-
1
-
-
84964452166
-
Zika virus
-
Petersen, L. R., Jamieson, D. J., Powers, A. M. & Honein, M. A. Zika virus. N. Engl. J. Med. 374, 1552-1563 (2016).
-
(2016)
N. Engl. J. Med.
, vol.374
, pp. 1552-1563
-
-
Petersen, L.R.1
Jamieson, D.J.2
Powers, A.M.3
Honein, M.A.4
-
2
-
-
84962870368
-
Zika virus as a cause of neurologic disorders
-
Broutet, N. et al. Zika virus as a cause of neurologic disorders. N. Engl. J. Med. 374, 1506-1509 (2016).
-
(2016)
N. Engl. J. Med.
, vol.374
, pp. 1506-1509
-
-
Broutet, N.1
-
3
-
-
84964933278
-
Zika virus associated with meningoencephalitis
-
Carteaux, G. et al. Zika virus associated with meningoencephalitis. N. Engl. J. Med. 374, 1595-1596 (2016).
-
(2016)
N. Engl. J. Med.
, vol.374
, pp. 1595-1596
-
-
Carteaux, G.1
-
4
-
-
84959496550
-
Acute myelitis due to Zika virus infection
-
Mecharles, S. et al. Acute myelitis due to Zika virus infection. Lancet 387, 1481 (2016).
-
(2016)
Lancet
, vol.387
, pp. 1481
-
-
Mecharles, S.1
-
6
-
-
84885695869
-
-
6th edn Ch. Lippincott-Raven Publishers
-
Lindenbach, B. D., C. L., M., C. L., M., Thiel, H. J. & Rice, C. M. in Fields Virology 6th edn. Ch. 25, 712-746 (Lippincott-Raven Publishers, 2013).
-
(2013)
Fields Virology
, vol.25
, pp. 712-746
-
-
Lindenbach, B.D.C.1
Thiel, H.J.2
Rice, C.M.3
-
7
-
-
84928471861
-
The flavivirus NS2B-NS3 proteasehelicase as a target for antiviral drug development
-
Luo, D., Vasudevan, S. G. & Lescar, J. The flavivirus NS2B-NS3 proteasehelicase as a target for antiviral drug development. Antiviral. Res. 118, 148-158 (2015).
-
(2015)
Antiviral. Res.
, vol.118
, pp. 148-158
-
-
Luo, D.1
Vasudevan, S.G.2
Lescar, J.3
-
8
-
-
53349178089
-
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
-
Ishikawa, H. & Barber, G. N. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 455, 674-678 (2008).
-
(2008)
Nature
, vol.455
, pp. 674-678
-
-
Ishikawa, H.1
Barber, G.N.2
-
9
-
-
53349168904
-
The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
-
Zhong, B. et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29, 538-550 (2008).
-
(2008)
Immunity
, vol.29
, pp. 538-550
-
-
Zhong, B.1
-
10
-
-
30844434186
-
Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway
-
Ramanathan, M. P. et al. Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway. Virology 345, 56-72 (2006).
-
(2006)
Virology
, vol.345
, pp. 56-72
-
-
Ramanathan, M.P.1
-
11
-
-
32344434707
-
Japanese encephalitis virus NS2B-NS3 protease binding to phage-displayed human brain proteins with the domain of trypsin inhibitor and basic region leucine zipper
-
Lin, C. W., Lin, K. H., Lyu, P. C. & Chen, W. J. Japanese encephalitis virus NS2B-NS3 protease binding to phage-displayed human brain proteins with the domain of trypsin inhibitor and basic region leucine zipper. Virus Res. 116, 106-113 (2006).
-
(2006)
Virus Res.
, vol.116
, pp. 106-113
-
-
Lin, C.W.1
Lin, K.H.2
Lyu, P.C.3
Chen, W.J.4
-
12
-
-
27644481761
-
NS1 protein secretion during the acute phase of West Nile virus infection
-
Macdonald, J. et al. NS1 protein secretion during the acute phase of West Nile virus infection. J. Virol. 79, 13924-13933 (2005).
-
(2005)
J. Virol.
, vol.79
, pp. 13924-13933
-
-
Macdonald, J.1
-
13
-
-
0025309446
-
Production of yellow fever virus proteins in infected cells: Identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera
-
Chambers, T. J., McCourt, D. W. & Rice, C. M. Production of yellow fever virus proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera. Virology 177, 159-174 (1990).
-
(1990)
Virology
, vol.177
, pp. 159-174
-
-
Chambers, T.J.1
McCourt, D.W.2
Rice, C.M.3
-
14
-
-
84855921187
-
Ligand-bound structures of the dengue virus protease reveal the active conformation
-
Noble, C. G., Seh, C. C., Chao, A. T. & Shi, P. Y. Ligand-bound structures of the dengue virus protease reveal the active conformation. J. Virol. 86, 438-446 (2012).
-
(2012)
J. Virol.
, vol.86
, pp. 438-446
-
-
Noble, C.G.1
Seh, C.C.2
Chao, A.T.3
Shi, P.Y.4
-
15
-
-
84873816287
-
Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease
-
Hammamy, M. Z., Haase, C., Hammami, M., Hilgenfeld, R. & Steinmetzer, T. Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease. ChemMedChem. 8, 231-241 (2013).
-
(2013)
ChemMedChem.
, vol.8
, pp. 231-241
-
-
Hammamy, M.Z.1
Haase, C.2
Hammami, M.3
Hilgenfeld, R.4
Steinmetzer, T.5
-
16
-
-
58649113845
-
Structure of West Nile virus NS3 protease: Ligand stabilization of the catalytic conformation
-
Robin, G. et al. Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation. J. Mol. Biol. 385, 1568-1577 (2009).
-
(2009)
J. Mol. Biol.
, vol.385
, pp. 1568-1577
-
-
Robin, G.1
-
17
-
-
33745025763
-
Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus
-
Erbel, P. et al. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat. Struct. Mol. Biol. 13, 372-373 (2006).
-
(2006)
Nat. Struct. Mol. Biol.
, vol.13
, pp. 372-373
-
-
Erbel, P.1
-
18
-
-
34247625945
-
Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
-
Aleshin, A. E., Shiryaev, S. A., Strongin, A. Y. & Liddington, R. C. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Prot. Sci. : Publ. Prot. Soc. 16, 795-806 (2007).
-
(2007)
Prot. Sci. : Publ. Prot. Soc.
, vol.16
, pp. 795-806
-
-
Aleshin, A.E.1
Shiryaev, S.A.2
Strongin, A.Y.3
Liddington, R.C.4
-
19
-
-
84952944013
-
Recombinant Dengue virus protein NS2B alters membrane permeability in different membrane models
-
Leon-Juarez, M. et al. Recombinant Dengue virus protein NS2B alters membrane permeability in different membrane models. Virol. J. 13, 1 (2016).
-
(2016)
Virol. J.
, vol.13
, pp. 1
-
-
Leon-Juarez, M.1
-
20
-
-
23344446921
-
Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries
-
Li, J. et al. Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J. Biol. Chem. 280, 28766-28774 (2005).
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 28766-28774
-
-
Li, J.1
-
21
-
-
0033571623
-
Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
-
Yao, N., Reichert, P., Taremi, S. S., Prosise, W. W. & Weber, P. C. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 7, 1353-1363 (1999).
-
(1999)
Structure
, vol.7
, pp. 1353-1363
-
-
Yao, N.1
Reichert, P.2
Taremi, S.S.3
Prosise, W.W.4
Weber, P.C.5
-
22
-
-
0025201350
-
Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
-
Chambers, T. J. et al. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Natl Acad. Sci. USA 87, 8898-8902 (1990).
-
(1990)
Proc. Natl Acad. Sci. USA
, vol.87
, pp. 8898-8902
-
-
Chambers, T.J.1
-
23
-
-
0025033393
-
In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3
-
Preugschat, F., Yao, C. W. & Strauss, J. H. In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3. J. Virol. 64, 4364-4374 (1990).
-
(1990)
J. Virol.
, vol.64
, pp. 4364-4374
-
-
Preugschat, F.1
Yao, C.W.2
Strauss, J.H.3
-
24
-
-
0001469617
-
-
6th edn Ch. Lippincott-Raven Publishers
-
Goff, S. P. in Fields Virology. 6th edn Ch. 47, 1424-1473 (Lippincott-Raven Publishers, 2013).
-
(2013)
Fields Virology
, vol.47
, pp. 1424-1473
-
-
Goff, S.P.1
-
25
-
-
33747452685
-
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
-
Lorenz, I. C., Marcotrigiano, J., Dentzer, T. G. & Rice, C. M. Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature 442, 831-835 (2006).
-
(2006)
Nature
, vol.442
, pp. 831-835
-
-
Lorenz, I.C.1
Marcotrigiano, J.2
Dentzer, T.G.3
Rice, C.M.4
-
26
-
-
0026419333
-
Structure of Sindbis virus core protein reveals a chymotrypsinlike serine proteinase and the organization of the virion
-
Choi, H. K. et al. Structure of Sindbis virus core protein reveals a chymotrypsinlike serine proteinase and the organization of the virion. Nature 354, 37-43 (1991).
-
(1991)
Nature
, vol.354
, pp. 37-43
-
-
Choi, H.K.1
-
27
-
-
0026039916
-
Processing of the yellow fever virus nonstructural polyprotein: A catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites
-
Chambers, T. J., Grakoui, A. & Rice, C. M. Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites. J. Virol. 65, 6042-6050 (1991).
-
(1991)
J. Virol.
, vol.65
, pp. 6042-6050
-
-
Chambers, T.J.1
Grakoui, A.2
Rice, C.M.3
-
28
-
-
84978832859
-
Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor
-
Lei, J. et al. Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor. Science 353, 503-505 (2016).
-
(2016)
Science
, vol.353
, pp. 503-505
-
-
Lei, J.1
-
29
-
-
0037779018
-
A graphical user interface to the CCP4 program suite
-
Potterton, E., Briggs, P., Turkenburg, M. & Dodson, E. A graphical user interface to the CCP4 program suite. Acta Crystallogr. D Biol. Crystallogr. 59, 1131-1137 (2003).
-
(2003)
Acta Crystallogr. D Biol. Crystallogr.
, vol.59
, pp. 1131-1137
-
-
Potterton, E.1
Briggs, P.2
Turkenburg, M.3
Dodson, E.4
-
30
-
-
79953737180
-
Overview of the CCP4 suite and current developments
-
Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
-
(2011)
Acta Crystallogr. D Biol. Crystallogr.
, vol.67
, pp. 235-242
-
-
Winn, M.D.1
-
31
-
-
84877111125
-
NMR analysis of a novel enzymatically active unlinked dengue NS2B-NS3 protease complex
-
Kim, Y. M. et al. NMR analysis of a novel enzymatically active unlinked dengue NS2B-NS3 protease complex. J. Biol. Chem. 288, 12891-12900 (2013).
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 12891-12900
-
-
Kim, Y.M.1
-
32
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6, 277-293 (1995).
-
(1995)
J. Biomol. NMR.
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
-
33
-
-
4644259437
-
Using NMRView to visualize and analyze the NMR spectra of macromolecules
-
Johnson, B. A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352 (2004).
-
(2004)
Methods Mol. Biol.
, vol.278
, pp. 313-352
-
-
Johnson, B.A.1
-
34
-
-
0032564349
-
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy
-
Pervushin, K. et al. NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy. Proc. Natl Acad. Sci. USA 95, 14147-14151 (1998).
-
(1998)
Proc. Natl Acad. Sci. USA
, vol.95
, pp. 14147-14151
-
-
Pervushin, K.1
-
35
-
-
0032506009
-
TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
-
Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wuthrich, K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl Acad. Sci. USA 95, 13585-13590 (1998).
-
(1998)
Proc. Natl Acad. Sci. USA
, vol.95
, pp. 13585-13590
-
-
Salzmann, M.1
Pervushin, K.2
Wider, G.3
Senn, H.4
Wuthrich, K.5
-
36
-
-
68349093958
-
TALOS: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
-
Shen, Y., Delaglio, F., Cornilescu, G. & Bax, A. TALOS: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223 (2009).
-
(2009)
J. Biomol. NMR
, vol.44
, pp. 213-223
-
-
Shen, Y.1
Delaglio, F.2
Cornilescu, G.3
Bax, A.4
-
37
-
-
0026597879
-
The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
-
Wishart, D. S., Sykes, B. D. & Richards, F. M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651 (1992).
-
(1992)
Biochemistry
, vol.31
, pp. 1647-1651
-
-
Wishart, D.S.1
Sykes, B.D.2
Richards, F.M.3
-
38
-
-
0024449503
-
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
-
Kay, L. E., Torchia, D. A. & Bax, A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979 (1989).
-
(1989)
Biochemistry
, vol.28
, pp. 8972-8979
-
-
Kay, L.E.1
Torchia, D.A.2
Bax, A.3
-
39
-
-
79960103751
-
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant
-
Gayen, S. et al. An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant. Proteins 79, 2557-2565 (2011).
-
(2011)
Proteins
, vol.79
, pp. 2557-2565
-
-
Gayen, S.1
-
40
-
-
0035824539
-
Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
-
Leung, D. et al. Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors. J. Biol. Chem. 276, 45762-45771 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 45762-45771
-
-
Leung, D.1
-
41
-
-
79953759821
-
IMOSFLM: A new graphical interface for diffraction-image processing with MOSFLM
-
Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R. & Leslie, A. G. iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 67, 271-281 (2011).
-
(2011)
Acta Crystallogr. D Biol. Crystallogr.
, vol.67
, pp. 271-281
-
-
Battye, T.G.1
Kontogiannis, L.2
Johnson, O.3
Powell, H.R.4
Leslie, A.G.5
-
43
-
-
79953747244
-
An introduction to data reduction: Space-group determination, scaling and intensity statistics
-
Evans, P. R. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D Biol. Crystallogr. 67, 282-292 (2011).
-
(2011)
Acta Crystallogr. D Biol. Crystallogr.
, vol.67
, pp. 282-292
-
-
Evans, P.R.1
-
44
-
-
0000560808
-
MOLREP: An automated program for molecular replacement
-
Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
-
(1997)
J. Appl. Crystallogr.
, vol.30
, pp. 1022-1025
-
-
Vagin, A.1
Teplyakov, A.2
-
45
-
-
84860273177
-
Towards automated crystallographic structure refinement with phenix refine
-
Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352-367 (2012).
-
(2012)
Acta Crystallogr. D Biol. Crystallogr.
, vol.68
, pp. 352-367
-
-
Afonine, P.V.1
-
46
-
-
76449098262
-
PHENIX: A comprehensive Python-based system for macromolecular structure solution
-
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
-
(2010)
Acta Crystallogr. D Biol. Crystallogr.
, vol.66
, pp. 213-221
-
-
Adams, P.D.1
-
47
-
-
84860279341
-
Use of knowledge-based restraints in phenix. Refine to improve macromolecular refinement at low resolution
-
Headd, J. J. et al. Use of knowledge-based restraints in phenix. refine to improve macromolecular refinement at low resolution. Acta Crystallogr. D Biol. Crystallogr. 68, 381-390 (2012).
-
(2012)
Acta Crystallogr. D Biol. Crystallogr.
, vol.68
, pp. 381-390
-
-
Headd, J.J.1
-
48
-
-
77949535720
-
Features and development of Coot
-
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallograph. Sect. D 66, 486-501 (2010).
-
(2010)
Acta Crystallograph. Sect. D
, vol.66
, pp. 486-501
-
-
Emsley, P.1
Lohkamp, B.2
Scott, W.G.3
Cowtan, K.4
-
49
-
-
13244281317
-
Coot: Model-building tools for molecular graphics
-
Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
-
(2004)
Acta Crystallogr. D
, vol.60
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
|