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Volumn 113, Issue 5, 2016, Pages 1162-1167

Onion-like glycodendrimersomes from sequencedefined Janus glycodendrimers and influence of architecture on reactivity to a lectin

Author keywords

Glycolipid mimics; Self assembly; Synthetic multilamellar vesicles

Indexed keywords

AGGLUTININ; DENDRIMER; GLYCAN; JANUS GLYCODENDRIMER; LECTIN; MANNOSE; UNCLASSIFIED DRUG; CARBOHYDRATE;

EID: 84957309340     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1524976113     Document Type: Article
Times cited : (84)

References (34)
  • 1
    • 77953076879 scopus 로고    scopus 로고
    • Self-assembly of Janus dendrimers into uniform dendrimersomes and other complex architectures
    • Percec V, et al. (2010) Self-assembly of Janus dendrimers into uniform dendrimersomes and other complex architectures. Science 328 (5981): 1009-1014.
    • (2010) Science , vol.328 , Issue.5981 , pp. 1009-1014
    • Percec, V.1
  • 2
    • 83755171312 scopus 로고    scopus 로고
    • Predicting the size and properties of dendrimersomes from the lamellar structure of their amphiphilic Janus dendrimers
    • Peterca M, Percec V, Leowanawat P, Bertin A (2011) Predicting the size and properties of dendrimersomes from the lamellar structure of their amphiphilic Janus dendrimers. J Am Chem Soc 133 (50): 20507-20520.
    • (2011) J Am Chem Soc , vol.133 , Issue.50 , pp. 20507-20520
    • Peterca, M.1    Percec, V.2    Leowanawat, P.3    Bertin, A.4
  • 3
    • 84903457066 scopus 로고    scopus 로고
    • Self-assembly of amphiphilic Janus dendrimers into uniform onion-like dendrimersomes with predictable size and number of bilayers
    • Zhang S, et al. (2014) Self-assembly of amphiphilic Janus dendrimers into uniform onion-like dendrimersomes with predictable size and number of bilayers. Proc Natl Acad Sci USA 111 (25): 9058-9063.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.25 , pp. 9058-9063
    • Zhang, S.1
  • 4
    • 0015521532 scopus 로고
    • The significance of glycosylated proteins
    • Winterburn PJ, Phelps CF (1972) The significance of glycosylated proteins. Nature 236 (5343): 147-151.
    • (1972) Nature , vol.236 , Issue.5343 , pp. 147-151
    • Winterburn, P.J.1    Phelps, C.F.2
  • 5
    • 84985532538 scopus 로고
    • Tumor lectinology: At the intersection of carbohydrate chemistry, biochemistry, cell biology and oncology
    • Gabius H-J (1988) Tumor lectinology: At the intersection of carbohydrate chemistry, biochemistry, cell biology and oncology. Angew Chem Int Ed Engl 27: 1267-1276.
    • (1988) Angew Chem Int Ed Engl , vol.27 , pp. 1267-1276
    • Gabius, H.-J.1
  • 6
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • Bertozzi CR, Kiessling LL (2001) Chemical glycobiology. Science 291 (5512): 2357-2364.
    • (2001) Science , vol.291 , Issue.5512 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 7
    • 77953635153 scopus 로고    scopus 로고
    • Chemical approaches to glycobiology
    • Kiessling LL, Splain RA (2010) Chemical approaches to glycobiology. Annu Rev Biochem 79: 619-653.
    • (2010) Annu Rev Biochem , vol.79 , pp. 619-653
    • Kiessling, L.L.1    Splain, R.A.2
  • 8
    • 84930821775 scopus 로고    scopus 로고
    • The magic of the sugar code
    • Gabius H-J (2015) The magic of the sugar code. Trends Biochem Sci 40 (7): 341.
    • (2015) Trends Biochem Sci , vol.40 , Issue.7 , pp. 341
    • Gabius, H.-J.1
  • 9
    • 84929600607 scopus 로고    scopus 로고
    • The logic of automated glycan assembly
    • Seeberger PH (2015) The logic of automated glycan assembly. Acc Chem Res 48 (5): 1450-1463.
    • (2015) Acc Chem Res , vol.48 , Issue.5 , pp. 1450-1463
    • Seeberger, P.H.1
  • 10
    • 0346981999 scopus 로고    scopus 로고
    • Influencing receptorligand binding mechanisms with multivalent ligand architecture
    • Gestwicki JE, Cairo CW, Strong LE, Oetjen KA, Kiessling LL (2002) Influencing receptorligand binding mechanisms with multivalent ligand architecture. J Am Chem Soc 124 (50): 14922-14933.
    • (2002) J Am Chem Soc , vol.124 , Issue.50 , pp. 14922-14933
    • Gestwicki, J.E.1    Cairo, C.W.2    Strong, L.E.3    Oetjen, K.A.4    Kiessling, L.L.5
  • 11
    • 0037960821 scopus 로고    scopus 로고
    • Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/hydroxyl-functionalized dendrimers
    • Woller EK, Walter ED, Morgan JR, Singel DJ, Cloninger MJ (2003) Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/hydroxyl-functionalized dendrimers. J AmChem Soc 125 (29): 8820-8826.
    • (2003) J AmChem Soc , vol.125 , Issue.29 , pp. 8820-8826
    • Woller, E.K.1    Walter, E.D.2    Morgan, J.R.3    Singel, D.J.4    Cloninger, M.J.5
  • 12
    • 77958510703 scopus 로고    scopus 로고
    • Glycopolypeptides via living polymerization of glycosylated-L-lysine N-carboxyanhydrides
    • Kramer JR, Deming TJ (2010) Glycopolypeptides via living polymerization of glycosylated-L-lysine N-carboxyanhydrides. J Am Chem Soc 132 (42): 15068-15071.
    • (2010) J Am Chem Soc , vol.132 , Issue.42 , pp. 15068-15071
    • Kramer, J.R.1    Deming, T.J.2
  • 13
    • 84893060002 scopus 로고    scopus 로고
    • Synthetic glycopolymers: Some recent developments
    • Zhang Q, Haddleton DM (2013) Synthetic glycopolymers: Some recent developments. Adv Polym Sci 262: 39-60.
    • (2013) Adv Polym Sci , vol.262 , pp. 39-60
    • Zhang, Q.1    Haddleton, D.M.2
  • 14
    • 84876713670 scopus 로고    scopus 로고
    • Real-time evaluation of binding mechanisms in multivalent interactions: A surface plasmon resonance kinetic approach
    • Munoz EM, Correa J, Riguera R, Fernandez-Megia E (2013) Real-time evaluation of binding mechanisms in multivalent interactions: A surface plasmon resonance kinetic approach. J Am Chem Soc 135 (16): 5966-5969.
    • (2013) J Am Chem Soc , vol.135 , Issue.16 , pp. 5966-5969
    • Munoz, E.M.1    Correa, J.2    Riguera, R.3    Fernandez-Megia, E.4
  • 15
    • 84893761630 scopus 로고    scopus 로고
    • Carbohydrate-lectin recognition of sequence-defined heteromultivalent glycooligomers
    • Ponader D, et al. (2014) Carbohydrate-lectin recognition of sequence-defined heteromultivalent glycooligomers. J Am Chem Soc 136 (5): 2008-2016.
    • (2014) J Am Chem Soc , vol.136 , Issue.5 , pp. 2008-2016
    • Ponader, D.1
  • 16
    • 84879348746 scopus 로고    scopus 로고
    • Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins
    • Percec V, et al. (2013) Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins. J Am Chem Soc 135 (24): 9055-9077.
    • (2013) J Am Chem Soc , vol.135 , Issue.24 , pp. 9055-9077
    • Percec, V.1
  • 17
    • 84930820197 scopus 로고    scopus 로고
    • The glycobiology of the CD system: A dictionary for translating marker designations into glycan/lectin structure and function
    • Gabius H-J, Kaltner H, Kopitz J, André S (2015) The glycobiology of the CD system: A dictionary for translating marker designations into glycan/lectin structure and function. Trends Biochem Sci 40 (7): 360-376.
    • (2015) Trends Biochem Sci , vol.40 , Issue.7 , pp. 360-376
    • Gabius, H.-J.1    Kaltner, H.2    Kopitz, J.3    André, S.4
  • 19
    • 84904704297 scopus 로고    scopus 로고
    • Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles
    • Colombo M, Raposo G, Théry C (2014) Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles. Annu Rev Cell Dev Biol 30: 255-289.
    • (2014) Annu Rev Cell Dev Biol , vol.30 , pp. 255-289
    • Colombo, M.1    Raposo, G.2    Théry, C.3
  • 20
    • 84929506373 scopus 로고    scopus 로고
    • Ectosomes and exosomes: Shedding the confusion between extracellular vesicles
    • Cocucci E, Meldolesi J (2015) Ectosomes and exosomes: Shedding the confusion between extracellular vesicles. Trends Cell Biol 25 (6): 364-372.
    • (2015) Trends Cell Biol , vol.25 , Issue.6 , pp. 364-372
    • Cocucci, E.1    Meldolesi, J.2
  • 21
    • 0037013292 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
    • Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y (2002) Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. J Biol Chem277 (18): 15979-15984.
    • (2002) J Biol Chem , vol.277 , Issue.18 , pp. 15979-15984
    • Velloso, L.M.1    Svensson, K.2    Schneider, G.3    Pettersson, R.F.4    Lindqvist, Y.5
  • 22
    • 34948911583 scopus 로고    scopus 로고
    • Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36
    • Satoh T, et al. (2007) Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36. J Biol Chem 282 (38): 28246-28255.
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 28246-28255
    • Satoh, T.1
  • 23
    • 84880070996 scopus 로고    scopus 로고
    • Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII)
    • Zheng C, et al. (2013) Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII). J Biol Chem 288 (28): 20499-20509.
    • (2013) J Biol Chem , vol.288 , Issue.28 , pp. 20499-20509
    • Zheng, C.1
  • 24
    • 84896861605 scopus 로고    scopus 로고
    • Structural basis for disparate sugarbinding specificities in the homologous cargo receptors ERGIC-53 and VIP36
    • Satoh T, Suzuki K, Yamaguchi T, Kato K (2014) Structural basis for disparate sugarbinding specificities in the homologous cargo receptors ERGIC-53 and VIP36. PLoS One 9 (2): E87963.
    • (2014) PLoS One , vol.9 , Issue.2 , pp. e87963
    • Satoh, T.1    Suzuki, K.2    Yamaguchi, T.3    Kato, K.4
  • 26
    • 0034733506 scopus 로고    scopus 로고
    • The structural features of concanavalin A governing non-proline peptide isomerization
    • Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R (2000) The structural features of concanavalin A governing non-proline peptide isomerization. J Biol Chem 275 (26): 19778-19787.
    • (2000) J Biol Chem , vol.275 , Issue.26 , pp. 19778-19787
    • Bouckaert, J.1    Dewallef, Y.2    Poortmans, F.3    Wyns, L.4    Loris, R.5
  • 27
    • 84911462287 scopus 로고    scopus 로고
    • Mimicking biological membranes with programmable glycan ligands self-assembled from amphiphilic Janus glycodendrimers
    • Zhang S, et al. (2014) Mimicking biological membranes with programmable glycan ligands self-assembled from amphiphilic Janus glycodendrimers. Angew Chem Int Ed Engl 53 (41): 10899-10903.
    • (2014) Angew Chem Int Ed Engl , vol.53 , Issue.41 , pp. 10899-10903
    • Zhang, S.1
  • 28
    • 84924918141 scopus 로고    scopus 로고
    • Dissecting molecular aspects of cell interactions using glycodendrimersomes with programmable glycan presentation and engineered human lectins
    • Zhang S, et al. (2015) Dissecting molecular aspects of cell interactions using glycodendrimersomes with programmable glycan presentation and engineered human lectins. Angew Chem Int Ed Engl 54 (13): 4036-4040.
    • (2015) Angew Chem Int Ed Engl , vol.54 , Issue.13 , pp. 4036-4040
    • Zhang, S.1
  • 29
    • 84945280400 scopus 로고    scopus 로고
    • Glycodendrimersomes from sequence-defined Janus glycodendrimers reveal high activity and sensor capacity for the agglutination by natural variants of human lectins
    • Zhang S, et al. (2015) Glycodendrimersomes from sequence-defined Janus glycodendrimers reveal high activity and sensor capacity for the agglutination by natural variants of human lectins. J Am Chem Soc 137 (41): 13334-13344.
    • (2015) J Am Chem Soc , vol.137 , Issue.41 , pp. 13334-13344
    • Zhang, S.1
  • 30
  • 31
    • 77956404731 scopus 로고    scopus 로고
    • Multivalent lectin-carbohydrate interactions energetics and mechanisms of binding
    • Dam TK, Brewer CF (2010) Multivalent lectin-carbohydrate interactions energetics and mechanisms of binding. Adv Carbohydr Chem Biochem 63: 139-164.
    • (2010) Adv Carbohydr Chem Biochem , vol.63 , pp. 139-164
    • Dam, T.K.1    Brewer, C.F.2
  • 32
    • 84930818151 scopus 로고    scopus 로고
    • Axon glycoprotein routing in nerve polarity, function, and repair
    • Abad-Rodríguez J, Díez-Revuelta N (2015) Axon glycoprotein routing in nerve polarity, function, and repair. Trends Biochem Sci 40 (7): 385-396.
    • (2015) Trends Biochem Sci , vol.40 , Issue.7 , pp. 385-396
    • Abad-Rodríguez, J.1    Díez-Revuelta, N.2
  • 33
    • 84928975425 scopus 로고    scopus 로고
    • Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface
    • Zhang S, et al. (2015) Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface. Proc Natl Acad Sci USA 112 (18): 5585-5590.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.18 , pp. 5585-5590
    • Zhang, S.1
  • 34
    • 19044370069 scopus 로고    scopus 로고
    • A new combined computational and NMR-spectroscopical strategy for the identification of additional conformational constraints of the bound ligand in an aprotic solvent
    • Siebert H-C, et al. (2000) A new combined computational and NMR-spectroscopical strategy for the identification of additional conformational constraints of the bound ligand in an aprotic solvent. ChemBioChem 1 (3): 181-195.
    • (2000) ChemBioChem , vol.1 , Issue.3 , pp. 181-195
    • Siebert, H.-C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.