1
40
3
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Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1007/bf01323238" target="_blank" rel="noreferrer noopener">http://doi.org/10.1007/bf01323238</a>
Pages
2163–2181
Issue
12
Volume
140
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
A block in glycoprotein processing correlates with small plaque morphology and virion targetting to cell-cell junctions for an oral and an anal strain of herpes simplex virus type-1.
Publisher
An entity responsible for making the resource available
Archives of virology
Date
A point or period of time associated with an event in the lifecycle of the resource
1995
1995
Subject
The topic of the resource
*Protein Processing; Anal Canal/virology; Animals; Cercopithecus aethiops; Electron; Fluorescent Antibody Technique; Genetic Complementation Test; Herpesvirus 1; Human/genetics/isolation & purification/*physiology; Humans; Indirect; Intercellular Junctions/physiology/*virology; Kinetics; Microscopy; Mouth/virology; Post-Translational; Species Specificity; Vero Cells; Viral Envelope Proteins/*biosynthesis/metabolism; Viral Plaque Assay; Virion/*physiology
Creator
An entity primarily responsible for making the resource
Dick J W; Rosenthal K S
Description
An account of the resource
The characteristics of two clinical isolates of HSV-1 obtained from an oral (424) and an anal (490) lesion were compared with the highly passaged KOS strain. In contrast to KOS, the clinical isolates produced small plaques, were more cell-associated and the predominant viral glycoprotein species for gC and gD in infected cell lysates was the precursor, high mannose glycoform. Total virus production in Vero cells was equivalent for the three virus strains in one-step growths. Pulse-chase studies of glycoprotein C processing showed a reduction in rate at 7.5 h post infection and a significant block in processing at 10.5 h post infection for 424 and 490 but not KOS. Similar results were obtained for gD. The significant reduction in glycoprotein processing for 424 and 490 suggests a block in transport of viral glycoproteins or virions to and through the Golgi apparatus. Extracellular virions and the cell surface, prior to cell lysis, contained the processed gC glycoform suggesting a competent cellular glycan processing system. Upon co-infection of 424 or 490 with KOS or a gC- KOS strain, gC was processed to levels equivalent to KOS indicating that 424 and 490 are not inhibitory but that an activity(s) encoded by KOS facilitates maturation of gC from 424 and 490. Unlike KOS infected Vero cells, virion-containing vacuoles were observed in the cytoplasm at 12 h p.i. and extracellular virions were concentrated at cell-cell junctions of 424 or 490 infected cells but not in the perinuclear region. These results suggest that intracellular transport of viral glycoproteins and virions in 424 and 490 infected cells is different from KOS infected cells. The reduced level of viral glycoprotein maturation, virus release, cell surface presence and presence of virions at cell-cell junctions are consistent with small plaque production in tissue culture cells.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1007/bf01323238" target="_blank" rel="noreferrer noopener">10.1007/bf01323238</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Protein Processing
1995
Anal Canal/virology
Animals
Archives of virology
Cercopithecus aethiops
Dick J W
Electron
Fluorescent Antibody Technique
Genetic Complementation Test
Herpesvirus 1
Human/genetics/isolation & purification/*physiology
Humans
Indirect
Intercellular Junctions/physiology/*virology
Kinetics
Microscopy
Mouth/virology
Post-Translational
Rosenthal K S
Species Specificity
Vero Cells
Viral Envelope Proteins/*biosynthesis/metabolism
Viral Plaque Assay
Virion/*physiology
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1074/jbc.M111553200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M111553200</a>
Pages
11423–11431
Issue
13
Volume
277
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
An N-terminal arginine-rich cluster and a proline-alanine-threonine repeat region determine the cellular localization of the herpes simplex virus type 1 ICP34.5 protein and its ligand, protein phosphatase 1.
Publisher
An entity responsible for making the resource available
The Journal of biological chemistry
Date
A point or period of time associated with an event in the lifecycle of the resource
2002
2002-03
Subject
The topic of the resource
*Repetitive Sequences; Alanine/metabolism; Amino Acid; Amino Acid Sequence; Animals; Arginine/metabolism; Base Sequence; Cell Compartmentation; Cercopithecus aethiops; DNA Primers; Fluorescent Antibody Technique; Indirect; Ligands; Molecular Sequence Data; Phosphoprotein Phosphatases/*metabolism; Proline/metabolism; Protein Phosphatase 1; Recombinant Proteins/chemistry/metabolism; Subcellular Fractions/metabolism; Threonine/metabolism; Vero Cells; Viral Proteins/chemistry/*metabolism
Creator
An entity primarily responsible for making the resource
Mao Hanwen; Rosenthal Kenneth S
Description
An account of the resource
The ICP34.5 protein facilitates herpes simplex virus replication by binding and activating protein phosphatase 1 (PP1) by means of a very conserved C-terminal
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M111553200" target="_blank" rel="noreferrer noopener">10.1074/jbc.M111553200</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Repetitive Sequences
2002
Alanine/metabolism
Amino Acid
Amino Acid Sequence
Animals
Arginine/metabolism
Base Sequence
Cell Compartmentation
Cercopithecus aethiops
DNA Primers
Fluorescent Antibody Technique
Indirect
Ligands
Mao Hanwen
Molecular Sequence Data
Phosphoprotein Phosphatases/*metabolism
Proline/metabolism
Protein Phosphatase 1
Recombinant Proteins/chemistry/metabolism
Rosenthal Kenneth S
Subcellular Fractions/metabolism
The Journal of biological chemistry
Threonine/metabolism
Vero Cells
Viral Proteins/chemistry/*metabolism
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
Pages
263–275
Issue
2
Volume
39
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Identification and functional characterization of two type VI collagen receptors, alpha 3 beta 1 integrin and NG2, during avian corneal stromal development.
Publisher
An entity responsible for making the resource available
Investigative ophthalmology & visual science
Date
A point or period of time associated with an event in the lifecycle of the resource
1998
1998-02
Subject
The topic of the resource
Animals; Chick Embryo; Fibroblasts/metabolism; Cell Movement/physiology; Immunoblotting; Integrins/*metabolism; Fluorescent Antibody Technique; Cell Culture Techniques; Extracellular Matrix/metabolism; Antigens/*metabolism; Cell Polarity/physiology; Cell Size/physiology; Collagen/*metabolism; Corneal Stroma/*embryology/*metabolism; Integrin alpha3beta1; Proteoglycans/*metabolism; Receptors; Indirect; Laminin/*metabolism
Creator
An entity primarily responsible for making the resource
Doane K J; Howell S J; Birk D E
Description
An account of the resource
PURPOSE: The development and maintenance of extracellular matrix architecture in the corneal stroma is associated with abundant type VI collagen deposition. This collagen has been implicated in mediating both cell-matrix and matrix-matrix interactions. Although corneal fibroblasts spread extensively on this collagen, its role in corneal development has not been elucidated. METHODS: To clarify the role of this collagen, two type VI collagen receptors were studied during corneal development using immunochemical techniques: alpha 3 beta 1 integrin and an integral membrane proteoglycan, NG2. RESULTS: At embryonic day 6, these receptors were present in a diffuse pattern on cells within the cornea and juxtacorneal regions, indicating a migratory phenotype. At embryonic day 14, when the stroma is fully differentiated, alpha 3 and NG2 were localized in a punctate pattern on a subset of corneal fibroblasts, whereas beta 1 was more ubiquitously expressed. Colocalization of NG2 and type VI collagen indicated that this collagen was present and punctate in its organization was associated with NG2-positive cells. Immunochemical analyses at embryonic days 5 and 14 revealed alpha 3 and beta 1 at 155 kDa and 120 kDa, respectively, and demonstrated that these subunits were interacting to form a heterodimer. NG2 was present with a core protein of 330 kDa and an intact proteoglycan of approximately 600 kDa, and analysis of stromal lysates indicated a chondroitin sulfate-containing proteoglycan. Matrix-receptor cross-linking demonstrated the interaction of beta 1 and NG2 in periocular mesenchyme cells and corneal fibroblasts with type VI collagen, whereas only a subset of cells expressed alpha 3, indicating the presence of another beta 1 integrin. No variations between in vivo and in vitro expression of either alpha 3 beta 1 or NG2 were observed. CONCLUSIONS: These data indicate that two receptors for type VI collagen, alpha 3 beta 1 and NG2, are present during corneal stromal development, with a functional interaction of these receptors with type VI collagen. These interactions may play a role in corneal cell migration, development, and maintenance of corneal architecture.
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
1998
Animals
Antigens/*metabolism
Birk D E
Cell Culture Techniques
Cell Movement/physiology
Cell Polarity/physiology
Cell Size/physiology
Chick Embryo
Collagen/*metabolism
Corneal Stroma/*embryology/*metabolism
Doane K J
Extracellular Matrix/metabolism
Fibroblasts/metabolism
Fluorescent Antibody Technique
Howell S J
Immunoblotting
Indirect
Integrin alpha3beta1
Integrins/*metabolism
Investigative ophthalmology & visual science
Laminin/*metabolism
Proteoglycans/*metabolism
Receptors