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Volumn 28, Issue 13, 2008, Pages 4434-4444

Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN 37; CHAPERONE; CYCLIN DEPENDENT KINASE 1; GELDANAMYCIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; POLYPEPTIDE; PROTEIN KINASE; PROTEIN KINASE TPK2; PROTEIN SIS1; PROTEIN YDJ1;

EID: 46149083959     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00543-08     Document Type: Article
Times cited : (23)

References (59)
  • 1
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1: A nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti, S., C. Esser, and J. Hohfeld. 2003. BAG-1: a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 8:225-231.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hohfeld, J.3
  • 3
    • 0034625161 scopus 로고    scopus 로고
    • Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis
    • Batkin, M., I. Schvartz, and S. Shaltiel. 2000. Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: characterization of the sites by mutagenesis. Biochemistry 39:5366-5373.
    • (2000) Biochemistry , vol.39 , pp. 5366-5373
    • Batkin, M.1    Schvartz, I.2    Shaltiel, S.3
  • 4
    • 0031004769 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70
    • Bercovieh, B., I. Stancovski, A. Mayer, N. Blumenfeld, A. Laszlo, A. L. Schwartz, and A. Ciechanover. 1997. Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70. J. Biol. Chem. 272:9002-9010.
    • (1997) J. Biol. Chem , vol.272 , pp. 9002-9010
    • Bercovieh, B.1    Stancovski, I.2    Mayer, A.3    Blumenfeld, N.4    Laszlo, A.5    Schwartz, A.L.6    Ciechanover, A.7
  • 5
    • 0032558972 scopus 로고    scopus 로고
    • Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeast
    • Brodsky, J. L., J. G. Lawrence, and A. J. Caplan. 1998. Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeast. Biochemistry 37:18045- 18055.
    • (1998) Biochemistry , vol.37 , pp. 18045-18055
    • Brodsky, J.L.1    Lawrence, J.G.2    Caplan, A.J.3
  • 7
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143-1155.
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 8
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • Caplan, A. J., and M. G. Douglas. 1991. Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114:609-621.
    • (1991) J. Cell Biol , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 9
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan, A. J., A. K. Mandal, and M. A. Theodoraki. 2007. Molecular chaperones and protein kinase quality control. Trends Cell Biol. 17:87-92.
    • (2007) Trends Cell Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 10
    • 0026686468 scopus 로고
    • Farnesylation of YDJIp is required for function at elevated growth temperatures in Saccharomyces cerevisiae
    • Caplan, A. J., J. Tsai, P. J. Casey, and M. G. Douglas. 1992. Farnesylation of YDJIp is required for function at elevated growth temperatures in Saccharomyces cerevisiae. J. Biol. Chem. 267:18890-18895.
    • (1992) J. Biol. Chem , vol.267 , pp. 18890-18895
    • Caplan, A.J.1    Tsai, J.2    Casey, P.J.3    Douglas, M.G.4
  • 11
    • 27144551963 scopus 로고    scopus 로고
    • ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: Inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia
    • Castro, J. E., C. E. Prada, O. Loria, A. Kamal, L. Chen, F. J. Burrows, and T. J. Kipps. 2005. ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia. Blood 106:2506-2512.
    • (2005) Blood , vol.106 , pp. 2506-2512
    • Castro, J.E.1    Prada, C.E.2    Loria, O.3    Kamal, A.4    Chen, L.5    Burrows, F.J.6    Kipps, T.J.7
  • 12
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M. E., and A. J. Caplan. 1998. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3:28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 13
    • 33748747967 scopus 로고    scopus 로고
    • Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway
    • Cintron, N. S., and D. Toft. 2006. Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway. J. Biol. Chem. 281:26235-26244.
    • (2006) J. Biol. Chem , vol.281 , pp. 26235-26244
    • Cintron, N.S.1    Toft, D.2
  • 17
    • 0030040989 scopus 로고    scopus 로고
    • The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast
    • Dey, B., A. J. Caplan, and F. Boschelli. 1996. The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast. Mol. Biol. Cell 7:91-100.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 91-100
    • Dey, B.1    Caplan, A.J.2    Boschelli, F.3
  • 18
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan, C. Y., S. Lee, and D. M. Cyr. 2003. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8:309-316.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 19
    • 0742305339 scopus 로고    scopus 로고
    • Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function
    • Fan, C. Y., S. Lee, H. Y. Ren, and D. M. Cyr. 2004. Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol. Biol. Cell 15:761-773.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 761-773
    • Fan, C.Y.1    Lee, S.2    Ren, H.Y.3    Cyr, D.M.4
  • 20
    • 0033974108 scopus 로고    scopus 로고
    • Cdc37 promotes the stability of protein kinases Cdc28 and Cak1
    • Farrell, A., and D. O. Morgan. 2000. Cdc37 promotes the stability of protein kinases Cdc28 and Cak1. Mol. Cell. Biol. 20:749-754.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 749-754
    • Farrell, A.1    Morgan, D.O.2
  • 21
    • 40749124091 scopus 로고    scopus 로고
    • Felts, S. J., L. M. Karnitz, and D. O. Toft. 2007. Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR). Cell Stress Chaperones 12:353-363.
    • Felts, S. J., L. M. Karnitz, and D. O. Toft. 2007. Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR). Cell Stress Chaperones 12:353-363.
  • 22
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:603-647.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 25
    • 0344875614 scopus 로고    scopus 로고
    • GrpE, a nucleotide exchange factor for DnaK
    • Harrison, C. 2003. GrpE, a nucleotide exchange factor for DnaK. Cell Stress Chaperones 8:218-224.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 218-224
    • Harrison, C.1
  • 26
    • 0032478703 scopus 로고    scopus 로고
    • Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase
    • Hartson, S. D., E. A. Ottinger, W. Huang, G. Barany, P. Burn, and R. L. Matts. 1998. Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase. J. Biol. Chem. 273:8475-8482.
    • (1998) J. Biol. Chem , vol.273 , pp. 8475-8482
    • Hartson, S.D.1    Ottinger, E.A.2    Huang, W.3    Barany, G.4    Burn, P.5    Matts, R.L.6
  • 28
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
    • Kabani, M., J. M. Beckerich, and J. L. Brodsky. 2002. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 22:4677-4689.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4677-4689
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 29
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways
    • Kimura, Y., I. Yahara, and S. Lindquist. 1995. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268:1362-1365.
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 30
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
    • Lee, D. H., M. Y. Sherman, and A. L. Goldberg. 1996. Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:4773-4781.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3
  • 31
    • 0037164751 scopus 로고    scopus 로고
    • The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
    • Lee, P., J. Rao, A. Fliss, E. Yang, S. Garrett, and A. J. Caplan. 2002. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J. Cell Biol. 159:1051-1059.
    • (2002) J. Cell Biol , vol.159 , pp. 1051-1059
    • Lee, P.1    Rao, J.2    Fliss, A.3    Yang, E.4    Garrett, S.5    Caplan, A.J.6
  • 33
    • 33748743974 scopus 로고    scopus 로고
    • Crystal structure of yeast Sisl peptide-binding fragment and Hsp70 Ssa1 C-terminal complex
    • Li, J., Y. Wu, X. Qian, and B. Sha. 2006. Crystal structure of yeast Sisl peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. Biochem. J. 398:353-360.
    • (2006) Biochem. J , vol.398 , pp. 353-360
    • Li, J.1    Wu, Y.2    Qian, X.3    Sha, B.4
  • 34
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1
    • Lu, Z., and D. M. Cyr. 1998. Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273:27824-27830.
    • (1998) J. Biol. Chem , vol.273 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 35
    • 0025824364 scopus 로고
    • Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins
    • Luke, M. M., A. Sutton, and K. T. Arndt. 1991. Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J. Cell Biol. 114:623-638.
    • (1991) J. Cell Biol , vol.114 , pp. 623-638
    • Luke, M.M.1    Sutton, A.2    Arndt, K.T.3
  • 36
  • 37
    • 0034602390 scopus 로고    scopus 로고
    • Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties
    • Mayr, C., K. Richter, H. Lilie, and J. Buchner. 2000. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J. Biol. Chem. 275:34140-34146.
    • (2000) J. Biol. Chem , vol.275 , pp. 34140-34146
    • Mayr, C.1    Richter, K.2    Lilie, H.3    Buchner, J.4
  • 38
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan, A. J., M. D. Scott, and J. Frydman. 2005. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121:739-748.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 39
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., C. Patterson, W. Zhang, J. M. Younger, and D. M. Cyr. 2001. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3:100-105.
    • (2001) Nat. Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 40
    • 33846107847 scopus 로고    scopus 로고
    • The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
    • Park, S. H., N. Bolender, F. Eisele, Z. Kostova, J. Takeuchi, P. Coffino, and D. H. Wolf. 2007. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol. Biol. Cell 18:153-165.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 153-165
    • Park, S.H.1    Bolender, N.2    Eisele, F.3    Kostova, Z.4    Takeuchi, J.5    Coffino, P.6    Wolf, D.H.7
  • 41
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the hsp90 molecular chaperone machinery
    • Pearl, L. H., and C. Prodromou. 2006. Structure and mechanism of the hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75:271-294.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 42
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high-affinity binding of Hsp90 and Cdc37
    • Prince, T., and R. L. Matts. 2004. Definition of protein kinase sequence motifs that trigger high-affinity binding of Hsp90 and Cdc37. J. Biol. Chem. 279:39975-39981.
    • (2004) J. Biol. Chem , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 43
    • 0035937187 scopus 로고    scopus 로고
    • Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor
    • Rao, J., P. Lee, S. Benzene, C. Cardozo, J. Albertus, D. M. Robins, and A. J. Caplan. 2001. Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J. Biol. Chem. 276:5814-5820.
    • (2001) J. Biol. Chem , vol.276 , pp. 5814-5820
    • Rao, J.1    Lee, P.2    Benzene, S.3    Cardozo, C.4    Albertus, J.5    Robins, D.M.6    Caplan, A.J.7
  • 45
    • 34249853249 scopus 로고    scopus 로고
    • Sahi, C, and E. A. Craig. 2007. Network of general and specialty J. protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. USA 104:7163-7168.
    • Sahi, C, and E. A. Craig. 2007. Network of general and specialty J. protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. USA 104:7163-7168.
  • 46
    • 34250871853 scopus 로고    scopus 로고
    • All in the family: Atypical Hsp70 chaperones are conserved modulators of FIsp70 activity
    • Shaner, L., and K. A. Morano. 2007. All in the family: atypical Hsp70 chaperones are conserved modulators of FIsp70 activity. Cell Stress Chaperones 12:1-8.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 1-8
    • Shaner, L.1    Morano, K.A.2
  • 47
    • 0018801093 scopus 로고
    • Sequence of two phosphorylated sites in the catalytic subunit of bovine cardiac muscle adenosine 3′:5′-monophosphate-dependent protein kinase
    • Shoji, S., K. Titani, J. G. Demaille, and E. H. Fischer. 1979. Sequence of two phosphorylated sites in the catalytic subunit of bovine cardiac muscle adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 254: 6211-6214.
    • (1979) J. Biol. Chem , vol.254 , pp. 6211-6214
    • Shoji, S.1    Titani, K.2    Demaille, J.G.3    Fischer, E.H.4
  • 48
    • 35248818750 scopus 로고    scopus 로고
    • Akt shows variable sensitivity to an Hsp90 inhibitor depending on cell context
    • Theodoraki, M. A., M. Kunjappu, D. W. Sternberg, and A. J. Caplan. 2007. Akt shows variable sensitivity to an Hsp90 inhibitor depending on cell context. Exp. Cell Res. 313:3851-3858.
    • (2007) Exp. Cell Res , vol.313 , pp. 3851-3858
    • Theodoraki, M.A.1    Kunjappu, M.2    Sternberg, D.W.3    Caplan, A.J.4
  • 49
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai, J., and M. G. Douglas. 1996. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271:9347-9354.
    • (1996) J. Biol. Chem , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 50
    • 28844478925 scopus 로고    scopus 로고
    • Molecular guardians for newborn proteins: Ribosome-associated chaperones and their role in protein folding
    • Wegrzyn, R. D., and E. Heuerling. 2005. Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding. Cell Mol. Life Sci. 62:2727-2738.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 2727-2738
    • Wegrzyn, R.D.1    Heuerling, E.2
  • 51
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff, B., J. P. Chapple, J. van der Spuy, J. Hohfeld, and M. E. Cheetham. 2005. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 15:1058-1064.
    • (2005) Curr. Biol , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 52
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L., and S. L. Lindquist. 2005. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5:761-772.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 53
    • 0027291238 scopus 로고
    • Heat-shock protein hsp90 governs the activity of pp60v-src kinase
    • Xu, Y., and S. Lindquist. 1993. Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sci. USA 90:7074-7078.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 54
    • 0029891796 scopus 로고    scopus 로고
    • The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation
    • Yaglom, J. A., A. L. Goldberg, D. Finley, and M. Y. Sherman. 1996. The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation. Mol. Cell. Biol. 16:3679-3684.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 3679-3684
    • Yaglom, J.A.1    Goldberg, A.L.2    Finley, D.3    Sherman, M.Y.4
  • 55
    • 29244432181 scopus 로고    scopus 로고
    • Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    • Yam, A. Y., V. Albanese, H. T. Lin, and J. Frydman. 2005. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J. Biol. Chem. 280:41252-41261.
    • (2005) J. Biol. Chem , vol.280 , pp. 41252-41261
    • Yam, A.Y.1    Albanese, V.2    Lin, H.T.3    Frydman, J.4
  • 56
    • 0030856102 scopus 로고    scopus 로고
    • Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli
    • Yonemoto, W., M. L. McGlone, B. Grant, and S. S. Taylor. 1997. Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli. Protein Eng. 10:915-925.
    • (1997) Protein Eng , vol.10 , pp. 915-925
    • Yonemoto, W.1    McGlone, M.L.2    Grant, B.3    Taylor, S.S.4
  • 57
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • Younger, J. M., H. Y. Ren, L. Chen, C. Y. Fan, A. Fields, C. Patterson, and D. M. Cyr. 2004. A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J. Cell Biol. 167:1075-1085.
    • (2004) J. Cell Biol , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 58
    • 19544371342 scopus 로고    scopus 로고
    • Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation
    • Yun, B. G., and R. L. Matts. 2005. Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation. Exp. Cell Res. 307:212-223.
    • (2005) Exp. Cell Res , vol.307 , pp. 212-223
    • Yun, B.G.1    Matts, R.L.2
  • 59
    • 1842477464 scopus 로고    scopus 로고
    • Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4
    • Zhao, Q., F. Boschelli, A. J. Caplan, and K. T. Arndt. 2004. Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem. 279:12560-12564.
    • (2004) J. Biol. Chem , vol.279 , pp. 12560-12564
    • Zhao, Q.1    Boschelli, F.2    Caplan, A.J.3    Arndt, K.T.4


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