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WNV:POLG

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Species (Taxon ID) West Nile virus (WNV). (11082)
Gene Name(s) No Information Provided.
Protein Name(s) Genome polyprotein

Peptide 2k Capsid protein C Core protein prM Peptide pr Small envelope protein M Matrix protein Envelope protein E Non-structural protein 1 NS1 Non-structural protein 2A NS2A Serine protease subunit NS2B Flavivirin protease NS2B regulatory subunit Non-structural protein 2B Serine protease NS3 Flavivirin protease NS3 catalytic subunit Non-structural protein 3 Non-structural protein 4A NS4A Non-structural protein 4B NS4B RNA-directed RNA polymerase NS5 NS5

External Links
UniProt P06935
EMBL M12294
PIR A25256
RefSeq NP_041724.2
PDB 2FP7
2G05
2G2G
2GGV
2IJO
2P5P
2YOL
3E90
3I50
PDBsum 2FP7
2G05
2G2G
2GGV
2IJO
2P5P
2YOL
3E90
3I50
DisProt DP00673
ProteinModelPortal P06935
SMR P06935
IntAct P06935
BindingDB P06935
ChEMBL CHEMBL5419
GeneID 912267
EvolutionaryTrace P06935
PRO PR:P06935
Proteomes UP000008600
GO GO:0044167
GO:0042025
GO:0016021
GO:0019028
GO:0019031
GO:0055036
GO:0005524
GO:0008026
GO:0003725
GO:0046872
GO:0004482
GO:0004483
GO:0008233
GO:0003724
GO:0003968
GO:0004252
GO:0070008
GO:0005198
GO:0075512
GO:0039654
GO:0039520
GO:0045070
GO:0006355
GO:0019050
GO:0039576
GO:0039574
GO:0039502
GO:0006351
GO:0039694
GO:0019062
Gene3D 2.60.40.350
2.60.98.10
3.30.387.10
3.40.50.150
3.40.50.300
InterPro IPR011492
IPR000069
IPR013755
IPR001122
IPR026470
IPR001157
IPR000752
IPR000487
IPR000404
IPR001528
IPR002535
IPR000336
IPR001850
IPR027287
IPR014412
IPR011998
IPR013754
IPR014001
IPR001650
IPR014756
IPR026490
IPR027417
IPR000208
IPR007094
IPR002877
IPR029063
IPR009003
Pfam PF01003
PF07652
PF02832
PF00869
PF01004
PF00948
PF01005
PF01002
PF01350
PF01349
PF00972
PF01570
PF01728
PF00271
PF00949
PIRSF PIRSF003817
SMART SM00487
SM00490
SUPFAM SSF50494
SSF52540
SSF53335
SSF56983
SSF81296
TIGRFAMs TIGR04240
PROSITE PS51527
PS51528
PS51192
PS51194
PS50507
PS51591

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0019050

suppression by virus of host apoptotic process

PMID:23115297[1]

ECO:0000314

P

As is the case with many RNA viruses, infection of mammalian cells with West Nile Virus has been reported to cause apoptosis. Replication of WNV and other flaviviruses is relatively slow, and therefore, it is not seemingly beneficial to the virus if the first viral protein produced in an infected cell induces programmed cell death. In contrast, during the early stages of flavivirus infection, apoptosis appears to be inhibited by a process that involves activation of the prosurvival kinase Akt. Recent studies revealed that antiapoptotic/survival signaling is activated shortly after flavivirus infection. This signaling process involves the kinase Akt, which is activated by PI3K-dependent phosphorylation on serine 473. As seen in figure 7, inhibition of PI3 kinase abrogates protection by WNV capsid protein. This was done when A549 cells were transduced with lentiviruses encoding WNV capsid protein or AcGFP alone, before challenge with anti-Fas with or without addition of LY294002.

complete
CACAO 6552

GO:0045070

positive regulation of viral genome replication

PMID:22553322[2]

ECO:0000315

P

Figure 3 and figure 4 for NS4B, but the expt was done in the presence of NS4 F86C mutation, but UniProt doesn't offer separate mature protein record for each component of the polyprotein from WNV.

complete
CACAO 6685

GO:0008233

peptidase activity

PMID:23291011[3]

ECO:0000314

F

As seen in Figure 1, WNV protease retained activity in most of the detergents tested in this study. WNV protease possesses catalytic activity in the presence of some detergents, making it useful for the removal of an affinity tag in a membrane protein preparation. It is suggested that WNV protease can be used for the preparation of a membrane protein or a transmembrane domain segment from a multi-span transmembrane protein.

complete
CACAO 6883

enables

GO:0033592

RNA strand annealing activity

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043489

RNA stabilization

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0106005

RNA 5'-cap (guanine-N7)-methylation

PMID:17267492[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004483

mRNA (nucleoside-2'-O-)-methyltransferase activity

PMID:17267492[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045070

positive regulation of viral genome replication

PMID:22553322[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019050

suppression by virus of host apoptotic process

PMID:23115297[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

PMID:23291011[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:1990814

DNA/DNA annealing activity

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:1990904

ribonucleoprotein complex

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:18033802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0080009

mRNA methylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004483

P

Seeded From UniProt

complete

involved_in

GO:0080009

mRNA methylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004483

P

Seeded From UniProt

complete

involved_in

GO:0080009

mRNA methylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004483

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001850

F

Seeded From UniProt

complete

enables

GO:0003724

RNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001850

F

Seeded From UniProt

complete

enables

GO:0003725

double-stranded RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000752

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000208
InterPro:IPR007094
InterPro:IPR014412

F

Seeded From UniProt

complete

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000487
InterPro:IPR014412

F

Seeded From UniProt

complete

enables

GO:0004482

mRNA (guanine-N7-)-methyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014412
InterPro:IPR026490

F

Seeded From UniProt

complete

enables

GO:0004483

mRNA (nucleoside-2'-O-)-methyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014412
InterPro:IPR026490

F

Seeded From UniProt

complete

enables

GO:0005198

structural molecule activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001122

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000208
InterPro:IPR001850
InterPro:IPR011492

F

Seeded From UniProt

complete

enables

GO:0008026

ATP-dependent helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011492

F

Seeded From UniProt

complete

enables

GO:0008168

methyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002877

F

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000404

P

Seeded From UniProt

complete

involved_in

GO:0016070

RNA metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000404

P

Seeded From UniProt

complete

enables

GO:0016817

hydrolase activity, acting on acid anhydrides

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014412

F

Seeded From UniProt

complete

enables

GO:0017111

nucleoside-triphosphatase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014412

F

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000404
InterPro:IPR000487

C

Seeded From UniProt

complete

part_of

GO:0019028

viral capsid

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001122

C

Seeded From UniProt

complete

part_of

GO:0019031

viral envelope

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000069

C

Seeded From UniProt

complete

involved_in

GO:0019058

viral life cycle

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000069

P

Seeded From UniProt

complete

involved_in

GO:0032259

methylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002877

P

Seeded From UniProt

complete

involved_in

GO:0039694

viral RNA genome replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007094

P

Seeded From UniProt

complete

enables

GO:0046983

protein dimerization activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011998

F

Seeded From UniProt

complete

enables

GO:0004483

mRNA (nucleoside-2'-O-)-methyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.1.1.57

F

Seeded From UniProt

complete

enables

GO:0017111

nucleoside-triphosphatase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.6.1.15

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.48

F

Seeded From UniProt

complete

enables

GO:0004482

mRNA (guanine-N7-)-methyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.1.1.56

F

Seeded From UniProt

complete

involved_in

GO:0075512

clathrin-dependent endocytosis of virus by host cell

PMID:15367621[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0039714

cytoplasmic viral factory

PMID:24465392[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0019031

viral envelope

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0261

C

Seeded From UniProt

complete

part_of

GO:0044165

host cell endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1038

C

Seeded From UniProt

complete

involved_in

GO:0032259

methylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0489

P

Seeded From UniProt

complete

involved_in

GO:0039576

suppression by virus of host JAK1 activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1096

P

Seeded From UniProt

complete

involved_in

GO:0039663

membrane fusion involved in viral entry into host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1168

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

part_of

GO:0030430

host cell cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1035
UniProtKB-SubCell:SL-0381

C

Seeded From UniProt

complete

involved_in

GO:0039564

suppression by virus of host STAT2 activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1106

P

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0696

F

Seeded From UniProt

complete

involved_in

GO:0006370

7-methylguanosine mRNA capping

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0506

P

Seeded From UniProt

complete

part_of

GO:0033644

host cell membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1043

C

Seeded From UniProt

complete

involved_in

GO:0030683

evasion or tolerance by virus of host immune response

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0899

P

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

involved_in

GO:0006397

mRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0507

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0039654

fusion of virus membrane with host endosome membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1170

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

involved_in

GO:0039563

suppression by virus of host STAT1 activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1105

P

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1048
UniProtKB-SubCell:SL-0414

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0039503

suppression by virus of host innate immune response

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1090

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0046718

viral entry into host cell

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1162
UniProtKB-KW:KW-1160

P

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0548

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0946
UniProtKB-SubCell:SL-0274

C

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

involved_in

GO:0075509

endocytosis involved in viral entry into host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1164

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0075512

clathrin-dependent endocytosis of virus by host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1165

P

Seeded From UniProt

complete

enables

GO:0008168

methyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0489

F

Seeded From UniProt

complete

involved_in

GO:0019062

virion attachment to host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1161

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

part_of

GO:0019028

viral capsid

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0167

C

Seeded From UniProt

complete

involved_in

GO:0039502

suppression by virus of host type I interferon-mediated signaling pathway

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1114

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0039520

induction by virus of host autophagy

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1072

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0039574

suppression by virus of host TYK2 activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1112

P

Seeded From UniProt

complete

part_of

GO:0044220

host cell perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0382

C

Seeded From UniProt

complete

part_of

GO:0044167

host cell endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0390

C

Seeded From UniProt

complete

part_of

GO:0055036

virion membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0275

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Urbanowski, MD & Hobman, TC (2013) The West Nile virus capsid protein blocks apoptosis through a phosphatidylinositol 3-kinase-dependent mechanism. J. Virol. 87 872-81 PubMed GONUTS page
  2. 2.0 2.1 Youn, S et al. (2012) Evidence for a genetic and physical interaction between nonstructural proteins NS1 and NS4B that modulates replication of West Nile virus. J. Virol. 86 7360-71 PubMed GONUTS page
  3. 3.0 3.1 Huang, Q et al. (2013) West Nile virus protease activity in detergent solutions and application for affinity tag removal. Anal. Biochem. 435 44-6 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 4.5 4.6 Ivanyi-Nagy, R et al. (2008) RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. Nucleic Acids Res. 36 712-25 PubMed GONUTS page
  5. 5.0 5.1 Zhou, Y et al. (2007) Structure and function of flavivirus NS5 methyltransferase. J. Virol. 81 3891-903 PubMed GONUTS page
  6. Chu, JJ & Ng, ML (2004) Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway. J. Virol. 78 10543-55 PubMed GONUTS page
  7. Kaufusi, PH et al. (2014) Induction of endoplasmic reticulum-derived replication-competent membrane structures by West Nile virus non-structural protein 4B. PLoS ONE 9 e84040 PubMed GONUTS page