cellular E3 Ubiquitin Ligase MKRN1 Degradation Involving the Viral Core Protein pVII.

Inturi, Raviteja / Mun, Kwangchol / Singethan, Katrin / Schreiner, Sabrina / Punga, Tanel

Journal of virology

2018 Volume 92, Issue 3

Abstract: Human adenoviruses (HAdVs) are common human pathogens encoding a highly abundant histone-like core protein, VII, which is involved in nuclear delivery and protection of viral DNA as well as in sequestering immune danger signals in infected cells. The ... ...

Abstract	Human adenoviruses (HAdVs) are common human pathogens encoding a highly abundant histone-like core protein, VII, which is involved in nuclear delivery and protection of viral DNA as well as in sequestering immune danger signals in infected cells. The molecular details of how protein VII acts as a multifunctional protein have remained to a large extent enigmatic. Here we report the identification of several cellular proteins interacting with the precursor pVII protein. We show that the cellular E3 ubiquitin ligase MKRN1 is a novel precursor pVII-interacting protein in HAdV-C5-infected cells. Surprisingly, the endogenous MKRN1 protein underwent proteasomal degradation during the late phase of HAdV-C5 infection in various human cell lines. MKRN1 protein degradation occurred independently of the HAdV E1B55K and E4orf6 proteins. We provide experimental evidence that the precursor pVII protein binding enhances MKRN1 self-ubiquitination, whereas the processed mature VII protein is deficient in this function. Based on these data, we propose that the pVII protein binding promotes MKRN1 self-ubiquitination, followed by proteasomal degradation of the MKRN1 protein, in HAdV-C5-infected cells. In addition, we show that measles virus and vesicular stomatitis virus infections reduce the MKRN1 protein accumulation in the recipient cells. Taken together, our results expand the functional repertoire of the HAdV-C5 precursor pVII protein in lytic virus infection and highlight MKRN1 as a potential common target during different virus infections.
MeSH term(s)	Adenovirus Infections, Human/enzymology ; Adenoviruses, Human ; Cell Line ; DNA, Viral/metabolism ; Humans ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Protein Binding ; Protein Precursors/metabolism ; Proteolysis ; Ribonucleoproteins/genetics ; Ribonucleoproteins/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Viral Core Proteins/metabolism ; Virus Replication
Chemical Substances	DNA, Viral ; Makorin ring finger protein 1 ; Nerve Tissue Proteins ; Protein Precursors ; Ribonucleoproteins ; Viral Core Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2018-01-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01154-17
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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: Complementation of the human adenovirus type 5 VA RNAI defect by the Vaccinia virus E3L protein and serotype-specific VA RNAIs.

Inturi, Raviteja / Kamel, Wael / Akusjärvi, Göran / Punga, Tanel

Virology

2015 Volume 485, Page(s) 25–35

Abstract: Human adenoviruses (HAdVs) encode for multifunctional non-coding virus-associated (VA) RNAs, which function as powerful suppressors of the cellular interferon (IFN) and RNA interference (RNAi) systems. In this study we tested the ability of various plant ...

Abstract	Human adenoviruses (HAdVs) encode for multifunctional non-coding virus-associated (VA) RNAs, which function as powerful suppressors of the cellular interferon (IFN) and RNA interference (RNAi) systems. In this study we tested the ability of various plant and animal virus encoded RNAi and IFN suppressor proteins to functionally substitute for the HAdV-5 VA RNAI. Our results revealed that only the Vaccinia virus (VACV) E3L protein was able to substitute for the HAdV-5 VA RNAI functions in virus-infected cells. Interestingly, the E3L protein rescues the translational defect but does not stimulate viral capsid mRNA accumulation observed with VA RNA. We further show that the E3L C-terminal region containing the dsRNA-binding domain is needed to enhance VA RNAI mutant virus replication. Additionally, we show that the HAdV-4 and HAdV-37 VA RNAI are more effective than the HAdV-5 VA RNAI in rescuing virus replication.
MeSH term(s)	Adenoviruses, Human/genetics ; Adenoviruses, Human/metabolism ; Capsid/metabolism ; Gene Expression Regulation, Viral ; Genetic Complementation Test ; HEK293 Cells ; Host-Pathogen Interactions ; Humans ; Oligopeptides/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; RNA Interference ; RNA, Messenger/antagonists & inhibitors ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Viral/antagonists & inhibitors ; RNA, Viral/genetics ; RNA, Viral/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Serogroup ; Transfection ; Vaccinia virus/genetics ; Vaccinia virus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	E3L protein, Vaccinia virus ; Oligopeptides ; RNA, Messenger ; RNA, Viral ; RNA-Binding Proteins ; Viral Proteins ; FLAG peptide (98849-88-8)
Language	English
Publishing date	2015-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2015.07.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.172: Show issues

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

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Adenovirus precursor pVII protein stability is regulated by its propeptide sequence.

Inturi, Raviteja / Thaduri, Srinivas / Punga, Tanel

PloS one

2013 Volume 8, Issue 11, Page(s) e80617

Abstract: Adenovirus encodes for the pVII protein, which interacts and modulates virus DNA structure in the infected cells. The pVII protein is synthesized as the precursor protein and undergoes proteolytic processing by viral proteinase Avp, leading to release of ...

Abstract	Adenovirus encodes for the pVII protein, which interacts and modulates virus DNA structure in the infected cells. The pVII protein is synthesized as the precursor protein and undergoes proteolytic processing by viral proteinase Avp, leading to release of a propeptide sequence and accumulation of the mature VII protein. Here we elucidate the molecular functions of the propeptide sequence present in the precursor pVII protein. The results show that the propeptide is the destabilizing element targeting the precursor pVII protein for proteasomal degradation. Our data further indicate that the propeptide sequence and the lysine residues K26 and K27 regulate the precursor pVII protein stability in a co-dependent manner. We also provide evidence that the Cullin-3 E3 ubiquitin ligase complex alters the precursor pVII protein stability by association with the propeptide sequence. In addition, we show that inactivation of the Cullin-3 protein activity reduces adenovirus E1A gene expression during early phase of virus infection. Collectively, our results indicate a novel function of the adenovirus propeptide sequence and involvement of Cullin-3 in adenovirus gene expression.
MeSH term(s)	Adenoviruses, Human/genetics ; Adenoviruses, Human/metabolism ; Amino Acid Sequence ; Cell Line ; Cell Nucleolus/metabolism ; Cullin Proteins/metabolism ; Gene Expression Regulation, Viral ; Humans ; Lysine/chemistry ; Peptide Fragments/chemistry ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Protein Precursors ; Protein Stability ; Protein Transport ; Proteolysis ; Ubiquitin-Protein Ligases/metabolism ; Viral Core Proteins/chemistry ; Viral Core Proteins/metabolism
Chemical Substances	CUL3 protein, human ; Cullin Proteins ; Peptide Fragments ; Protein Precursors ; Viral Core Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2013-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0080617
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: Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs.

Nature communications

2023 Volume 14, Issue 1, Page(s) 2409

Abstract: Viruses mimic host short linear motifs (SLiMs) to hijack and deregulate cellular functions. Studies of motif-mediated interactions therefore provide insight into virus-host dependencies, and reveal targets for therapeutic intervention. Here, we describe ... ...

Abstract	Viruses mimic host short linear motifs (SLiMs) to hijack and deregulate cellular functions. Studies of motif-mediated interactions therefore provide insight into virus-host dependencies, and reveal targets for therapeutic intervention. Here, we describe the pan-viral discovery of 1712 SLiM-based virus-host interactions using a phage peptidome tiling the intrinsically disordered protein regions of 229 RNA viruses. We find mimicry of host SLiMs to be a ubiquitous viral strategy, reveal novel host proteins hijacked by viruses, and identify cellular pathways frequently deregulated by viral motif mimicry. Using structural and biophysical analyses, we show that viral mimicry-based interactions have similar binding strength and bound conformations as endogenous interactions. Finally, we establish polyadenylate-binding protein 1 as a potential target for broad-spectrum antiviral agent development. Our platform enables rapid discovery of mechanisms of viral interference and the identification of potential therapeutic targets which can aid in combating future epidemics and pandemics.
MeSH term(s)	Bacteriophages/genetics ; Viruses/genetics ; Intrinsically Disordered Proteins/metabolism ; Amino Acid Motifs ; Host-Pathogen Interactions/genetics
Chemical Substances	Intrinsically Disordered Proteins
Language	English
Publishing date	2023-04-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-38015-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Full text online

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

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito