A serpin shapes the extracellular environment to prevent influenza A virus maturation - Wikidata - wikimedia - TriplyDB

A serpin shapes the extracellular environment to prevent influenza A virus maturation

A serpin shapes the extracellular environment to prevent influenza A virus maturation

http://www.wikidata.org/entity/Q35083702

about

Aberrant coagulation causes a hyper-inflammatory response in severe influenza pneumonia Tetherin Sensitivity of Influenza A Viruses Is Strain Specific: Role of Hemagglutinin and Neuraminidase.Integrating Transcriptomic and Proteomic Data Using Predictive Regulatory Network Models of Host Response to Pathogens.Infectious disease. Life-threatening influenza and impaired interferon amplification in human IRF7 deficiency Endogenous Murine BST-2/Tetherin Is Not a Major Restriction Factor of Influenza A Virus Infection.Respiratory protease/antiprotease balance determines susceptibility to viral infection and can be modified by nutritional antioxidants Identification of Interferon-Stimulated Genes with Antiretroviral Activity.Oviductal estrogen receptor α signaling prevents protease-mediated embryo death Host genetics of severe influenza: from mouse Mx1 to human IRF7 A Plant-Derived Nucleic Acid Reconciles Type I IFN and a Pyroptotic-like Event in Immunity against Respiratory Viruses.Influenza A Virus Virulence Depends on Two Amino Acids in the N-Terminal Domain of Its NS1 Protein To Facilitate Inhibition of the RNA-Dependent Protein Kinase PKR.Lateral Organization of Influenza Virus Proteins in the Budozone Region of the Plasma Membrane.The Impact of the Interferon/TNF-Related Apoptosis-Inducing Ligand Signaling Axis on Disease Progression in Respiratory Viral Infection and Beyond.Recurrent rhinovirus infections in a child with inherited MDA5 deficiency.The cellular endosomal protein stannin inhibits intracellular trafficking of human papillomavirus during virus entry.A robust cell culture system supporting the complete life cycle of hepatitis B virus.Cytokine Profiles of Severe Influenza Virus-Related Complications in Children.Host Cell Restriction Factors that Limit Influenza A Infection.Role of Antheraea pernyi serpin 12 in prophenoloxidase activation and immune responses.Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown.The study on serum and urine of renal interstitial fibrosis rats induced by unilateral ureteral obstruction based on metabonomics and network analysis methods.Interferon-Stimulated Gene (ISG)-Expression Screening Reveals the Specific Antibunyaviral Activity of ISG20.Recent advances in antiviral interferon-stimulated gene biology.Influenza A Virus Facilitates Its Infectivity by Activating p53 to Inhibit the Expression of Interferon-Induced Transmembrane Proteins.LY6E mediates an evolutionarily conserved enhancement of virus infection by targeting a late entry step TMPRSS11A activates the influenza A virus hemagglutinin and the MERS coronavirus spike protein and is insensitive against blockade by HAI-1 Canine Influenza Virus is Mildly Restricted by Canine Tetherin Protein

P2860

Q26753030-01DE0DC5-27D3-4338-9545-40471A87C95C Q30376050-F6445F84-98F9-4A9C-9358-874CF585EBF2 Q31114011-FDEFDAE8-B0AD-42C4-B806-417B172DAECA Q34468857-EDC820FF-3B66-479E-9C08-58D90DED963E Q35840924-754FEF0A-A034-440A-B182-AC44D572E32B Q36104532-3DE9DD06-A646-44C6-BB8F-6C8CAB58353A Q36134164-96E4B952-377A-4E31-ABB0-0E45DDE9D001 Q36479358-1EE53D79-E2ED-43AA-A5E2-B05222882B54 Q36522870-EDEFFF8E-53AD-4873-9B53-9204AA3394B1 Q38605090-3795FED9-2EBD-4EB9-91DF-8EFA6189E2B9 Q38714315-191DA668-3AB6-4204-925E-D2878DDDB0F2 Q38716278-3D67DFEE-E0C3-44B1-BB45-5013C92B6884 Q39223220-D5E8AB6C-62E5-4FDE-BC64-FE8D722B4688 Q40162658-7D3592CE-8591-44C9-B4ED-E0EE0A51F285 Q42517266-3F252EA0-83F8-40C4-8A73-80689C9AC8F8 Q45323970-71B79D43-D673-4208-A01D-AE10CF8AA2DC Q45324457-F510AFBC-CFF2-42C0-ABBB-0718DD21D2AF Q47097744-F7C7393A-AEA7-4FEA-9FC6-77691AE19413 Q47343713-A4CC4CAA-8A77-452D-9398-6CF0213E8DCD Q50209147-9BFD4A74-5FFD-486B-80EF-F3EA8D3D049C Q50880891-53A1AB84-5C77-4102-B0C8-6A57BA4BFC05 Q52563024-13BAF591-DE8F-4E6D-ACC7-8684DFC64C44 Q54250434-1767F13C-D714-4E75-86FE-D905170C8F13 Q55122030-D4F62A6C-CB22-48C1-AD84-C7311C57ACE8 Q56994354-E86F2CC6-25F0-4112-8D02-31039ECF61DC Q57252412-EFD509E4-D13C-40BE-A4E8-87451837FACC Q58559710-7586E079-A52E-43C7-AA37-1CC65594F5B7

P2860

A serpin shapes the extracellular environment to prevent influenza A virus maturation

http://www.wikidata.org/entity/Q35083702

description

2015 nî lūn-bûn

@nan

2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@ast

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@en

type

label

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@ast

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@en

prefLabel

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@ast

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@en

P1433

Q35083702-A045356E-A23A-46F6-AE2D-42E8535BE59D

P1476

Q35083702-438AB64B-5DA4-45D8-BD8F-7B64F0F82C82

P2093

Q35083702-184FC13D-68D1-4FA6-8411-E5066DA9CC65

Q35083702-5FE33C54-52D0-499F-8F61-F662968FB30D

Q35083702-6D774BE8-BC00-4CEE-84AC-E98C1D86719E

Q35083702-767F0B8E-968C-46C9-8A3B-6A4339EDEA53

Q35083702-8B3A8A28-5DDB-4ECB-9CEE-DA87B7D67986

Q35083702-C7A5A842-B092-4B5F-AA36-C40A8D73C2C1

Q35083702-DC7DF410-5B38-4123-BA50-ACAE6BD10861

Q35083702-EF0F5909-3FA5-4758-A9D3-689FA2D345FF

P2860

Q35083702-061538C5-A0A8-46FC-B730-51011BE8B477

Q35083702-0860A715-EBCF-405F-9899-8BE3EE4340E6

Q35083702-09584D63-1B12-460C-9903-DA601A3734AB

Q35083702-0B0F09F1-AA7C-4D8F-A7B4-8AB0E4B3F56E

Q35083702-0D0F048C-FA40-425A-AB99-B4132A4BD4DC

Q35083702-1FB0297C-FA02-4241-B6CB-66E40466CCD8

Q35083702-238FCAD3-F9A3-450B-B8DF-AB9F8615DEA2

Q35083702-3270490A-5417-4811-B3FF-2C03F92F91CC

Q35083702-3697BD96-65D6-4806-8F44-3FA27B688BFD

Q35083702-391B646E-B973-4908-AD1A-ED08F781C29F

P304

Q35083702-4CA07122-1722-4BA5-8F09-2F4B401A3054

P31

Q35083702-B07921A6-074B-4E44-AC1E-6DF1F247A7E0

P356

Q35083702-6215F55F-4004-4470-8962-40209310B950

P407

Q35083702-1D66B1AE-CEF4-48B4-9120-89449083B6A4

P433

Q35083702-DFEE31C2-58D3-45B2-A837-42DCF8F18FB4

P478

Q35083702-4732A242-51AB-4656-A874-05DA51DC59B4

P50

Q35083702-07001B9A-D6DE-4C85-9BF6-CC9D8FF5CC5E

Q35083702-10B30102-0C38-4B38-A1F3-EE16B3F8A141

Q35083702-130EBF46-7CC1-4811-BB98-FF0A3E9FCA23

Q35083702-4B14F790-5425-4D8F-8A6D-7D7A093B30A3

Q35083702-7102B6DD-4D6A-42F4-9E32-4D0602B97F49

Q35083702-AE29A3DA-28C4-4DDD-BEA4-8418E9CEB0E4

Q35083702-D96A3EA2-4F39-4DA2-8548-9D0EA2276970

P577

Q35083702-9594F41D-0534-4F6A-8D7C-6FACADE5D4C9

P5875

Q35083702-0BF5AB27-E87B-4533-8BFD-118FEB514C10

P698

Q35083702-735B647D-B3C3-4592-AF57-AF11B063EFF2

P932

Q35083702-7EC698E6-B1EA-42CE-A692-7D50241EAED5

P356

J.CELL.2015.01.040

P1433

P1476

A serpin shapes the extracellular environment to prevent influenza A virus maturation

@en

P2093

Brenna Flatley

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

Charles M Rice

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

Hans-Heinrich Hoffmann

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

Jing W Xiao

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

Kierstin L Bell

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

Paul D Bieniasz

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

Rachel H Gilmore

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

Yingpu Yu

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

P2860

Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene

A diverse range of gene products are effectors of the type I interferon antiviral response

Live attenuated influenza viruses containing NS1 truncations as vaccine candidates against H5N1 highly pathogenic avian influenza

Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium

Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu

Tmprss2 is essential for influenza H1N1 virus pathogenesis in mice.

Transforming growth factor-β: activation by neuraminidase and role in highly pathogenic H5N1 influenza pathogenesis.

Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2.

Aprotinin, a protease inhibitor, suppresses proteolytic activation of pandemic H1N1v influenza virus.

Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation

P304

631-643

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

P31

scholarly article

P356

10.1016/J.CELL.2015.01.040

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

P407

P433

4

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

P478

160

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

P50

Jean-Laurent Casanova

Michael J Ciancanelli

Meike Dittmann Chevillotte

Stefania Crotta

Margaret A Scull

P577

2015-02-01T00:00:00Z

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

P5875

272168168

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

P698

25679759

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

P932

4328142

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