메뉴 건너뛰기




Volumn 110, Issue 7, 2013, Pages 2466-2471

Cell-permeable probe for identification and imaging of sialidases

Author keywords

ABPP probe; Click chemistry; Imaging agents; Proteomics

Indexed keywords

ALKYNE HINGED 3 FLUOROSIALYL FLUORIDE; BIOTIN; ESTER PROTECTED ALKYNE HINGED 3 FLUOROSIALYL FLUORIDE; FLUORIDE; N ACETYLNEURAMINIC ACID; OSELTAMIVIR; SIALIDASE; STREPTAVIDIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84873722983     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1222183110     Document Type: Article
Times cited : (60)

References (60)
  • 2
    • 34948865783 scopus 로고    scopus 로고
    • Sialic acid utilization by bacterial pathogens
    • DOI 10.1099/mic.0.2007/009480-0
    • Severi E, Hood DW, Thomas GH (2007) Sialic acid utilization by bacterial pathogens. Microbiology 153(Pt 9):2817-2822. (Pubitemid 47517045)
    • (2007) Microbiology , vol.153 , Issue.9 , pp. 2817-2822
    • Severi, E.1    Hood, D.W.2    Thomas, G.H.3
  • 3
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • DOI 10.1021/cr000407m
    • Angata T, Varki A (2002) Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective. Chem Rev 102(2):439-469. (Pubitemid 35381636)
    • (2002) Chemical Reviews , vol.102 , Issue.2 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 4
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki A (2007) Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 446(7139):1023-1029.
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1023-1029
    • Varki, A.1
  • 5
    • 84861413498 scopus 로고    scopus 로고
    • Mammalian sialidases: Physiological and pathological roles in cellular functions
    • Miyagi T, Yamaguchi K (2012) Mammalian sialidases: Physiological and pathological roles in cellular functions. Glycobiology 22(7):880-896.
    • (2012) Glycobiology , vol.22 , Issue.7 , pp. 880-896
    • Miyagi, T.1    Yamaguchi, K.2
  • 6
    • 77956568840 scopus 로고    scopus 로고
    • Sialidases in vertebrates: A family of enzymes tailored for several cell functions
    • Monti E, et al. (2010) Sialidases in vertebrates: A family of enzymes tailored for several cell functions. Adv Carbohydr Chem Biochem 64:403-479.
    • (2010) Adv Carbohydr Chem Biochem , vol.64 , pp. 403-479
    • Monti, E.1
  • 7
    • 0015500920 scopus 로고
    • Localization of sialidase in the plasma membrane of rat liver cells
    • Schengrund CL, Jensen DS, Rosenberg A (1972) Localization of sialidase in the plasma membrane of rat liver cells. J Biol Chem 247(9):2742- 2746.
    • (1972) J Biol Chem , vol.247 , Issue.9 , pp. 2742-2746
    • Schengrund, C.L.1    Jensen, D.S.2    Rosenberg, A.3
  • 8
    • 0016210929 scopus 로고
    • Enzyme activity in invasive tumors of human breast and colon
    • Bosmann HB, Hall TC (1974) Enzyme activity in invasive tumors of human breast and colon. Proc Natl Acad Sci USA 71(5):1833-1837.
    • (1974) Proc Natl Acad Sci USA , vol.71 , Issue.5 , pp. 1833-1837
    • Bosmann, H.B.1    Hall, T.C.2
  • 9
    • 59149093715 scopus 로고    scopus 로고
    • Aberrant expression of sialidase and cancer progression
    • Miyagi T (2008) Aberrant expression of sialidase and cancer progression. Proc Jpn Acad, Ser B, Phys Biol Sci 84(10):407-418.
    • (2008) Proc Jpn Acad, Ser B, Phys Biol Sci , vol.84 , Issue.10 , pp. 407-418
    • Miyagi, T.1
  • 10
    • 34247154933 scopus 로고    scopus 로고
    • A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells
    • DOI 10.1038/sj.onc.1210341, PII 1210341
    • Wada T, et al. (2007) A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells. Oncogene 26(17):2483-2490. (Pubitemid 46597274)
    • (2007) Oncogene , vol.26 , Issue.17 , pp. 2483-2490
    • Wada, T.1    Hata, K.2    Yamaguchi, K.3    Shiozaki, K.4    Koseki, K.5    Moriya, S.6    Miyagi, T.7
  • 11
    • 55949107403 scopus 로고    scopus 로고
    • Plasma membrane-associated sialidase as a crucial regulator of transmembrane signalling
    • Miyagi T, Wada T, Yamaguchi K, Hata K, Shiozaki K (2008) Plasma membrane-associated sialidase as a crucial regulator of transmembrane signalling. J Biochem 144(3):279-285.
    • (2008) J Biochem , vol.144 , Issue.3 , pp. 279-285
    • Miyagi, T.1    Wada, T.2    Yamaguchi, K.3    Hata, K.4    Shiozaki, K.5
  • 12
    • 3543071604 scopus 로고    scopus 로고
    • Sialidase and malignancy: A minireview
    • DOI 10.1023/B:GLYC.0000024250.48506.bf
    • Miyagi T, Wada T, Yamaguchi K, Hata K (2004) Sialidase and malignancy: A minireview. Glycoconj J 20(3):189-198. (Pubitemid 39024047)
    • (2003) Glycoconjugate Journal , vol.20 , Issue.3 , pp. 189-198
    • Miyagi, T.1    Wada, T.2    Yamaguchi, K.3    Hata, K.4
  • 13
    • 0001437175 scopus 로고    scopus 로고
    • Disorders of glycoprotein degradation: α-mannosidosis, β-mannosidosis, fucosidosis, and sialidosis
    • eds Valle D, et al. (McGraw-Hill, New York), Available at
    • Thomas GH (2001) Disorders of glycoprotein degradation: α-mannosidosis, β-mannosidosis, fucosidosis, and sialidosis. Scriver's Online Metabolic and Molecular Bases of Inherited Disease, eds Valle D, et al. (McGraw-Hill, New York), Available at http://dx.doi.org/10.1036/ ommbid.170.
    • (2001) Scriver's Online Metabolic and Molecular Bases of Inherited Disease
    • Thomas, G.H.1
  • 14
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • DOI 10.1021/cr050288g
    • Evans MJ, Cravatt BF (2006) Mechanism-based profiling of enzyme families. Chem Rev 106(8):3279-3301. (Pubitemid 44376936)
    • (2006) Chemical Reviews , vol.106 , Issue.8 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 15
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cyclo-addition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev VV, Green LG, Fokin VV, Sharpless KB (2002) A stepwise huisgen cyclo-addition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew Chem Int Ed Engl 41(14):2596-2599.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 16
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • DOI 10.1016/S1359-6446(03)02933-7, PII S1359644603029337
    • Kolb HC, Sharpless KB (2003) The growing impact of click chemistry on drug discovery. Drug Discov Today 8(24):1128-1137. (Pubitemid 37547919)
    • (2003) Drug Discovery Today , vol.8 , Issue.24 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 18
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • DOI 10.1021/bi002579j
    • Kidd D, Liu Y, Cravatt BF (2001) Profiling serine hydrolase activities in complex proteomes. Biochemistry 40(13):4005-4015. (Pubitemid 32280438)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 19
    • 0036051482 scopus 로고    scopus 로고
    • Chemical approaches for functionally probing the proteome
    • Greenbaum D, et al. (2002) Chemical approaches for functionally probing the proteome. Mol Cell Proteomics 1(1):60-68.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.1 , pp. 60-68
    • Greenbaum, D.1
  • 20
    • 29444460784 scopus 로고    scopus 로고
    • Activity-based probes that target diverse cysteine protease families
    • Kato D, et al. (2005) Activity-based probes that target diverse cysteine protease families. Nat Chem Biol 1(1):33-38.
    • (2005) Nat Chem Biol , vol.1 , Issue.1 , pp. 33-38
    • Kato, D.1
  • 21
    • 33646594411 scopus 로고    scopus 로고
    • A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C
    • DOI 10.1021/ja060835v
    • Yuan F, Verhelst SH, Blum G, Coussens LM, Bogyo M (2006) A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C. J Am Chem Soc 128(17):5616-5617. (Pubitemid 43724347)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.17 , pp. 5616-5617
    • Yuan, F.1    Verhelst, S.H.L.2    Blum, G.3    Coussens, L.M.4    Bogyo, M.5
  • 22
    • 0013177603 scopus 로고    scopus 로고
    • Solid-phase synthesis of peptide vinyl sulfones as potential inhibitors and activity-based probes of cysteine proteases
    • DOI 10.1021/ol0275567
    • Wang G, Mahesh U, Chen GYJ, Yao SQ (2003) Solid-phase synthesis of peptide vinyl sulfones as potential inhibitors and activity-based probes of cysteine proteases. Org Lett 5(5):737-740. (Pubitemid 37141091)
    • (2003) Organic Letters , vol.5 , Issue.5 , pp. 737-740
    • Wang, G.1    Mahesh, U.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 23
    • 66149144747 scopus 로고    scopus 로고
    • Activity-based protein profiling of protein tyrosine phosphatases
    • Walls C, Zhou B, Zhang ZY (2009) Activity-based protein profiling of protein tyrosine phosphatases. Methods Mol Biol 519:417-429.
    • (2009) Methods Mol Biol , vol.519 , pp. 417-429
    • Walls, C.1    Zhou, B.2    Zhang, Z.Y.3
  • 24
    • 75149193938 scopus 로고    scopus 로고
    • Peptide-based activity-based probes (ABPs) for target-specific profiling of protein tyrosine phosphatases (PTPs)
    • Kalesh KA, et al. (2010) Peptide-based activity-based probes (ABPs) for target-specific profiling of protein tyrosine phosphatases (PTPs). Chem Commun (Camb) 46(4):589-591.
    • (2010) Chem Commun (Camb) , vol.46 , Issue.4 , pp. 589-591
    • Kalesh, K.A.1
  • 25
    • 70349128914 scopus 로고    scopus 로고
    • Profiling protein tyrosine phosphatase activity with mechanistic probes
    • Krishnamurthy D, Barrios AM (2009) Profiling protein tyrosine phosphatase activity with mechanistic probes. Curr Opin Chem Biol 13(4):375-381.
    • (2009) Curr Opin Chem Biol , vol.13 , Issue.4 , pp. 375-381
    • Krishnamurthy, D.1    Barrios, A.M.2
  • 26
    • 0036022519 scopus 로고    scopus 로고
    • Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype
    • DOI 10.1038/nbt714
    • Adam GC, Sorensen EJ, Cravatt BF (2002) Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype. Nat Biotechnol 20(8):805-809. (Pubitemid 34836757)
    • (2002) Nature Biotechnology , vol.20 , Issue.8 , pp. 805-809
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 29
    • 84863116427 scopus 로고    scopus 로고
    • Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes
    • Shi H, Zhang CJ, Chen GY, Yao SQ (2012) Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes. J Am Chem Soc 134(6):3001-3014.
    • (2012) J Am Chem Soc , vol.134 , Issue.6 , pp. 3001-3014
    • Shi, H.1    Zhang, C.J.2    Chen, G.Y.3    Yao, S.Q.4
  • 31
    • 7744233875 scopus 로고    scopus 로고
    • Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases
    • DOI 10.1021/ja047044i
    • Chan EWS, Chattopadhaya S, Panicker RC, Huang X, Yao SQ (2004) Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases. J Am Chem Soc 126(44):14435-14446. (Pubitemid 39463627)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.44 , pp. 14435-14446
    • Chan, E.W.S.1    Chattopadhaya, S.2    Panicker, R.C.3    Huang, X.4    Yao, S.Q.5
  • 32
    • 33646462162 scopus 로고    scopus 로고
    • Proteomic profiling of metal-loprotease activities with cocktails of active-site probes
    • Sieber SA, Niessen S, Hoover HS, Cravatt BF (2006) Proteomic profiling of metal-loprotease activities with cocktails of active-site probes. Nat Chem Biol 2(5):274-281.
    • (2006) Nat Chem Biol , vol.2 , Issue.5 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 33
    • 0037126198 scopus 로고    scopus 로고
    • Design and synthesis of activity probes for glycosidases
    • Tsai CS, Li YK, Lo LC (2002) Design and synthesis of activity probes for glycosidases. Org Lett 4(21):3607-3610.
    • (2002) Org Lett , vol.4 , Issue.21 , pp. 3607-3610
    • Tsai, C.S.1    Li, Y.K.2    Lo, L.C.3
  • 34
    • 7244251649 scopus 로고    scopus 로고
    • A strategy for functional proteomic analysis of glycosidase activity from cell lysates
    • DOI 10.1002/anie.200454235
    • Vocadlo DJ, Bertozzi CR (2004) A strategy for functional proteomic analysis of glycosidase activity from cell lysates. Angew Chem Int Ed Engl 43(40):5338-5342. (Pubitemid 39433912)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.40 , pp. 5338-5342
    • Vocadlo, D.J.1    Bertozzi, C.R.2
  • 35
    • 38349018251 scopus 로고    scopus 로고
    • Synthesis and use of mechanism-based protein-profiling probes for retaining beta-D-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ
    • Stubbs KA, et al. (2008) Synthesis and use of mechanism-based protein-profiling probes for retaining beta-D-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ. J Am Chem Soc 130(1):327-335.
    • (2008) J Am Chem Soc , vol.130 , Issue.1 , pp. 327-335
    • Stubbs, K.A.1
  • 36
    • 78649302683 scopus 로고    scopus 로고
    • Ultrasensitive in situ visualization of active glucocerebrosidase molecules
    • Witte MD, et al. (2010) Ultrasensitive in situ visualization of active glucocerebrosidase molecules. Nat Chem Biol 6(12):907-913.
    • (2010) Nat Chem Biol , vol.6 , Issue.12 , pp. 907-913
    • Witte, M.D.1
  • 37
    • 0025291833 scopus 로고
    • Photoaffinity labeling of a bacterial sialidase with an aryl azide derivative of sialic acid
    • van der Horst GT, Mancini GM, Brossmer R, Rose U, Verheijen FW (1990) Photoaffinity labeling of a bacterial sialidase with an aryl azide derivative of sialic acid. J Biol Chem 265(19):10801-10804.
    • (1990) J Biol Chem , vol.265 , Issue.19 , pp. 10801-10804
    • Van Der Horst, G.T.1    Mancini, G.M.2    Brossmer, R.3    Rose, U.4    Verheijen, F.W.5
  • 38
    • 27544498863 scopus 로고    scopus 로고
    • Design of a mechanism-based probe for neuraminidase to capture influenza viruses
    • Lu CP, et al. (2005) Design of a mechanism-based probe for neuraminidase to capture influenza viruses. Angew Chem Int Ed Engl 44(42):6888-6892.
    • (2005) Angew Chem Int Ed Engl , vol.44 , Issue.42 , pp. 6888-6892
    • Lu, C.P.1
  • 39
    • 33947483287 scopus 로고
    • Inhibition of N-acetylneuraminic acid aldolase by 3-fluorosialic acid
    • Gantt R, Millner S, Binkley SB (1964) Inhibition of N-acetylneuraminic acid aldolase by 3-fluorosialic acid. Biochemistry 3(12):1952-1960.
    • (1964) Biochemistry , vol.3 , Issue.12 , pp. 1952-1960
    • Gantt, R.1    Millner, S.2    Binkley, S.B.3
  • 41
    • 0028763159 scopus 로고
    • Inhibition of bacterial and viral sialidases by 3-fluoro-N- acetylneuraminic acid
    • DOI 10.1016/0008-6215(94)00133-2
    • Hagiwara T, Kijima-Suda I, Ido T, Ohrui H, Tomita K (1994) Inhibition of bacterial and viral sialidases by 3-fluoro-N-acetylneuraminic acid. Carbohydr Res 263(1):167-172. (Pubitemid 24297423)
    • (1994) Carbohydrate Research , vol.263 , Issue.1 , pp. 167-172
    • Hagiwara, T.1    Kijima-Suda, I.2    Ido, T.3    Ohrui, H.4    Tomita, K.5
  • 42
    • 0033592105 scopus 로고    scopus 로고
    • An efficient synthesis of CMP-3-fluoroneuraminic acid
    • Burkart MD, Vincent SP, Wong CH (1999) An efficient synthesis of CMP-3-fluoroneuraminic acid. Chem Commun (16):1525 -1526.
    • (1999) Chem Commun , Issue.16 , pp. 1525-1526
    • Burkart, M.D.1    Vincent, S.P.2    Wong, C.H.3
  • 43
    • 0033868508 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of fluorinated sugar nucleotide: Useful mechanistic Probes for glycosyltransferases
    • DOI 10.1016/S0968-0896(00)00139-5, PII S0968089600001395
    • Burkart MD, et al. (2000) Chemo-enzymatic synthesis of fluorinated sugar nucleotide: Useful mechanistic probes for glycosyltransferases. Bioorg Med Chem 8(8):1937-1946. (Pubitemid 30612485)
    • (2000) Bioorganic and Medicinal Chemistry , vol.8 , Issue.8 , pp. 1937-1946
    • Burkart, M.D.1    Vincent, S.P.2    Duffels, A.3    Murray, B.W.4    Ley, S.V.5    Wong, C.-H.6
  • 44
    • 0033866275 scopus 로고    scopus 로고
    • Syntheses of C-3-modified sialylglycosides as selective inhibitors of influenza hemagglutinin and neuraminidase
    • Sun XL, et al. (2000) Syntheses of C-3-modified sialylglycosides as selective inhibitors of influenza hemagglutinin and neuraminidase. Eur J Org Chem 2000(14):2643-2653.
    • (2000) Eur J Org Chem , vol.2000 , Issue.14 , pp. 2643-2653
    • Sun, X.L.1
  • 45
    • 0036266460 scopus 로고    scopus 로고
    • An O-glycoside of sialic acid derivative that inhibits both hemagglutinin and sialidase activities of influenza viruses
    • Guo CT, et al. (2002) An O-glycoside of sialic acid derivative that inhibits both hemagglutinin and sialidase activities of influenza viruses. Glycobiology 12(3):183-190.
    • (2002) Glycobiology , vol.12 , Issue.3 , pp. 183-190
    • Guo, C.T.1
  • 47
    • 41949134837 scopus 로고    scopus 로고
    • A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors
    • Buchini S, Buschiazzo A, Withers SG (2008) A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors. Angew Chem Int Ed Engl 47(14):2700-2703.
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.14 , pp. 2700-2703
    • Buchini, S.1    Buschiazzo, A.2    Withers, S.G.3
  • 48
    • 0028899712 scopus 로고
    • Disaccharide uptake and priming in animal cells: Inhibition of sialyl Lewis X by acetylated Gal beta 1→4GlcNAc beta-Onaphthalenemethanol
    • Sarkar AK, Fritz TA, Taylor WH, Esko JD (1995) Disaccharide uptake and priming in animal cells: Inhibition of sialyl Lewis X by acetylated Gal beta 1→4GlcNAc beta-Onaphthalenemethanol. Proc Natl Acad Sci USA 92(8):3323-3327.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.8 , pp. 3323-3327
    • Sarkar, A.K.1    Fritz, T.A.2    Taylor, W.H.3    Esko, J.D.4
  • 53
    • 77649204572 scopus 로고    scopus 로고
    • Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively
    • Bigi A, et al. (2010) Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively. Glycobiology 20(2):148-157.
    • (2010) Glycobiology , vol.20 , Issue.2 , pp. 148-157
    • Bigi, A.1
  • 55
    • 53049107996 scopus 로고    scopus 로고
    • Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase
    • Gut H, King SJ, Walsh MA (2008) Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase. FEBS Lett 582(23-24):3348-3352.
    • (2008) FEBS Lett , vol.582 , Issue.23-24 , pp. 3348-3352
    • Gut, H.1    King, S.J.2    Walsh, M.A.3
  • 56
    • 44049099406 scopus 로고    scopus 로고
    • The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates
    • Newstead SL, et al. (2008) The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates. J Biol Chem 283(14):9080-9088.
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 9080-9088
    • Newstead, S.L.1
  • 57
    • 0029904847 scopus 로고    scopus 로고
    • Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase: Possible implication for intralysosomal catabolism of keratan sulfate
    • DOI 10.1074/jbc.271.45.28359
    • Pshezhetsky AV, Potier M (1996) Association of N-acetylgalactosamine-6- sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate. J Biol Chem 271(45):28359-28365. (Pubitemid 26374653)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28359-28365
    • Pshezhetsky, A.V.1    Potier, M.2
  • 58
    • 45949098128 scopus 로고    scopus 로고
    • Influenza activity - United States and worldwide, 2007-08 season
    • Centers for Disease Control and Prevention (CDC)
    • Centers for Disease Control and Prevention (CDC) (2008) Influenza activity - United States and worldwide, 2007-08 season. MMWR Morb Mortal Wkly Rep 57(25):692-697.
    • (2008) MMWR Morb Mortal Wkly Rep , vol.57 , Issue.25 , pp. 692-697
  • 59
    • 50949106863 scopus 로고    scopus 로고
    • Surveillance for neuraminidase inhibitor resistance among human influenza a and B viruses circulating worldwide from 2004 to 2008
    • Sheu TG, et al. (2008) Surveillance for neuraminidase inhibitor resistance among human influenza A and B viruses circulating worldwide from 2004 to 2008. Antimicrob Agents Chemother 52(9):3284-3292.
    • (2008) Antimicrob Agents Chemother , vol.52 , Issue.9 , pp. 3284-3292
    • Sheu, T.G.1
  • 60
    • 3242811187 scopus 로고    scopus 로고
    • A fluorogenic probe for the copper(I)-catalyzed azide-alkyne ligation reaction: Modulation of the fluorescence emission via 3(n,pi)-1(pi,pi) inversion
    • Zhou Z, Fahrni CJ (2004) A fluorogenic probe for the copper(I)-catalyzed azide-alkyne ligation reaction: Modulation of the fluorescence emission via 3(n,pi)-1(pi,pi) inversion. J Am Chem Soc 126(29):8862-8863.
    • (2004) J Am Chem Soc , vol.126 , pp. 8862-8863
    • Zhou, Z.1    Fahrni, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.