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Article ; Online: Mismatched donor transplantation with post-transplantation cyclophosphamide for advanced cutaneous T-cell lymphoma: a single-center retrospective study.

2022 Volume 63, Issue 12, Page(s) 2987–2991

MeSH term(s)	Humans ; Retrospective Studies ; Cyclophosphamide/adverse effects ; Graft vs Host Disease ; Lymphoma, T-Cell, Cutaneous/drug therapy ; Hematopoietic Stem Cell Transplantation ; Transplantation Conditioning
Chemical Substances	Cyclophosphamide (8N3DW7272P)
Language	English
Publishing date	2022-08-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1042374-6
ISSN	1029-2403 ; 1042-8194
ISSN (online)	1029-2403
ISSN	1042-8194
DOI	10.1080/10428194.2022.2105330
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Article ; Online: Emerging theme: cellular PDZ proteins as common targets of pathogenic viruses.

Javier, Ronald T / Rice, Andrew P

Journal of virology

2011 Volume 85, Issue 22, Page(s) 11544–11556

Abstract: More than a decade ago, three viral oncoproteins, adenovirus type 9 E4-ORF1, human T-lymphotropic ...

Abstract	More than a decade ago, three viral oncoproteins, adenovirus type 9 E4-ORF1, human T-lymphotropic virus type 1 Tax, and high-risk human papillomavirus E6, were found to encode a related carboxyl-terminal PDZ domain-binding motif (PBM) that mediates interactions with a select group of cellular PDZ proteins. Recent studies have shown that many other viruses also encode PBM-containing proteins that bind to cellular PDZ proteins. Interestingly, these recently recognized viruses include not only some with oncogenic potential (hepatitis B virus, rhesus papillomavirus, cottontail rabbit papillomavirus) but also many without this potential (influenza virus, Dengue virus, tick-borne encephalitis virus, rabies virus, severe acute respiratory syndrome coronavirus, human immunodeficiency virus). Examination of the cellular PDZ proteins that are targets of viral PBMs reveals that the viral proteins often interact with the same or similar types of PDZ proteins, most notably Dlg1 and other members of the membrane-associated guanylate kinase protein family, as well as Scribble. In addition, cellular PDZ protein targets of viral PBMs commonly control tight junction formation, cell polarity establishment, and apoptosis. These findings reveal a new theme in virology wherein many different virus families encode proteins that bind and perturb the function of cellular PDZ proteins. The inhibition or perturbation of the function of cellular PDZ proteins appears to be a widely used strategy for viruses to enhance their replication, disseminate in the host, and transmit to new hosts.
MeSH term(s)	Animals ; Host-Pathogen Interactions ; Humans ; Protein Binding ; Protein Interaction Domains and Motifs ; Viral Proteins/metabolism ; Viruses/pathogenicity
Chemical Substances	Viral Proteins
Keywords	covid19
Language	English
Publishing date	2011-07-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.05410-11
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Article ; Online: Multi-omics analysis identifies IgG2b class-switching with ALCAM-CD6 co-stimulation in joint-draining lymph nodes during advanced inflammatory-erosive arthritis.

Kenney, H Mark / Rangel-Moreno, Javier / Peng, Yue / Chen, Kiana L / Bruno, Jennifer / Embong, Abdul / Pritchett, Elizabeth / Fox, Jeffrey I / Becerril-Villanueva, Enrique / Gamboa-Domínguez, Armando / Quataert, Sally / Muthukrishnan, Gowrishankar / Wood, Ronald W / Korman, Benjamin D / Anolik, Jennifer H / Xing, Lianping / Ritchlin, Christopher T / Schwarz, Edward M / Wu, Chia-Lung

Frontiers in immunology

2023 Volume 14, Page(s) 1237498

Abstract: ... lymphatic endothelial cells, macrophages, B-cells, and T-cells) in the joint-draining lymph node sinuses and their associated ... macrophages and T-cells via ALCAM-CD6 co-stimulation, initiating IgG2b class-switching and plasma cell ...

Abstract	Introduction: Defective lymphatic drainage and translocation of B-cells in inflamed (Bin) joint-draining lymph node sinuses are pathogenic phenomena in patients with severe rheumatoid arthritis (RA). However, the molecular mechanisms underlying this lymphatic dysfunction remain poorly understood. Herein, we utilized multi-omic spatial and single-cell transcriptomics to evaluate altered cellular composition (including lymphatic endothelial cells, macrophages, B-cells, and T-cells) in the joint-draining lymph node sinuses and their associated phenotypic changes and cell-cell interactions during RA development using the tumor necrosis factor transgenic (TNF-Tg) mouse model. Methods: Popliteal lymph nodes (PLNs) from wild-type (n=10) and TNF-Tg male mice with "Early" (5 to 6-months of age; n=6) and "Advanced" (>8-months of age; n=12) arthritis were harvested and processed for spatial transcriptomics. Single-cell RNA sequencing (scRNAseq) was performed in PLNs from the TNF-Tg cohorts (n=6 PLNs pooled/cohort). PLN histopathology and ELISPOT along with ankle histology and micro-CT were evaluated. Histopathology of human lymph nodes and synovia was performed for clinical correlation. Results: Advanced PLN sinuses exhibited an increased Discussion: Collectively, these data support a model of flare in chronic TNF-induced arthritis in which loss of lymphatic flow through affected joint-draining lymph nodes facilitates the interaction between effluxing macrophages and T-cells via ALCAM-CD6 co-stimulation, initiating IgG2b class-switching and plasma cell differentiation of the expanded Bin population. Future work is warranted to investigate immunoglobulin clonality and potential autoimmune consequences, as well as the efficacy of anti-CD6 therapy to prevent these pathogenic events.
MeSH term(s)	Animals ; Humans ; Male ; Mice ; Activated-Leukocyte Cell Adhesion Molecule ; Arthritis, Rheumatoid ; Endothelial Cells ; Immunoglobulin G ; Multiomics ; Immunoglobulin Class Switching
Chemical Substances	Activated-Leukocyte Cell Adhesion Molecule ; ALCAM protein, human ; Immunoglobulin G
Language	English
Publishing date	2023-08-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.2023.1237498
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Article ; Online: Evolution of Yin and Yang isoforms of a chromatin remodeling subunit precedes the creation of two genes.

Xu, Wen / Long, Lijiang / Zhao, Yuehui / Stevens, Lewis / Felipe, Irene / Munoz, Javier / Ellis, Ronald E / McGrath, Patrick T

eLife

2019 Volume 8

Abstract: Genes can encode multiple isoforms, broadening their functions and providing a molecular substrate to evolve phenotypic diversity. Evolution of isoform function is a potential route to adapt to new environments. Here we show that de novo, beneficial ... ...

Abstract	Genes can encode multiple isoforms, broadening their functions and providing a molecular substrate to evolve phenotypic diversity. Evolution of isoform function is a potential route to adapt to new environments. Here we show that de novo, beneficial alleles in the
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/genetics ; Evolution, Molecular ; Female ; Gametogenesis ; Male ; Protein Isoforms/genetics
Chemical Substances	Caenorhabditis elegans Proteins ; Chromosomal Proteins, Non-Histone ; NURF-1 protein, C elegans ; Protein Isoforms
Language	English
Publishing date	2019-09-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.48119
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Article ; Online: Hijacking Dlg1 for oncogenic phosphatidylinositol 3-kinase activation in human epithelial cells is a conserved mechanism of human adenovirus E4-ORF1 proteins.

Kumar, Manish / Kong, Kathleen / Javier, Ronald T

Journal of virology

2014 Volume 88, Issue 24, Page(s) 14268–14277

Abstract: ... complex that translocates to the plasma membrane (K. Kong, M. Kumar, M. Taruishi, and R. T. Javier, PLoS ...

Abstract	Unlabelled: The E4-ORF1 gene of human adenoviruses encodes a 14-kDa protein that promotes viral replication as well as cellular metabolic reprogramming, survival, and transformation by constitutively activating cellular phosphatidylinositol 3-kinase (PI3K). We recently reported that the E4-ORF1 protein from subgroup D human adenovirus type 9 upregulates and oncogenically activates PI3K by a novel mechanism involving separate interactions of E4-ORF1 with cellular discs large 1 (Dlg1) and PI3K to form a ternary complex that translocates to the plasma membrane (K. Kong, M. Kumar, M. Taruishi, and R. T. Javier, PLoS Pathog. 10:e1004102, 2014, doi:10.1371/journal.ppat.1004102). The current study was carried out to investigate whether other human adenovirus E4-ORF1 proteins share this mechanism of action. The results showed that in human MCF10A epithelial cells, stable expression of E4-ORF1 proteins encoded by representative human adenovirus serotypes from subgroups A to D induce ternary complex formation, Dlg1-dependent PI3K activation, PI3K protein elevation, Dlg1 and PI3K membrane recruitment, and PI3K-dependent cellular transformation. The first three of these E4-ORF1 activities were also observed in MCF10A cells infected with each wild-type human adenovirus from subgroups A to D. Our findings indicate that most, if not all, human adenovirus E4-ORF1 proteins share a conserved molecular mechanism of PI3K activation, which confers a common capacity to promote oncogenic transformation in human epithelial cells. Importance: PI3K activation by the adenovirus E4-ORF1 protein mediates oncogenic cellular transformation by human adenovirus type 9, augments viral protein expression and replication by human adenovirus type 5, and dysregulates cellular glucose and lipid metabolism by human adenovirus type 36. For the first time, we report that E4-ORF1 proteins from human adenoviruses in subgroups A to D evolved a conserved molecular mechanism to mediate constitutive PI3K activation that can provoke oncogenic transformation in human epithelial cells. The results raise potential safety concerns about the use of vectors encoding the E4-ORF1 gene in human gene therapy and vaccination. Our findings further suggest that the conserved mechanism revealed here may be targeted for development of therapeutic drugs to treat and prevent adenovirus-associated human diseases.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Adenovirus E4 Proteins/metabolism ; Adenoviruses, Human/physiology ; Cell Line ; Discs Large Homolog 1 Protein ; Epithelial Cells/virology ; Host-Pathogen Interactions ; Humans ; Membrane Proteins/metabolism ; Phosphatidylinositol 3-Kinase/metabolism ; Protein Binding ; Protein Multimerization
Chemical Substances	Adaptor Proteins, Signal Transducing ; Adenovirus E4 Proteins ; DLG1 protein, human ; Discs Large Homolog 1 Protein ; Membrane Proteins ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137)
Language	English
Publishing date	2014-09-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.02324-14
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Article ; Online: Evolution of Yin and Yang isoforms of a chromatin remodeling subunit precedes the creation of two genes

Wen Xu / Lijiang Long / Yuehui Zhao / Lewis Stevens / Irene Felipe / Javier Munoz / Ronald E Ellis / Patrick T McGrath

eLife, Vol

2019 Volume 8

Abstract	Genes can encode multiple isoforms, broadening their functions and providing a molecular substrate to evolve phenotypic diversity. Evolution of isoform function is a potential route to adapt to new environments. Here we show that de novo, beneficial alleles in the nurf-1 gene became fixed in two laboratory lineages of C. elegans after isolation from the wild in 1951, before methods of cryopreservation were developed. nurf-1 encodes an ortholog of BPTF, a large (>300 kD) multidomain subunit of the NURF chromatin remodeling complex. Using CRISPR-Cas9 genome editing and transgenic rescue, we demonstrate that in C. elegans, nurf-1 has split into two, largely non-overlapping isoforms (NURF-1.D and NURF-1.B, which we call Yin and Yang, respectively) that share only two of 26 exons. Both isoforms are essential for normal gametogenesis but have opposite effects on male/female gamete differentiation. Reproduction in hermaphrodites, which involves production of both sperm and oocytes, requires a balance of these opposing Yin and Yang isoforms. Transgenic rescue and genetic position of the fixed mutations suggest that different isoforms are modified in each laboratory strain. In a related clade of Caenorhabditis nematodes, the shared exons have duplicated, resulting in the split of the Yin and Yang isoforms into separate genes, each containing approximately 200 amino acids of duplicated sequence that has undergone accelerated protein evolution following the duplication. Associated with this duplication event is the loss of two additional nurf-1 transcripts, including the long-form transcript and a newly identified, highly expressed transcript encoded by the duplicated exons. We propose these lost transcripts are non-functional side products necessary to transcribe the Yin and Yang transcripts in the same cells. Our work demonstrates how gene sharing, through the production of multiple isoforms, can precede the creation of new, independent genes.
Keywords	other Caenorhabditis species ; Isoform evolution ; adaptive conflict ; alternative transcripts ; chromatin remodeling ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2019-09-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article ; Online: Adenovirus E4-ORF1 Dysregulates Epidermal Growth Factor and Insulin/Insulin-Like Growth Factor Receptors To Mediate Constitutive Myc Expression.

Kong, Kathleen / Kumar, Manish / Taruishi, Midori / Javier, Ronald T

Journal of virology

2015 Volume 89, Issue 21, Page(s) 10774–10785

Abstract: Unlabelled: The E4-ORF1 protein encoded by human adenovirus stimulates viral replication in human epithelial cells by binding and activating cellular phosphatidylinositol 3-kinase (PI3K) at the plasma membrane and cellular Myc in the nucleus. In this ... ...

Abstract	Unlabelled: The E4-ORF1 protein encoded by human adenovirus stimulates viral replication in human epithelial cells by binding and activating cellular phosphatidylinositol 3-kinase (PI3K) at the plasma membrane and cellular Myc in the nucleus. In this study, we showed that E4-ORF1 hijacks the tyrosine kinase activities of cellular epidermal growth factor receptor (EGFR) and insulin receptor (InsR)/insulin-like growth factor receptor 1 (IGF1R), as well as the lipid kinase activity of PI3K, to mediate constitutive Myc protein expression. We additionally demonstrated that EGFR contributes to constitutive Myc expression through the capacity of E4-ORF1 to induce ligand-independent EGFR activation and stimulation of the Ras/Mek/Erk pathway, the latter activity of which was conserved by human adenoviruses. Results further suggested that EGFR normally forms a complex with the cellular PDZ protein Discs Large 1 (Dlg1), a component of the Dlg1:E4-ORF1:PI3K ternary complex that mediates E4-ORF1-induced PI3K activation, and that E4-ORF1 binds the Dlg1:EGFR complex and promotes the association of EGFR with InsR and IGF1R. In addition to its role in constitutive Myc expression, InsR/IGF1R also negatively regulates EGFR autophosphorylation and EGFR-mediated Ras/Mek/Erk signaling, and data suggested that E4-ORF1 binding to Dlg1 antagonizes these activities. Collectively, our findings suggest that in human epithelial cells, E4-ORF1 targets EGFR, InsR/IGF1R, and PI3K at the plasma membrane to activate cytosolic signaling pathways that sustain Myc protein levels in the nucleus. We postulate that E4-ORF1-induced constitutive Myc expression functions to ensure the formation of nuclear E4-ORF1:Myc complexes, which have been shown to activate Myc and to enhance adenovirus replication. Importance: While human adenoviruses primarily produce self-limited acute infections in humans, these agents are associated with life-threatening diseases in immunocompromised patients and in otherwise healthy individuals infected with certain virulent serotypes. The adenovirus E4-ORF1 protein enhances viral replication by activating the cellular lipid kinase PI3K and the cellular transcription factor Myc. Here we report that E4-ORF1 usurps the functions of the cellular tyrosine kinase receptors EGFR and InsR /: IGF1R, as well as PI3K, to sustain Myc protein expression in cells. Furthermore, sustained Myc expression depended on E4-ORF1-induced ligand-independent EGFR activation that stimulated Ras/Mek/Erk signaling, a function found to be conserved by human adenoviruses. Given the established roles of PI3K, the Ras/Mek/Erk pathway, and Myc in the adenovirus life cycle, our findings may aid in the development of safer, more effective therapeutic strategies to treat severe adenovirus infections as well as improved adenovirus vectors for use in vaccination and gene and cancer therapy.
MeSH term(s)	Adenoviridae/genetics ; Adenoviridae/metabolism ; Adenovirus E4 Proteins/metabolism ; Analysis of Variance ; Epidermal Growth Factor/metabolism ; Gene Expression Regulation, Viral/physiology ; Humans ; Immunoblotting ; Immunoprecipitation ; Open Reading Frames/genetics ; Proto-Oncogene Proteins c-myc/metabolism ; Receptors, Somatomedin/metabolism
Chemical Substances	Adenovirus E4 Proteins ; MYC protein, human ; Proto-Oncogene Proteins c-myc ; Receptors, Somatomedin ; Epidermal Growth Factor (62229-50-9)
Language	English
Publishing date	2015-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01463-15
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Article ; Online: The human adenovirus E4-ORF1 protein subverts discs large 1 to mediate membrane recruitment and dysregulation of phosphatidylinositol 3-kinase.

Kong, Kathleen / Kumar, Manish / Taruishi, Midori / Javier, Ronald T

PLoS pathogens

2014 Volume 10, Issue 5, Page(s) e1004102

Abstract: ... papillomavirus, human T-cell leukemia virus type 1, and influenza A virus, which also target Dlg1 and activate ...

Abstract	Adenoviruses infect epithelial cells lining mucous membranes to cause acute diseases in people. They are also utilized as vectors for vaccination and for gene and cancer therapy, as well as tools to discover mechanisms of cancer due to their tumorigenic potential in experimental animals. The adenovirus E4-ORF1 gene encodes an oncoprotein that promotes viral replication, cell survival, and transformation by activating phosphatidylinositol 3-kinase (PI3K). While the mechanism of activation is not understood, this function depends on a complex formed between E4-ORF1 and the membrane-associated cellular PDZ protein Discs Large 1 (Dlg1), a common viral target having both tumor suppressor and oncogenic functions. Here, we report that in human epithelial cells, E4-ORF1 interacts with the regulatory and catalytic subunits of PI3K and elevates their levels. Like PI3K activation, PI3K protein elevation by E4-ORF1 requires Dlg1. We further show that Dlg1, E4-ORF1, and PI3K form a ternary complex at the plasma membrane. At this site, Dlg1 also co-localizes with the activated PI3K effector protein Akt, indicating that the ternary complex mediates PI3K signaling. Signifying the functional importance of the ternary complex, the capacity of E4-ORF1 to induce soft agar growth and focus formation in cells is ablated either by a mutation that prevents E4-ORF1 binding to Dlg1 or by a PI3K inhibitor drug. These results demonstrate that E4-ORF1 interacts with Dlg1 and PI3K to assemble a ternary complex where E4-ORF1 hijacks the Dlg1 oncogenic function to relocate cytoplasmic PI3K to the membrane for constitutive activation. This novel mechanism of Dlg1 subversion by adenovirus to dysregulate PI3K could be used by other pathogenic viruses, such as human papillomavirus, human T-cell leukemia virus type 1, and influenza A virus, which also target Dlg1 and activate PI3K in cells.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Adenoviridae Infections/metabolism ; Adenoviridae Infections/pathology ; Cell Membrane/metabolism ; Cell Transformation, Viral/genetics ; Cells, Cultured ; Discs Large Homolog 1 Protein ; Enzyme Activation ; Epithelial Cells/metabolism ; Epithelial Cells/virology ; HeLa Cells ; Host-Pathogen Interactions ; Humans ; Membrane Proteins/metabolism ; Oncogene Proteins, Viral/metabolism ; Oncogene Proteins, Viral/physiology ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Binding ; Protein Transport
Chemical Substances	Adaptor Proteins, Signal Transducing ; DLG1 protein, human ; Discs Large Homolog 1 Protein ; E4 protein, Adenovirus 9 ; Membrane Proteins ; Oncogene Proteins, Viral
Language	English
Publishing date	2014-05-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1004102
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Article ; Online: The human adenovirus E4-ORF1 protein subverts discs large 1 to mediate membrane recruitment and dysregulation of phosphatidylinositol 3-kinase.

Kathleen Kong / Manish Kumar / Midori Taruishi / Ronald T Javier

PLoS Pathogens, Vol 10, Iss 5, p e

2014 Volume 1004102

Abstract: ... papillomavirus, human T-cell leukemia virus type 1, and influenza A virus, which also target Dlg1 and activate ...

Abstract	Adenoviruses infect epithelial cells lining mucous membranes to cause acute diseases in people. They are also utilized as vectors for vaccination and for gene and cancer therapy, as well as tools to discover mechanisms of cancer due to their tumorigenic potential in experimental animals. The adenovirus E4-ORF1 gene encodes an oncoprotein that promotes viral replication, cell survival, and transformation by activating phosphatidylinositol 3-kinase (PI3K). While the mechanism of activation is not understood, this function depends on a complex formed between E4-ORF1 and the membrane-associated cellular PDZ protein Discs Large 1 (Dlg1), a common viral target having both tumor suppressor and oncogenic functions. Here, we report that in human epithelial cells, E4-ORF1 interacts with the regulatory and catalytic subunits of PI3K and elevates their levels. Like PI3K activation, PI3K protein elevation by E4-ORF1 requires Dlg1. We further show that Dlg1, E4-ORF1, and PI3K form a ternary complex at the plasma membrane. At this site, Dlg1 also co-localizes with the activated PI3K effector protein Akt, indicating that the ternary complex mediates PI3K signaling. Signifying the functional importance of the ternary complex, the capacity of E4-ORF1 to induce soft agar growth and focus formation in cells is ablated either by a mutation that prevents E4-ORF1 binding to Dlg1 or by a PI3K inhibitor drug. These results demonstrate that E4-ORF1 interacts with Dlg1 and PI3K to assemble a ternary complex where E4-ORF1 hijacks the Dlg1 oncogenic function to relocate cytoplasmic PI3K to the membrane for constitutive activation. This novel mechanism of Dlg1 subversion by adenovirus to dysregulate PI3K could be used by other pathogenic viruses, such as human papillomavirus, human T-cell leukemia virus type 1, and influenza A virus, which also target Dlg1 and activate PI3K in cells.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2014-05-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: MRI and Ultrasound Imaging of the Shoulder Using Positional Maneuvers.

Beltran, Luis S / Adler, Ronald / Stone, Taylor / Surace, Joseph / Beltran, Javier / Bencardino, Jenny T

AJR. American journal of roentgenology

2015 Volume 205, Issue 3, Page(s) W244–54

Abstract: Objective: The purpose of this article is to review the normal anatomy and pathologic conditions of the shoulder on the basis of the appearance on MR and ultrasound images obtained during performance of abduction external rotation and flexion adduction ... ...

Abstract	Objective: The purpose of this article is to review the normal anatomy and pathologic conditions of the shoulder on the basis of the appearance on MR and ultrasound images obtained during performance of abduction external rotation and flexion adduction internal rotation positional maneuvers. Conclusion: Positional MRI and ultrasound are highly useful in evaluation of the shoulder. Knowledge of the normal appearance of anatomic structures and pathologic changes in nontraditional imaging planes is necessary to avoid pitfalls in interpretation.
MeSH term(s)	Arthrography ; Humans ; Joint Diseases/diagnosis ; Magnetic Resonance Imaging ; Patient Positioning ; Shoulder Joint/diagnostic imaging ; Shoulder Joint/pathology ; Ultrasonography
Language	English
Publishing date	2015-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	82076-3
ISSN	1546-3141 ; 0361-803X ; 0092-5381
ISSN (online)	1546-3141
ISSN	0361-803X ; 0092-5381
DOI	10.2214/AJR.15.14512
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