Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment. - Wikidata - wikimedia - TriplyDB

Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment.

Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment.

http://www.wikidata.org/entity/Q39237210

about

Tegument Assembly and Secondary Envelopment of Alphaherpesviruses Role of human cytomegalovirus tegument proteins in virion assembly A herpes simplex virus-derived replicative vector expressing LIF limits experimental demyelinating disease and modulates autoimmunity Crystal Structure of the Herpesvirus Inner Tegument Protein UL37 Supports Its Essential Role in Control of Viral Trafficking Conserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids.The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis.Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry.A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection.Herpes simplex virus 1 protein UL37 interacts with viral glycoprotein gK and membrane protein UL20 and functions in cytoplasmic virion envelopment.Blocking ESCRT-mediated envelopment inhibits microtubule-dependent trafficking of alphaherpesviruses in vitro.Structural analysis of herpes simplex virus by optical super-resolution imaging.Herpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36p Varicella zoster virus glycoprotein C increases chemokine-mediated leukocyte migration.Novel Structure and Unexpected RNA-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein UL21.Insights into the function of tegument proteins from the varicella zoster virus.ORF7 of Varicella-Zoster Virus Is Required for Viral Cytoplasmic Envelopment in Differentiated Neuronal Cells.Cellular Protein WDR11 Interacts with Specific Herpes Simplex Virus Proteins at the trans-Golgi Network To Promote Virus Replication.Insights into herpesvirus tegument organization from structural analyses of the 970 central residues of HSV-1 UL36 protein.The Interaction between Herpes Simplex Virus 1 Tegument Proteins UL51 and UL14 and Its Role in Virion Morphogenesis.Herpes simplex virus 1 interferes with autophagy of murine dendritic cells and impairs their ability to stimulate CD8+ T lymphocytes.Crystal structure of the N-terminal half of the traffic controller UL37 from Herpes Simplex virus Type 1.Vaccinia virus proteins A36 and F12/E2 show strong preferences for different kinesin light chain isoforms.Human Antiviral Protein IFIX Suppresses Viral Gene Expression during Herpes Simplex Virus 1 (HSV-1) Infection and Is Counteracted by Virus-induced Proteasomal Degradation.Herpes Simplex Virus Capsid Localization to ESCRT-VPS4 Complexes in the Presence and Absence of the Large Tegument Protein UL36p.Targeting of viral capsids to nuclear pores in a cell-free reconstitution system.Human Cytomegalovirus pUL47 Modulates Tegumentation and Capsid Accumulation at the Viral Assembly Complex.A Therapeutic Antiviral Antibody Inhibits the Anterograde Directed Neuron-to-Cell Spread of Herpes Simplex Virus and Protects against Ocular Disease.Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.Inner tegument proteins of Herpes Simplex Virus are sufficient for intracellular capsid motility in neurons but not for axonal targeting.The pUL37 tegument protein guides alpha-herpesvirus retrograde axonal transport to promote neuroinvasion.Cytoskeletons in the Closet-Subversion in Alphaherpesvirus Infections.Infection and Transport of Herpes Simplex Virus Type 1 in Neurons: Role of the Cytoskeleton.The interaction of HSV-1 tegument proteins pUL36 and pUL37: a novel target for antivirals that inhibit viral assembly

P2860

Q26782247-4772533C-424B-4AA4-9E7A-3C2C07079FE3 Q27015069-BCCD3977-7087-4BAB-BAF5-6BC44A6F6984 Q27319470-729A5C9E-0901-425B-9470-AAF4C7F21EEB Q27682027-54392F21-B873-4352-BFC0-00530F91FCA9 Q30355292-B867B435-5946-45DC-B0AA-0555B685ED2E Q30384593-65CBEA51-534F-4151-9E57-DCBB05A79CBE Q30405542-E2D1D827-2B3E-4EC7-9FF6-B6650D680E0D Q30554266-029FF72A-1A93-4350-8D88-952B2ACE4735 Q30557071-915B88BF-B53B-442E-A46B-463E16AEF7FF Q33887656-BB9FA4AA-43DA-45E4-86D8-4292FD6FB31D Q34594977-CDFE9529-D448-465B-BDE0-C1E32CEB3708 Q35114299-389D7F40-A3F0-404F-9CC8-BEF825A6A27C Q36281823-1E14461E-9DC8-408F-B8D3-448480FADD69 Q36380849-8FB07CA4-B9EB-40CD-A11F-E446945FF4EB Q36950924-6F990B33-F741-404C-BAD8-A1538837C74D Q38553727-E11A5985-BDF3-48E7-ADA7-EDBDB56B82EC Q38709702-54D13EBA-028C-4562-9502-8DCD912CC667 Q38852516-46FCDCA8-4B38-4325-A6AB-DE84CA070E70 Q38910076-735244A6-128C-4AEC-A4D3-5385C9F3F8FF Q39578027-9E3EC367-CA91-4073-88C8-C098274C0789 Q40096323-69BE7F4D-3BC5-4FBA-9614-6A327A64587F Q40097539-31FF4ED0-6FA7-4B27-9F66-BCB1D6116ED2 Q40209222-A3BE0BF0-A0A0-4668-9E2E-DBBCB7512CA2 Q40376097-E2647953-0DFA-4102-8AF8-A022CC5E0140 Q40649067-DE90617E-292D-4CD9-A789-4EF77A38627D Q41104953-CF4BA728-6DDD-41C9-AE14-E5375F91F3B0 Q41253250-9EA2B73E-DE19-4203-BC13-057C4116A00E Q45324468-89F883FF-B559-4835-98E7-66EA5FDBAB98 Q47205447-E5D4DCC8-1CD7-4E0C-AC0D-888B8F23FC60 Q47239097-2A1AC8DD-AD9F-4134-A964-6051963D8653 Q47319444-78F9E303-A747-42FC-8F16-0FA9111151E1 Q50042112-3ECEBD10-E1F0-4B2A-97F5-27AAB447EE29 Q55260609-A31D8EEE-499B-4093-A456-7D7BBEE4064B Q57076505-C29375C9-35B7-4E70-9A42-B0155205B2FB

P2860

Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment.

http://www.wikidata.org/entity/Q39237210

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@en

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@nl

type

label

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@en

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@nl

prefLabel

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@en

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@nl

P1433

Q39237210-C1C8F388-F6A1-4FF4-8E5F-AEA64F784C5D

P1476

Q39237210-EBCD4808-9D8A-49E0-B529-8CAF0BD1F5DB

P2093

Q39237210-02A7ADB5-CCE5-469F-A039-238E735D83A7

Q39237210-12F0761E-1F7E-4F22-9438-9EF2D69F594E

Q39237210-194439F4-7623-4A47-9EC3-0B1F6AC48F28

Q39237210-32F36F8F-44F7-4A2A-90AC-53015B732A80

Q39237210-7F5C14D0-009B-4797-94B1-7AC996778939

Q39237210-85C32DFA-94C2-499D-998B-93AB28389767

Q39237210-96749754-C044-48DB-9259-817EA612EBF4

P2860

Q39237210-0088AD8D-6590-432A-9BEA-C9119AC0E7A6

Q39237210-0513475E-30E0-4039-B6C3-8261EC9E6D51

Q39237210-06358CDA-DC4B-4E6A-B974-59FE04D36C64

Q39237210-0D02CD76-3A1A-4599-A429-0528832417F1

Q39237210-1321EF9C-73C0-4E27-BCD5-DDBFF88078B8

Q39237210-1336A50D-08C0-40BD-BA6B-60C0CE226F68

Q39237210-16C88E27-064D-4732-8A50-3E8FD08360B3

Q39237210-18E50262-8232-4F11-88F4-54F1F27390E5

Q39237210-1DB8A084-6FBD-4069-9488-73FB6D7BF9C1

Q39237210-1FBC66E7-5868-4F03-86C2-4BD2172D4E96

P304

Q39237210-30F3DD5F-DF88-4BC2-9B28-9CABFCF99BCF

P31

Q39237210-06F42611-C0AE-4199-8956-0C9CC6F25938

P356

Q39237210-CC5899DA-91BC-4E72-9A7A-1F2A67C00CAE

P433

Q39237210-22FFF3DC-5B6F-4A2F-BB10-32CE3E3E9286

P478

Q39237210-1375A5A6-20EC-4047-9C74-4308528DCAC4

P577

Q39237210-6FB2AAF9-BA11-4202-B2B5-1BCB8724EFD0

P698

Q39237210-FF5FDA3C-7157-40A1-A78D-72BDAACF8588

P356

P1433

Cellular Microbiology

P1476

Cytosolic herpes simplex virus ...... rior to secondary envelopment.

@en

P2093

Anja Pohlmann

http://www.w3.org/2001/XMLSchema#string

Anne Binz

http://www.w3.org/2001/XMLSchema#string

Beate Sodeik

http://www.w3.org/2001/XMLSchema#string

Julia Schipke

http://www.w3.org/2001/XMLSchema#string

Katinka Döhner

http://www.w3.org/2001/XMLSchema#string

Malte Sandbaumhüter

http://www.w3.org/2001/XMLSchema#string

Rudolf Bauerfeind

http://www.w3.org/2001/XMLSchema#string

P2860

Evolutionarily conserved herpesviral protein interaction networks

Herpes Simplex: Insights on Pathogenesis and Possible Vaccines

Determination of interactions between tegument proteins of herpes simplex virus type 1

Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus

Coupling viruses to dynein and kinesin-1

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein

The neurotropic herpes viruses: herpes simplex and varicella-zoster

Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.

Assembly of vaccinia virus: role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks

Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells

P304

248-269

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1111/CMI.12075

http://www.w3.org/2001/XMLSchema#string

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

15

http://www.w3.org/2001/XMLSchema#string

P577

2012-12-20T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23186167

http://www.w3.org/2001/XMLSchema#string