LIVIVO - Search results -

Search results

Result 1 - 10 of total 45

Search options

Article ; Online: Special Issue "New Frontiers in Small DNA Virus Research".

Strati, Katerina / Pyeon, Dohun

2023 Volume 15, Issue 1

Abstract: Scientific progress in understanding, preventing, treating, and managing viral infections and associated diseases exemplifies the extent to which research on small DNA tumor viruses has impacted human health [ ... ]. ...

Abstract	Scientific progress in understanding, preventing, treating, and managing viral infections and associated diseases exemplifies the extent to which research on small DNA tumor viruses has impacted human health [...].
MeSH term(s)	Humans ; DNA Viruses/genetics ; Virus Diseases ; DNA Tumor Viruses
Language	English
Publishing date	2023-01-16
Publishing country	Switzerland
Document type	Editorial ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v15010259
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article ; Online: The Chemokine CXCL14 as a Potential Immunotherapeutic Agent for Cancer Therapy.

Giacobbi, Nicholas S / Mullapudi, Shreya / Nabors, Harrison / Pyeon, Dohun

Viruses

2024 Volume 16, Issue 2

Abstract: There is great enthusiasm toward the development of novel immunotherapies for the treatment of cancer, and given their roles in immune system regulation, chemokines stand out as promising candidates for use in new cancer therapies. Many previous studies ... ...

Abstract	There is great enthusiasm toward the development of novel immunotherapies for the treatment of cancer, and given their roles in immune system regulation, chemokines stand out as promising candidates for use in new cancer therapies. Many previous studies have shown how chemokine signaling pathways could be targeted to halt cancer progression. We and others have revealed that the chemokine CXCL14 promotes antitumor immune responses, suggesting that CXCL14 may be effective for cancer immunotherapy. However, it is still unknown what mechanism governs CXCL14-mediated antitumor activity, how to deliver CXCL14, what dose to apply, and what combinations with existing therapy may boost antitumor immune responses in cancer patients. Here, we provide updates on the role of CXCL14 in cancer progression and discuss the potential development and application of CXCL14 as an immunotherapeutic agent.
MeSH term(s)	Humans ; Chemokines ; Chemokines, CXC ; Immunotherapy ; Neoplasms/therapy ; Neoplasms/pathology
Chemical Substances	Chemokines ; Chemokines, CXC ; CXCL14 protein, human
Language	English
Publishing date	2024-02-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v16020302
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: APOBEC3: Friend or Foe in Human Papillomavirus Infection and Oncogenesis?

Warren, Cody J / Santiago, Mario L / Pyeon, Dohun

Annual review of virology

2022 Volume 9, Issue 1, Page(s) 375–395

Abstract: Human papillomavirus (HPV) infection is a causative agent of multiple human cancers, including cervical and head and neck cancers. In these HPV-positive tumors, somatic mutations are caused by aberrant activation of DNA mutators such as members of the ... ...

Abstract	Human papillomavirus (HPV) infection is a causative agent of multiple human cancers, including cervical and head and neck cancers. In these HPV-positive tumors, somatic mutations are caused by aberrant activation of DNA mutators such as members of the apolipoprotein B messenger RNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3) family of cytidine deaminases. APOBEC3 proteins are most notable for their restriction of various viruses, including anti-HPV activity. However, the potential role of APOBEC3 proteins in HPV-induced cancer progression has recently garnered significant attention. Ongoing research stems from the observations that elevated APOBEC3 expression is driven by HPV oncogene expression and that APOBEC3 activity is likely a significant contributor to somatic mutagenesis in HPV-positive cancers. This review focuses on recent advances in the study of APOBEC3 proteins and their roles in HPV infection and HPV-driven oncogenesis. Further, we discuss critical gaps and unanswered questions in our understanding of APOBEC3 in virus-associated cancers.
MeSH term(s)	APOBEC Deaminases/genetics ; Apolipoproteins ; Carcinogenesis/genetics ; Cytidine ; Humans ; Neoplasms ; Papillomavirus Infections/genetics ; Papillomavirus Infections/metabolism ; Peptides ; Proteins/genetics ; RNA, Messenger
Chemical Substances	Apolipoproteins ; Peptides ; Proteins ; RNA, Messenger ; Cytidine (5CSZ8459RP) ; APOBEC Deaminases (EC 3.5.4.5) ; APOBEC3 proteins, human (EC 3.5.4.5)
Language	English
Publishing date	2022-06-07
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2764224-0
ISSN	2327-0578 ; 2327-056X
ISSN (online)	2327-0578
ISSN	2327-056X
DOI	10.1146/annurev-virology-092920-030354
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: The membrane-associated ubiquitin ligase MARCHF8 stabilizes the human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in head and neck cancer.

Khalil, Mohamed I / Yang, Canchai / Vu, Lexi / Chadha, Smriti / Nabors, Harrison / James, Claire D / Morgan, Iain M / Pyeon, Dohun

Journal of virology

2024 Volume 98, Issue 2, Page(s) e0172623

Abstract: The human papillomavirus (HPV) oncoprotein E7 is a relatively short-lived protein required for HPV-driven cancer development and maintenance. E7 is degraded through ubiquitination mediated by cullin 1 (CUL1) and the ubiquitin-conjugating enzyme E2 L3 ( ... ...

Abstract	The human papillomavirus (HPV) oncoprotein E7 is a relatively short-lived protein required for HPV-driven cancer development and maintenance. E7 is degraded through ubiquitination mediated by cullin 1 (CUL1) and the ubiquitin-conjugating enzyme E2 L3 (UBE2L3). However, E7 proteins are maintained at high levels in most HPV-positive cancer cells. A previous proteomics study has shown that UBE2L3 and CUL1 protein levels are increased by the knockdown of the E3 ubiquitin ligase membrane-associated ring-CH-type finger 8 (MARCHF8). We have recently demonstrated that HPV16 upregulates MARCHF8 expression in HPV-positive keratinocytes and head and neck cancer (HPV+ HNC) cells. Here, we report that MARCHF8 stabilizes the HPV16 E7 protein by degrading the components of the S-phase kinase-associated protein 1-CUL1-F-box ubiquitin ligase complex in HPV+ HNC cells. We found that
MeSH term(s)	Humans ; Cullin Proteins/genetics ; Cullin Proteins/metabolism ; Head and Neck Neoplasms/genetics ; Human Papillomavirus Viruses ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/metabolism ; Papillomavirus E7 Proteins/genetics ; Papillomavirus E7 Proteins/metabolism ; Papillomavirus Infections/pathology ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Cullin 1 ; Cullin Proteins ; Oncogene Proteins, Viral ; Papillomavirus E7 Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; UBE2L3 protein, human (EC 2.3.2.23) ; Ubiquitin ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; MARCHF8 protein, human (EC 2.3.2.27)
Language	English
Publishing date	2024-01-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01726-23
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: The Key Differences between Human Papillomavirus-Positive and -Negative Head and Neck Cancers: Biological and Clinical Implications.

Powell, Steven F / Vu, Lexi / Spanos, William C / Pyeon, Dohun

Cancers

2021 Volume 13, Issue 20

Abstract: Head and neck squamous cell carcinoma (HNSCC) is a unique malignancy associated with two distinct risk factors: exposure to typical carcinogens and infection of human papillomavirus (HPV). HPV encodes the potent oncoproteins E6 and E7, which bypass many ... ...

Abstract	Head and neck squamous cell carcinoma (HNSCC) is a unique malignancy associated with two distinct risk factors: exposure to typical carcinogens and infection of human papillomavirus (HPV). HPV encodes the potent oncoproteins E6 and E7, which bypass many important oncogenic processes and result in cancer development. In contrast, HPV-negative HNSCC is developed through multiple mutations in diverse oncogenic driver genes. While the risk factors associated with HPV-positive and HPV-negative HNSCCs are discrete, HNSCC patients still show highly complex molecular signatures, immune infiltrations, and treatment responses even within the same anatomical subtypes. Here, we summarize the current understanding of biological mechanisms, treatment approaches, and clinical outcomes in comparison between HPV-positive and -negative HNSCCs.
Language	English
Publishing date	2021-10-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13205206
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Rational Design and Synthesis of D-galactosyl Lysophospholipids as Selective Substrates and non-ATP-competitive Inhibitors of Phosphatidylinositol Phosphate Kinases.

Sun, Mengxia / Zhang, Chi / Sui, Dexin / Yang, Canchai / Pyeon, Dohun / Huang, Xuefei / Hu, Jian

Chemistry (Weinheim an der Bergstrasse, Germany)

2022 Volume 29, Issue 2, Page(s) e202202083

Abstract: Phosphatidylinositol phosphate kinases (PIPKs) produce lipid signaling molecules and have been attracting increasing attention as drug targets for cancer, neurodegenerative diseases, and viral infection. Given the potential cross-inhibition of kinases ... ...

Abstract	Phosphatidylinositol phosphate kinases (PIPKs) produce lipid signaling molecules and have been attracting increasing attention as drug targets for cancer, neurodegenerative diseases, and viral infection. Given the potential cross-inhibition of kinases and other ATP-utilizing enzymes by ATP-competitive inhibitors, targeting the unique lipid substrate binding site represents a superior strategy for PIPK inhibition. Here, by taking advantage of the nearly identical stereochemistry between myo-inositol and D-galactose, we designed and synthesized a panel of D-galactosyl lysophospholipids, one of which was found to be a selective substrate of phosphatidylinositol 4-phosphate 5-kinase. Derivatization of this compound led to the discovery of a human PIKfyve inhibitor with an apparent IC
MeSH term(s)	Humans ; COVID-19 ; Galactose ; Lysophospholipids ; Phosphates ; Phosphatidylinositol Phosphates ; Phosphatidylinositols/metabolism ; SARS-CoV-2/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/metabolism
Chemical Substances	Galactose (X2RN3Q8DNE) ; Lysophospholipids ; Phosphates ; Phosphatidylinositol Phosphates ; Phosphatidylinositols ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-)
Language	English
Publishing date	2022-11-24
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1478547-X
ISSN	1521-3765 ; 0947-6539
ISSN (online)	1521-3765
ISSN	0947-6539
DOI	10.1002/chem.202202083
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: The membrane-associated ubiquitin ligase MARCHF8 stabilizes the human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in head and neck cancer.

Khalil, Mohamed I / Yang, Canchai / Vu, Lexi / Chadha, Smriti / Nabors, Harrison / James, Claire D / Morgan, Iain M / Pyeon, Dohun

bioRxiv : the preprint server for biology

2023

Abstract	The human papillomavirus (HPV) oncoprotein E7 is a relatively short-lived protein required for HPV-driven cancer development and maintenance. E7 is degraded through ubiquitination mediated by cullin 1 (CUL1) and the ubiquitin-conjugating enzyme E2 L3 (UBE2L3). However, E7 proteins are maintained at high levels in most HPV-positive cancer cells. A previous proteomics study has shown that UBE2L3 and CUL1 protein levels are increased by the knockdown of the E3 ubiquitin ligase membrane-associated ring-CH-type finger 8 (MARCHF8). We have recently demonstrated that HPV upregulates MARCHF8 expression in HPV-positive keratinocytes and head and neck cancer (HPV+ HNC) cells. Here, we report that MARCHF8 stabilizes the E7 protein by degrading the components of the SKP1-CUL1-F-box (SCF) ubiquitin ligase complex in HPV+ HNC cells. We found that
Language	English
Publishing date	2023-11-04
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.11.03.565564
Database	MEDical Literature Analysis and Retrieval System OnLINE

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 ▾

Article ; Online: The antiviral immune forces awaken in the cancer wars.

Pyeon, Dohun / Vu, Lexi / Giacobbi, Nicholas S / Westrich, Joseph A

PLoS pathogens

2020 Volume 16, Issue 9, Page(s) e1008814

MeSH term(s)	Antigens, Neoplasm/immunology ; Antiviral Agents/metabolism ; Humans ; Immunity, Innate/immunology ; Neoplasms/drug therapy ; Neoplasms/immunology ; Neoplasms/metabolism ; Neoplasms/virology ; Viruses/immunology
Chemical Substances	Antigens, Neoplasm ; Antiviral Agents
Language	English
Publishing date	2020-09-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.1008814
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: DNA Tumor Virus Regulation of Host DNA Methylation and Its Implications for Immune Evasion and Oncogenesis.

Kuss-Duerkop, Sharon K / Westrich, Joseph A / Pyeon, Dohun

Viruses

2018 Volume 10, Issue 2

Abstract: Viruses have evolved various mechanisms to evade host immunity and ensure efficient viral replication and persistence. Several DNA tumor viruses modulate host DNA methyltransferases for epigenetic dysregulation of immune-related gene expression in host ... ...

Abstract	Viruses have evolved various mechanisms to evade host immunity and ensure efficient viral replication and persistence. Several DNA tumor viruses modulate host DNA methyltransferases for epigenetic dysregulation of immune-related gene expression in host cells. The host immune responses suppressed by virus-induced aberrant DNA methylation are also frequently involved in antitumor immune responses. Here, we describe viral mechanisms and virus-host interactions by which DNA tumor viruses regulate host DNA methylation to evade antiviral immunity, which may contribute to the generation of an immunosuppressive microenvironment during cancer development. Recent trials of immunotherapies have shown promising results to treat multiple cancers; however, a significant number of non-responders necessitate identifying additional targets for cancer immunotherapies. Thus, understanding immune evasion mechanisms of cancer-causing viruses may provide great insights for reversing immune suppression to prevent and treat associated cancers.
MeSH term(s)	Cell Transformation, Neoplastic/genetics ; Cell Transformation, Viral ; DNA Methylation ; DNA Tumor Viruses/classification ; DNA Tumor Viruses/physiology ; Host-Pathogen Interactions ; Humans ; Immune Evasion ; Tumor Virus Infections/complications ; Tumor Virus Infections/genetics ; Tumor Virus Infections/virology
Language	English
Publishing date	2018-02-13
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v10020082
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Interaction between Nef and INI1/SMARCB1 augments replicability of HIV-1 in resting human peripheral blood mononuclear cells.

Pyeon, Dohun / Park, In-Woo

Archives of virology

2015 Volume 160, Issue 3, Page(s) 727–737

Abstract: A central feature of HIV-1 infection is the inability of entering virus to integrate into chromosomes of resting T lymphocytes unless they are mitogenically activated. In contrast, SIVpbj1.9 replicates in initially resting T lymphocytes by activating ... ...

Abstract	A central feature of HIV-1 infection is the inability of entering virus to integrate into chromosomes of resting T lymphocytes unless they are mitogenically activated. In contrast, SIVpbj1.9 replicates in initially resting T lymphocytes by activating infected cells. Previous reports have shown that a difference in Nef-mediated T cell activation between HIV-1 and SIVpbj1.9 plays a critical role in the differing abilities of these viruses to replicate in resting lymphocytes. However, the molecular details of these differences are still unclear. Here, we show that infection with a chimeric virus, HSIVnef, which harbors the 5' 308 nucleotides of SIVpbj1.9 nef in place of the 5' 221 nucleotides of HIV-1 nef in the HIV-1 proviral backbone, resulted in integration of the provirus into host chromosomes without mitogenic activation and thereby replication in resting human PBMCs (hPBMCs). These results indicate that Nef is an essential viral determinant for the integration of provirus into host chromosomes in resting T cells. Using the yeast two-hybrid system, we identified integrase interactor-1 (INI1/SMARCB1) as a cellular factor that is involved in the integration process via interaction with Nef. Although INI1 interacted with both SIVpbj1.9 and HIV-1 Nefs, SIVpbj1.9 Nef, but not HIV-1 Nef, enhanced proviral integration into host DNA. Furthermore, mutational analysis revealed that the basic-amino-acid-rich amino-terminal domain in SIVpbj1.9 Nef is crucial for interaction with INI1 and virus replication in resting hPBMCs. Taken together, these data indicate that Nef is a critical viral protein for incorporating nascent proviral DNA into host chromosomes in resting PBMCs and that this occurs through interaction with INI1. This elucidates the basis for replication of the integrated provirus when the host cell is in a resting state.
MeSH term(s)	Chromosomal Proteins, Non-Histone/metabolism ; DNA-Binding Proteins/metabolism ; HIV-1/physiology ; Host-Pathogen Interactions ; Humans ; Leukocytes, Mononuclear/virology ; Protein Binding ; Protein Interaction Mapping ; Recombination, Genetic ; SMARCB1 Protein ; Simian Immunodeficiency Virus/genetics ; Transcription Factors/metabolism ; Two-Hybrid System Techniques ; Virus Integration ; Virus Replication ; nef Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; SMARCB1 Protein ; SMARCB1 protein, human ; Transcription Factors ; nef Gene Products, Human Immunodeficiency Virus ; nef protein, Human immunodeficiency virus 1
Language	English
Publishing date	2015-03
Publishing country	Austria
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	7491-3
ISSN	1432-8798 ; 0304-8608
ISSN (online)	1432-8798
ISSN	0304-8608
DOI	10.1007/s00705-014-2315-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ud II Zs.110: 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 ▾

To top

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito