메뉴 건너뛰기




Volumn 287, Issue 53, 2012, Pages 44320-44329

A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation

Author keywords

[No Author keywords available]

Indexed keywords

ARM STRUCTURES; CELLULAR PROCESS; CYTOSOLIC; DIPEPTIDYL PEPTIDASE; POSITIVE CHARGES; SUMOYLATION; WILD TYPES;

EID: 84871782137     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.397224     Document Type: Article
Times cited : (51)

References (62)
  • 1
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway. Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R., and Lima, C. D. (2010) The SUMO pathway. Emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11, 861-871
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 2
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. (2004) Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 4
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin andSUMOmodifications in DNA repair
    • Bergink, S., and Jentsch, S. (2009) Principles of ubiquitin andSUMOmodifications in DNA repair. Nature 458, 461-467
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 5
    • 24344445216 scopus 로고    scopus 로고
    • Something aboutSUMOinhibits transcription
    • Gill, G. (2005) Something aboutSUMOinhibits transcription. Curr. Opin. Genet. Dev. 15, 536-541
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 536-541
    • Gill, G.1
  • 6
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler, J. S., and Dejean, A. (2003) Nuclear and unclear functions of SUMO. Nat. Rev. Mol. Cell Biol. 4, 690-699
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 690-699
    • Seeler, J.S.1    Dejean, A.2
  • 7
    • 80052765356 scopus 로고    scopus 로고
    • SUMOylation and de-SUMOylation in response to DNA damage
    • Dou, H., Huang, C., Van Nguyen, T., Lu, L. S., and Yeh, E. T. (2011) SUMOylation and de-SUMOylation in response to DNA damage. FEBS Lett. 585, 2891-2896
    • (2011) FEBS Lett. , vol.585 , pp. 2891-2896
    • Dou, H.1    Huang, C.2    Van Nguyen, T.3    Lu, L.S.4    Yeh, E.T.5
  • 9
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M. H., Matic, I., Mann, M., and Hay, R. T. (2011) Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal. 4, rs4
    • (2011) Sci. Signal. , vol.4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 10
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal, A. C., Andersen, J. S., Ogg, S. C., Hay, R. T., Mann, M., and Lamond, A. I. (2006) Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell. Proteomics 5, 2298-2310
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 11
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic, I., Schimmel, J., Hendriks, I. A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., and Vertegaal, A. C. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell 39, 641-652
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    Van Santen, M.A.4    Van De Rijke, F.5    Van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.9
  • 12
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction. What's your function? New insights through SUMO-interacting motifs
    • Kerscher, O. (2007) SUMO junction. What's your function? New insights through SUMO-interacting motifs. EMBO reports 8, 550-555
    • (2007) EMBO Reports , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 13
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty, A. (2000) Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275, 36316-36323
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1
  • 15
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif. A reversal of the bound orientation
    • Song, J., Zhang, Z., Hu, W., and Chen, Y. (2005) Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif. A reversal of the bound orientation. J. Biol. Chem. 280, 40122-40129
    • (2005) J. Biol. Chem. , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 16
    • 14244260623 scopus 로고    scopus 로고
    • Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae
    • Hannich, J. T., Lewis, A., Kroetz, M. B., Li, S. J., Heide, H., Emili, A., and Hochstrasser, M. (2005) Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J. Biol. Chem. 280, 4102-4110
    • (2005) J. Biol. Chem. , vol.280 , pp. 4102-4110
    • Hannich, J.T.1    Lewis, A.2    Kroetz, M.B.3    Li, S.J.4    Heide, H.5    Emili, A.6    Hochstrasser, M.7
  • 18
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier, P., and Muller, S. (2009) Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol. Cell 33, 400-409
    • (2009) Mol. Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 20
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter, D., and Lima, C. D. (2005) Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435, 687-692
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 22
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases. A serine protease subfamily with high potential for drug discovery
    • Rosenblum, J. S., and Kozarich, J. W. (2003) Prolyl peptidases. A serine protease subfamily with high potential for drug discovery. Curr. Opin. Chem. Biol. 7, 496-504
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 23
    • 15044359454 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors: How do they work as new antidiabetic agents?
    • McIntosh, C. H., Demuth, H. U., Pospisilik, J. A., and Pederson, R. (2005) Dipeptidyl peptidase IV inhibitors: how do they work as new antidiabetic agents? Regul. Pept. 128, 159-165
    • (2005) Regul. Pept. , vol.128 , pp. 159-165
    • McIntosh, C.H.1    Demuth, H.U.2    Pospisilik, J.A.3    Pederson, R.4
  • 24
    • 0034471657 scopus 로고    scopus 로고
    • Postproline-cleaving peptidases having DP IV like enzyme activity. Post-proline peptidases
    • Abbott, C. A., Yu, D., McCaughan, G. W., and Gorrell, M. D. (2000) Postproline-cleaving peptidases having DP IV like enzyme activity. Post-proline peptidases. Adv. Exp. Med. Biol. 477, 103-109
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 103-109
    • Abbott, C.A.1    Yu, D.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 25
    • 3042734543 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity
    • Ajami, K., Abbott, C. A., McCaughan, G. W., and Gorrell, M. D. (2004) Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity. Biochim. Biophys. Acta 1679, 18-28
    • (2004) Biochim. Biophys. Acta , vol.1679 , pp. 18-28
    • Ajami, K.1    Abbott, C.A.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 26
    • 67650351587 scopus 로고    scopus 로고
    • Expression pattern of dipeptidyl peptidase IV activity and/or structure homologues in cancer
    • Kotacková, L., Baláziová, E., and Sedo, A. (2009) Expression pattern of dipeptidyl peptidase IV activity and/or structure homologues in cancer. Folia Biol. (Praha) 55, 77-84
    • (2009) Folia Biol. (Praha) , vol.55 , pp. 77-84
    • Kotacková, L.1    Baláziová, E.2    Sedo, A.3
  • 35
    • 33646706075 scopus 로고    scopus 로고
    • Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis
    • Yu, D. M., Wang, X. M., McCaughan, G. W., and Gorrell, M. D. (2006) Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis. FEBS J. 273, 2447-2460
    • (2006) FEBS J. , vol.273 , pp. 2447-2460
    • Yu, D.M.1    Wang, X.M.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 36
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO-conjugating enzymes
    • Bossis, G., and Melchior, F. (2006) Regulation of SUMOylation by reversible oxidation of SUMO-conjugating enzymes. Mol. Cell 21, 349-357
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 37
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25
    • Meulmeester, E., Kunze, M., Hsiao, H. H., Urlaub, H., and Melchior, F. (2008) Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell 30, 610-619
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 38
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler, A., Gast, A., Seeler, J. S., Dejean, A., and Melchior, F. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 41
    • 33845648469 scopus 로고    scopus 로고
    • Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site
    • Rummey, C., and Metz, G. (2007) Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site. Proteins 66, 160-171
    • (2007) Proteins , vol.66 , pp. 160-171
    • Rummey, C.1    Metz, G.2
  • 42
    • 80051862999 scopus 로고    scopus 로고
    • Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9). Is DPP8-selectivity an attainable goal?
    • Van Goethem, S., Matheeussen, V., Joossens, J., Lambeir, A. M., Chen, X., De Meester, I., Haemers, A., Augustyns, K., and Van der Veken, P. (2011) Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9). Is DPP8-selectivity an attainable goal? J. Med. Chem. 54, 5737-5746
    • (2011) J. Med. Chem. , vol.54 , pp. 5737-5746
    • Van Goethem, S.1    Matheeussen, V.2    Joossens, J.3    Lambeir, A.M.4    Chen, X.5    De Meester, I.6    Haemers, A.7    Augustyns, K.8    Van Der Veken, P.9
  • 43
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen, H. B., Branner, S., Wiberg, F. C., and Wagtmann, N. (2003) Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. 10, 19-25
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 45
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma, R., Löffler, B., Stihle, M., Huber, W., Ruf, A., and Hennig, M. (2003) Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 11, 947-959
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Löffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 46
    • 1642534610 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation
    • Aertgeerts, K. (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci. 13, 412-421
    • (2004) Protein Sci. , vol.13 , pp. 412-421
    • Aertgeerts, K.1
  • 47
    • 5644261220 scopus 로고    scopus 로고
    • Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface
    • Weihofen, W. A. (2004) Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface. J. Biol. Chem. 279, 43330-43335
    • (2004) J. Biol. Chem. , vol.279 , pp. 43330-43335
    • Weihofen, W.A.1
  • 48
    • 21244503095 scopus 로고    scopus 로고
    • Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein
    • Aertgeerts, K. (2005) Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein. J. Biol. Chem. 280, 19441-19444
    • (2005) J. Biol. Chem. , vol.280 , pp. 19441-19444
    • Aertgeerts, K.1
  • 49
    • 5144227957 scopus 로고    scopus 로고
    • Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family
    • Strop, P., Bankovich, A. J., Hansen, K. C., Garcia, K. C., and Brunger, A. T. (2004) Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family. J. Mol. Biol. 343, 1055-1065
    • (2004) J. Mol. Biol. , vol.343 , pp. 1055-1065
    • Strop, P.1    Bankovich, A.J.2    Hansen, K.C.3    Garcia, K.C.4    Brunger, A.T.5
  • 50
    • 80255122763 scopus 로고    scopus 로고
    • Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9
    • Tang, H. K., Chen, K. C., Liou, G. G., Cheng, S. C., Chien, C. H., Tang, H. Y., Huang, L. H., Chang, H. P., Chou, C. Y., and Chen, X. (2011) Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9. FEBS Lett. 585, 3409-3414
    • (2011) FEBS Lett. , vol.585 , pp. 3409-3414
    • Tang, H.K.1    Chen, K.C.2    Liou, G.G.3    Cheng, S.C.4    Chien, C.H.5    Tang, H.Y.6    Huang, L.H.7    Chang, H.P.8    Chou, C.Y.9    Chen, X.10
  • 51
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang, X. D., Goeres, J., Zhang, H., Yen, T. J., Porter, A. C., and Matunis, M. J. (2008) SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell 29, 729-741
    • (2008) Mol. Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 52
    • 57649198342 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification
    • Zhu, J., Zhu, S., Guzzo, C. M., Ellis, N. A., Sung, K. S., Choi, C. Y., and Matunis, M. J. (2008) Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification. J. Biol. Chem. 283, 29405-29415
    • (2008) J. Biol. Chem. , vol.283 , pp. 29405-29415
    • Zhu, J.1    Zhu, S.2    Guzzo, C.M.3    Ellis, N.A.4    Sung, K.S.5    Choi, C.Y.6    Matunis, M.J.7
  • 54
    • 67749145683 scopus 로고    scopus 로고
    • SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation
    • Cho, G., Lim, Y., and Golden, J. A. (2009) SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation. J. Biol. Chem. 284, 19592-19600
    • (2009) J. Biol. Chem. , vol.284 , pp. 19592-19600
    • Cho, G.1    Lim, Y.2    Golden, J.A.3
  • 55
    • 14344261035 scopus 로고    scopus 로고
    • Solution structure of human SUMO-3 C47S and its binding surface for Ubc9
    • Ding, H., Xu, Y., Chen, Q., Dai, H., Tang, Y., Wu, J., and Shi, Y. (2005) Solution structure of human SUMO-3 C47S and its binding surface for Ubc9. Biochemistry 44, 2790-2799
    • (2005) Biochemistry , vol.44 , pp. 2790-2799
    • Ding, H.1    Xu, Y.2    Chen, Q.3    Dai, H.4    Tang, Y.5    Wu, J.6    Shi, Y.7
  • 56
    • 34250013122 scopus 로고    scopus 로고
    • Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation
    • Knipscheer, P., van Dijk, W. J., Olsen, J. V., Mann, M., and Sixma, T. K. (2007) Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO J. 26, 2797-2807
    • (2007) EMBO J. , vol.26 , pp. 2797-2807
    • Knipscheer, P.1    Van Dijk, W.J.2    Olsen, J.V.3    Mann, M.4    Sixma, T.K.5
  • 57
    • 34248176792 scopus 로고    scopus 로고
    • Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction
    • Capili, A. D., and Lima, C. D. (2007) Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction. J. Mol. Biol. 369, 608-618
    • (2007) J. Mol. Biol. , vol.369 , pp. 608-618
    • Capili, A.D.1    Lima, C.D.2
  • 58
    • 34248146499 scopus 로고    scopus 로고
    • Structure of a SUMO-binding motif mimic bound to Smt3p-Ubc9p. Conservation of a noncovalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway
    • Duda, D. M., van Waardenburg, R. C., Borg, L. A., McGarity, S., Nourse, A., Waddell, M. B., Bjornsti, M. A., and Schulman, B. A. (2007) Structure of a SUMO-binding motif mimic bound to Smt3p-Ubc9p. Conservation of a noncovalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway. J. Mol. Biol. 369, 619-630
    • (2007) J. Mol. Biol. , vol.369 , pp. 619-630
    • Duda, D.M.1    Van Waardenburg, R.C.2    Borg, L.A.3    McGarity, S.4    Nourse, A.5    Waddell, M.B.6    Bjornsti, M.A.7    Schulman, B.A.8
  • 59
    • 80053912258 scopus 로고    scopus 로고
    • Swapping the SUMO isoform specificity of SUMO proteases SENP6 and SENP7
    • Alegre, K. O., and Reverter, D. (2011) Swapping the SUMO isoform specificity of SUMO proteases SENP6 and SENP7. J. Biol. Chem. 286, 36142-36151
    • (2011) J. Biol. Chem. , vol.286 , pp. 36142-36151
    • Alegre, K.O.1    Reverter, D.2
  • 60
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor down-regulation
    • Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L., and Radhakrishnan, I. (2003) Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor down-regulation. EMBO J. 22, 4597-4606
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 61
    • 0038820381 scopus 로고    scopus 로고
    • Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding
    • Kang, R. S., Daniels, C. M., Francis, S. A., Shih, S. C., Salerno, W. J., Hicke, L., and Radhakrishnan, I. (2003) Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell 113, 621-630
    • (2003) Cell , vol.113 , pp. 621-630
    • Kang, R.S.1    Daniels, C.M.2    Francis, S.A.3    Shih, S.C.4    Salerno, W.J.5    Hicke, L.6    Radhakrishnan, I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.