메뉴 건너뛰기




Volumn 43, Issue , 2015, Pages 966-974

Correction: Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems (Biochemical Society Transactions (2016) 43:5 (966-974) DOI: 10.1042/BST20150128);Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems

Author keywords

ATP binding cassette (ABC) transporter regulation; ATP binding cassette subfamily B (ABCB); Cystic fibrosis transmembrane conductance regulator (CFTR); FK506 binding protein (FKBP); P glycoprotein; Protein phosphorylation

Indexed keywords

ABC TRANSPORTER; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; FK 506 BINDING PROTEIN; HEAT SHOCK PROTEIN 90; MULTIDRUG RESISTANCE PROTEIN 1; MULTIDRUG RESISTANCE PROTEIN 3; ADENOSINE TRIPHOSPHATE; PLANT PROTEIN;

EID: 84947256967     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20150128_2     Document Type: Erratum
Times cited : (34)

References (110)
  • 1
    • 34247123807 scopus 로고    scopus 로고
    • Structure and function of ABC transporters
    • CrossRef PubMed
    • Linton, K.J. (2007) Structure and function of ABC transporters. Physiology 22, 122-130 CrossRef PubMed
    • (2007) Physiology , vol.22 , pp. 122-130
    • Linton, K.J.1
  • 2
    • 84922342044 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • CrossRef PubMed
    • Wilkens, S. (2015) Structure and mechanism of ABC transporters. F1000Prime Rep. 7, 14 CrossRef PubMed
    • (2015) F1000Prime Rep. , vol.7 , pp. 14
    • Wilkens, S.1
  • 3
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • CrossRef PubMed
    • Dean, M., Rzhetsky, A. and Allikmets, R. (2001) The human ATP-binding cassette (ABC) transporter superfamily. Genome Res. 11, 1156-1166 CrossRef PubMed
    • (2001) Genome Res. , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 4
    • 79953794574 scopus 로고    scopus 로고
    • Regulation of ABC transporter function via phosphorylation by protein kinases
    • CrossRef PubMed
    • Stolarczyk, E.I., Reiling, C.J. and Paumi, C.M. (2011) Regulation of ABC transporter function via phosphorylation by protein kinases. Curr. Pharm. Biotechnol. 12, 621-635 CrossRef PubMed
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 621-635
    • Stolarczyk, E.I.1    Reiling, C.J.2    Paumi, C.M.3
  • 6
    • 33846678695 scopus 로고    scopus 로고
    • The ABCA subfamily-gene and protein structures, functions and associated hereditary diseases
    • CrossRef PubMed
    • Albrecht, C. and Viturro, E. (2007) The ABCA subfamily-gene and protein structures, functions and associated hereditary diseases. Pflugers Arch. 453, 581-589 CrossRef PubMed
    • (2007) Pflugers Arch. , vol.453 , pp. 581-589
    • Albrecht, C.1    Viturro, E.2
  • 7
    • 80052509365 scopus 로고    scopus 로고
    • The lipid translocase, ABCA4: Seeing is believing
    • CrossRef PubMed
    • Pollock, N.L. and Callaghan, R. (2011) The lipid translocase, ABCA4: seeing is believing. FEBS J. 278, 3204-3214 CrossRef PubMed
    • (2011) FEBS J. , vol.278 , pp. 3204-3214
    • Pollock, N.L.1    Callaghan, R.2
  • 8
    • 84875220318 scopus 로고    scopus 로고
    • A comprehensive review of retinal gene therapy
    • CrossRef PubMed
    • Boye, S.E., Boye, S.L., Lewin, A.S. and Hauswirth, W.W. (2013) A comprehensive review of retinal gene therapy. Mol. Ther. 21, 509-519 CrossRef PubMed
    • (2013) Mol. Ther. , vol.21 , pp. 509-519
    • Boye, S.E.1    Boye, S.L.2    Lewin, A.S.3    Hauswirth, W.W.4
  • 9
    • 0035682189 scopus 로고    scopus 로고
    • Overview: ABC transporters and human disease
    • CrossRef PubMed
    • Gottesman, M.M. and Ambudkar, S. V. (2001) Overview: ABC transporters and human disease. J. Bioenerg. Biomembr. 33, 453-458 CrossRef PubMed
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 453-458
    • Gottesman, M.M.1    Ambudkar, S.V.2
  • 11
    • 77955895736 scopus 로고    scopus 로고
    • ABC proteins in antigen translocation and viral inhibition
    • CrossRef PubMed
    • Parcej, D. and Tampé, R. (2010) ABC proteins in antigen translocation and viral inhibition. Nat. Chem. Biol. 6, 572-580 CrossRef PubMed
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 572-580
    • Parcej, D.1    Tampé, R.2
  • 12
    • 84921032443 scopus 로고    scopus 로고
    • ABC transporters in adaptive immunity
    • CrossRef PubMed
    • Seyffer, F. and Tampé, R. (2015) ABC transporters in adaptive immunity. Biochim. Biophys. Acta 1850, 449-460 CrossRef PubMed
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 449-460
    • Seyffer, F.1    Tampé, R.2
  • 13
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • CrossRef PubMed
    • Cheng, S.H., Rich, D.P., Marshall, J., Gregory, R.J., Welsh, M.J. and Smith, A.E. (1991) Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 66, 1027-1036 CrossRef PubMed
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 14
    • 0032750221 scopus 로고    scopus 로고
    • Differential function of the two nucleotide binding domains on cystic fibrosis transmembrane conductance regulator
    • CrossRef PubMed
    • Nagel, G. (1999) Differential function of the two nucleotide binding domains on cystic fibrosis transmembrane conductance regulator. Biochim. Biophys. Acta 1461, 263-274 CrossRef PubMed
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 263-274
    • Nagel, G.1
  • 15
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • CrossRef PubMed
    • Dean, M. and Annilo, T. (2005) Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genomics Hum. Genet. 6, 123-142 CrossRef PubMed
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 17
    • 0033745088 scopus 로고    scopus 로고
    • Hepatic secretion of conjugated drugs and endogenous substances
    • CrossRef PubMed
    • Keppler, D. and Kö nig, J. (2000) Hepatic secretion of conjugated drugs and endogenous substances. Semin. Liver Dis. 20, 265-272 CrossRef PubMed
    • (2000) Semin. Liver Dis. , vol.20 , pp. 265-272
    • Keppler, D.1    König, J.2
  • 18
    • 84939540802 scopus 로고    scopus 로고
    • It takes more than two to tango: Regulation of plant ABC transporters
    • (Geisler, M., ed.), Springer, Switzerland
    • Geisler, M. (2014) It takes more than two to tango: regulation of plant ABC transporters. In Plant ABC Transporters (Geisler, M., ed.), pp. 241-270, Springer, Switzerland
    • (2014) Plant ABC Transporters , pp. 241-270
    • Geisler, M.1
  • 19
    • 34548385670 scopus 로고    scopus 로고
    • Mechanism of action of a sulphonylurea receptor SUR1 mutation (F132L) that causes DEND syndrome
    • CrossRef PubMed
    • Proks, P., Shimomura, K., Craig, T.J., Girard, C.A.J. and Ashcroft, F.M. (2007) Mechanism of action of a sulphonylurea receptor SUR1 mutation (F132L) that causes DEND syndrome. Hum. Mol. Genet. 16, 2011-2019 CrossRef PubMed
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2011-2019
    • Proks, P.1    Shimomura, K.2    Craig, T.J.3    Girard, C.A.J.4    Ashcroft, F.M.5
  • 20
    • 84922541623 scopus 로고    scopus 로고
    • Differing clinical presentations of two unrelated cases of X-lined adrenoleukodystrophy with identical mutation Y296C in the ABCD1 gene
    • PubMed
    • Sutovský, S., Kolníková, M., Petrovic, R., Kollár, B., Siarnik, P., Chandoga, J., Fischerová, M. and Turcáni, P. (2014) Differing clinical presentations of two unrelated cases of X-lined adrenoleukodystrophy with identical mutation Y296C in the ABCD1 gene. Neuro. Endrocinol. Lett. 35, 411-416 PubMed
    • (2014) Neuro. Endrocinol. Lett. , vol.35 , pp. 411-416
    • Sutovský, S.1    Kolníková, M.2    Petrovic, R.3    Kollár, B.4    Siarnik, P.5    Chandoga, J.6    Fischerová, M.7    Turcáni, P.8
  • 21
    • 84879576778 scopus 로고    scopus 로고
    • Impaired very long-chain acyl-CoA β-oxidation in human X-linked adrenoleukodystrophy fibroblasts is a direct consequence of ABCD1 transporter dysfunction
    • CrossRef PubMed
    • Wiesinger, C., Kunze, M., Regelsberger, G., Forss-Petter, S. and Berger, J. (2013) Impaired very long-chain acyl-CoA β-oxidation in human X-linked adrenoleukodystrophy fibroblasts is a direct consequence of ABCD1 transporter dysfunction. J. Biol. Chem. 288, 19269-19279 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 19269-19279
    • Wiesinger, C.1    Kunze, M.2    Regelsberger, G.3    Forss-Petter, S.4    Berger, J.5
  • 22
    • 17744390348 scopus 로고    scopus 로고
    • Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters
    • CrossRef PubMed
    • Berge, K.E. (2000) Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters. Science 290, 1771-1775 CrossRef PubMed
    • (2000) Science , vol.290 , pp. 1771-1775
    • Berge, K.E.1
  • 23
    • 80053436675 scopus 로고    scopus 로고
    • The ABCG family of membrane-associated transporters: You don't have to be big to be mighty
    • CrossRef PubMed
    • Kerr, I.D., Haider, A.J. and Gelissen, I.C. (2011) The ABCG family of membrane-associated transporters: you don't have to be big to be mighty. Br. J. Pharmacol. 164, 1767-1779 CrossRef PubMed
    • (2011) Br. J. Pharmacol. , vol.164 , pp. 1767-1779
    • Kerr, I.D.1    Haider, A.J.2    Gelissen, I.C.3
  • 24
    • 80052495026 scopus 로고    scopus 로고
    • ABCG transporters and disease
    • CrossRef PubMed
    • Woodward, O.M., Kö ttgen, A. and Kö ttgen, M. (2011) ABCG transporters and disease. FEBS J. 278, 3215-3225 CrossRef PubMed
    • (2011) FEBS J. , vol.278 , pp. 3215-3225
    • Woodward, O.M.1    Köttgen, A.2    Kö Ttgen, M.3
  • 26
    • 42149150462 scopus 로고    scopus 로고
    • The phosphate regulon and bacterial virulence: A regulatory network connecting phosphate homeostasis and pathogenesis
    • CrossRef PubMed
    • Lamarche, M.G., Wanner, B.L., Cré pin, S. and Harel, J. (2008) The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis. FEMS Microbiol. Rev. 32, 461-473 CrossRef PubMed
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 461-473
    • Lamarche, M.G.1    Wanner, B.L.2    Crépin, S.3    Harel, J.4
  • 29
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • CrossRef PubMed
    • Davidson, A.L. and Chen, J. (2004) ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 73, 241-268 CrossRef PubMed
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 30
    • 0028928549 scopus 로고
    • Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals
    • CrossRef PubMed
    • Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. (1995). Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27, 320-329 CrossRef PubMed
    • (1995) Curr. Genet. , vol.27 , pp. 320-329
    • Prasad, R.1    De Wergifosse, P.2    Goffeau, A.3    Balzi, E.4
  • 31
    • 0031909801 scopus 로고    scopus 로고
    • Characterisation of human steroid hormone transport mediated by Cdr1p, a multidrug transporter of Candida albicans, belonging to the ATP binding cassette super family
    • CrossRef PubMed
    • Krishnamurthy, S., Gupta, V., Snehlata, P. and Prasad, R. (1998). Characterisation of human steroid hormone transport mediated by Cdr1p, a multidrug transporter of Candida albicans, belonging to the ATP binding cassette super family. FEMS Microbiol. Lett. 158, 69-74 CrossRef PubMed
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 69-74
    • Krishnamurthy, S.1    Gupta, V.2    Snehlata, P.3    Prasad, R.4
  • 32
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
    • CrossRef PubMed
    • Hunter, T. (1995) Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling. Cell 80, 225-236 CrossRef PubMed
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 33
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease
    • CrossRef PubMed
    • Cohen, P. (2001) The role of protein phosphorylation in human health and disease. Eur. J. Biochem. 268, 5001-5010 CrossRef PubMed
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 34
    • 0242467078 scopus 로고    scopus 로고
    • PKA-mediated phosphorylation of the human K(ATP) channel: Separate roles of Kir6.2 and SUR1 subunit phosphorylation
    • CrossRef PubMed
    • Bé guin, P., Nagashima, K., Nishimura, M., Gonoi, T. and Seino, S. (1999) PKA-mediated phosphorylation of the human K(ATP) channel: separate roles of Kir6.2 and SUR1 subunit phosphorylation. EMBO J. 18, 4722-4732 CrossRef PubMed
    • (1999) EMBO J. , vol.18 , pp. 4722-4732
    • Béguin, P.1    Nagashima, K.2    Nishimura, M.3    Gonoi, T.4    Seino, S.5
  • 35
    • 0027460274 scopus 로고
    • Identification of specific sites in human P-glycoprotein phosphorylated by protein kinase C
    • PubMed
    • Chambers, T., Pohl, J., Raynor, R. and Kuo, J. (1993) Identification of specific sites in human P-glycoprotein phosphorylated by protein kinase C. J. Biol. Chem. 268, 4592-4595 PubMed
    • (1993) J. Biol. Chem. , vol.268 , pp. 4592-4595
    • Chambers, T.1    Pohl, J.2    Raynor, R.3    Kuo, J.4
  • 36
    • 0028213201 scopus 로고
    • Phosphorylation by protein kinase C and cyclic AMP-dependent protein kinase of synthetic peptides derived from the linker region of human P-glycoprotein
    • PubMed
    • Chambers, T., Pohl, J., Glass, D. and Kuo, J. (1994) Phosphorylation by protein kinase C and cyclic AMP-dependent protein kinase of synthetic peptides derived from the linker region of human P-glycoprotein. Biochem. J. 299, 309-315 PubMed
    • (1994) Biochem. J. , vol.299 , pp. 309-315
    • Chambers, T.1    Pohl, J.2    Glass, D.3    Kuo, J.4
  • 38
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • CrossRef PubMed
    • Tan, Y., Demeter, M.R., Ruan, H. and Comb, M.J. (2000) BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J. Biol. Chem. 275, 25865-25869 CrossRef PubMed
    • (2000) J. Biol. Chem. , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 39
    • 84865257568 scopus 로고    scopus 로고
    • Casein kinase 2α regulates multidrug resistance-associated protein 1 function via phosphorylation of Thr249
    • CrossRef PubMed
    • Stolarczyk, E.I., Reiling, C.J., Pickin, K.A., Coppage, R., Knecht, M.R. and Paumi, C.M. (2012) Casein kinase 2α regulates multidrug resistance-associated protein 1 function via phosphorylation of Thr249. Mol. Pharmacol. 82, 488-499 CrossRef PubMed
    • (2012) Mol. Pharmacol. , vol.82 , pp. 488-499
    • Stolarczyk, E.I.1    Reiling, C.J.2    Pickin, K.A.3    Coppage, R.4    Knecht, M.R.5    Paumi, C.M.6
  • 40
    • 34250362729 scopus 로고    scopus 로고
    • Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: Implications for posttranscriptional regulation of cyclooxygenase-2
    • CrossRef PubMed
    • Doller, A., Huwiler, A., Müller, R., Radeke, H.H., Pfeilschifter, J. and Eberhardt, W. (2007) Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2. Mol. Biol. Cell 18, 2137-2148 CrossRef PubMed
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2137-2148
    • Doller, A.1    Huwiler, A.2    Müller, R.3    Radeke, H.H.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 41
    • 0023897154 scopus 로고
    • Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases
    • CrossRef PubMed
    • Masatoshi, H., Shigeo, I., Toshio, T., Kazuo, N., Masaaki, I. and Hiroyoshi, H. (1988) Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases. Biochem. Pharmacol. 37, 2987-2992 CrossRef PubMed
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 2987-2992
    • Masatoshi, H.1    Shigeo, I.2    Toshio, T.3    Kazuo, N.4    Masaaki, I.5    Hiroyoshi, H.6
  • 44
    • 0032754371 scopus 로고    scopus 로고
    • Molecular pharmacology of the CFTR Cl- channel
    • CrossRef PubMed
    • Hwang, T.-C. and Sheppard, D.N. (1999) Molecular pharmacology of the CFTR Cl- channel. Trends Pharmacol. Sci. 20, 448-453 CrossRef PubMed
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 448-453
    • Hwang, T.-C.1    Sheppard, D.N.2
  • 45
    • 0032940125 scopus 로고    scopus 로고
    • Pharmacology of CFTR chloride channel activity
    • PubMed
    • Schultz, B.D., Singh, A.K., Devor, D.C. and Bridges, R.J. (1999). Pharmacology of CFTR chloride channel activity. Physiol Rev. 79, S109-S144 PubMed
    • (1999) Physiol Rev. , vol.79 , pp. S109-S144
    • Schultz, B.D.1    Singh, A.K.2    Devor, D.C.3    Bridges, R.J.4
  • 47
    • 0031881489 scopus 로고    scopus 로고
    • Actions of genistein on cystic fibrosis transmembrane conductance regulator channel gating. Evidence for two binding sites with opposite effects
    • CrossRef PubMed
    • Wang, F. (1998) Actions of genistein on cystic fibrosis transmembrane conductance regulator channel gating. Evidence for two binding sites with opposite effects. J. Gen. Physiol. 111, 477-490 CrossRef PubMed
    • (1998) J. Gen. Physiol. , vol.111 , pp. 477-490
    • Wang, F.1
  • 49
    • 0025296461 scopus 로고
    • Correlation of protein kinase C translocation, P-glycoprotein phosphorylation and reduced drug accumulation in multidrug resistant human KB cells
    • CrossRef PubMed
    • Chambers, T.C., Chalikonda, I. and Eilon, G. (1990) Correlation of protein kinase C translocation, P-glycoprotein phosphorylation and reduced drug accumulation in multidrug resistant human KB cells. Biochem. Biophys. Res. Commun. 169, 253-259 CrossRef PubMed
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 253-259
    • Chambers, T.C.1    Chalikonda, I.2    Eilon, G.3
  • 50
    • 0030800860 scopus 로고    scopus 로고
    • Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity
    • CrossRef PubMed
    • Szabó, K., Bakos, E., Welker, E., Müller, M., Goodfellow, H.R., Higgins, C.F., Váradi, A. and Sarkadi, B. (1997) Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity. J. Biol. Chem. 272, 23165-23171 CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 23165-23171
    • Szabó, K.1    Bakos, E.2    Welker, E.3    Müller, M.4    Goodfellow, H.R.5    Higgins, C.F.6    Váradi, A.7    Sarkadi, B.8
  • 51
    • 0027362087 scopus 로고
    • Identification of the major phosphorylation domain of murine mdr1b P-glycoprotein. Analysis of the protein kinase A and protein kinase C phosphorylation sites
    • PubMed
    • Orr, G.A., Han, E.K., Browne, P.C., Nieves, E., O'Connor, B.M., Yang, C.P. and Horwitz, S.B. (1993) Identification of the major phosphorylation domain of murine mdr1b P-glycoprotein. Analysis of the protein kinase A and protein kinase C phosphorylation sites. J. Biol. Chem. 268, 25054-25062 PubMed
    • (1993) J. Biol. Chem. , vol.268 , pp. 25054-25062
    • Orr, G.A.1    Han, E.K.2    Browne, P.C.3    Nieves, E.4    O'Connor, B.M.5    Yang, C.P.6    Horwitz, S.B.7
  • 52
    • 0032725782 scopus 로고    scopus 로고
    • Influence of phosphorylation by protein kinase A on CFTR at the cell surface and endoplasmic reticulum
    • CrossRef PubMed
    • Seibert, F.S., Chang, X.-B., Aleksandrov, A.A., Clarke, D.M., Hanrahan, J.W. and Riordan, J.R. (1999) Influence of phosphorylation by protein kinase A on CFTR at the cell surface and endoplasmic reticulum. Biochim. Biophys. Acta 1461, 275-283 CrossRef PubMed
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 275-283
    • Seibert, F.S.1    Chang, X.-B.2    Aleksandrov, A.A.3    Clarke, D.M.4    Hanrahan, J.W.5    Riordan, J.R.6
  • 53
    • 84873127876 scopus 로고    scopus 로고
    • CFTR-SLC26 transporter interactions in epithelia
    • CrossRef PubMed
    • Fong, P. (2012) CFTR-SLC26 transporter interactions in epithelia. Biophys. Rev. 4, 107-116 CrossRef PubMed
    • (2012) Biophys. Rev. , vol.4 , pp. 107-116
    • Fong, P.1
  • 54
    • 65549153992 scopus 로고    scopus 로고
    • Role of individual R domain phosphorylation sites in CFTR regulation by protein kinase A
    • CrossRef PubMed
    • Hegedus, T., Aleksandrov, A., Mengos, A., Cui, L., Jensen, T.J. and Riordan, J.R. (2009) Role of individual R domain phosphorylation sites in CFTR regulation by protein kinase A. Biochim. Biophys. Acta 1788, 1341-1349 CrossRef PubMed
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1341-1349
    • Hegedus, T.1    Aleksandrov, A.2    Mengos, A.3    Cui, L.4    Jensen, T.J.5    Riordan, J.R.6
  • 55
    • 75649088951 scopus 로고    scopus 로고
    • NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR
    • CrossRef PubMed
    • Kanelis, V., Hudson, R.P., Thibodeau, P.H., Thomas, P.J. and Forman-Kay, J.D. (2010) NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR. EMBO J. 29, 263-277 CrossRef PubMed
    • (2010) EMBO J. , vol.29 , pp. 263-277
    • Kanelis, V.1    Hudson, R.P.2    Thibodeau, P.H.3    Thomas, P.J.4    Forman-Kay, J.D.5
  • 56
    • 42649118768 scopus 로고    scopus 로고
    • Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR
    • CrossRef PubMed
    • Hegedus, T., Serohijos, A.W.R., Dokholyan, N.V, He, L. and Riordan, J.R. (2008) Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR. J. Mol. Biol. 378, 1052-1063 CrossRef PubMed
    • (2008) J. Mol. Biol. , vol.378 , pp. 1052-1063
    • Hegedus, T.1    Serohijos, A.W.R.2    Dokholyan, N.V.3    He, L.4    Riordan, J.R.5
  • 57
    • 71449097048 scopus 로고    scopus 로고
    • ABC transporters in Saccharomyces cerevisiae and their interactors: New technology advances the biology of the ABCC (MRP) subfamily
    • CrossRef PubMed
    • Paumi, C.M., Chuk, M., Snider, J., Stagljar, I. and Michaelis, S. (2009). ABC transporters in Saccharomyces cerevisiae and their interactors: new technology advances the biology of the ABCC (MRP) subfamily. Microbiol. Mol. Biol. Rev. 73, 577-593 CrossRef PubMed
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 577-593
    • Paumi, C.M.1    Chuk, M.2    Snider, J.3    Stagljar, I.4    Michaelis, S.5
  • 58
    • 55249120230 scopus 로고    scopus 로고
    • Negative regulation of the yeast ABC transporter Ycf1p by phosphorylation within its N-terminal extension
    • CrossRef PubMed
    • Paumi, C.M., Chuk, M., Chevelev, I., Stagljar, I. and Michaelis, S. (2008). Negative regulation of the yeast ABC transporter Ycf1p by phosphorylation within its N-terminal extension. J. Biol. Chem. 283, 27079-27088 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 27079-27088
    • Paumi, C.M.1    Chuk, M.2    Chevelev, I.3    Stagljar, I.4    Michaelis, S.5
  • 59
    • 78650492409 scopus 로고    scopus 로고
    • Suppression of Ycf1p function by Cka1p-dependent phosphorylation is attenuated in response to salt stress
    • CrossRef PubMed
    • Pickin, K.A., Ezenwajiaku, N., Overcash, H., Sethi, M., Knecht, M.R. and Paumi, C.M. (2010) Suppression of Ycf1p function by Cka1p-dependent phosphorylation is attenuated in response to salt stress. FEMS Yeast Res. 10, 839-857 CrossRef PubMed
    • (2010) FEMS Yeast Res. , vol.10 , pp. 839-857
    • Pickin, K.A.1    Ezenwajiaku, N.2    Overcash, H.3    Sethi, M.4    Knecht, M.R.5    Paumi, C.M.6
  • 60
    • 84893723233 scopus 로고    scopus 로고
    • Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function
    • CrossRef PubMed
    • Katayama, K., Yamaguchi, M., Noguchi, K. and Sugimoto, Y. (2014). Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function. Cancer Lett. 345, 124-131 CrossRef PubMed
    • (2014) Cancer Lett. , vol.345 , pp. 124-131
    • Katayama, K.1    Yamaguchi, M.2    Noguchi, K.3    Sugimoto, Y.4
  • 61
    • 84862641651 scopus 로고    scopus 로고
    • FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability
    • CrossRef PubMed
    • Hutt, D.M., Roth, D.M., Chalfant, M.A., Youker, R.T., Matteson, J., Brodsky, J.L. and Balch, W.E. (2012) FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability. J. Biol. Chem. 287, 21914-21925 CrossRef PubMed
    • (2012) J. Biol. Chem. , vol.287 , pp. 21914-21925
    • Hutt, D.M.1    Roth, D.M.2    Chalfant, M.A.3    Youker, R.T.4    Matteson, J.5    Brodsky, J.L.6    Balch, W.E.7
  • 62
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • CrossRef PubMed
    • Loo, M.A., Jensen, T.J., Cui, L., Hou, Y., Chang, X.B. and Riordan, J.R. (1998) Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 17, 6879-6887 CrossRef PubMed
    • (1998) EMBO J. , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 63
    • 34447543047 scopus 로고    scopus 로고
    • The Bcl-2 regulator FKBP38-calmodulin-Ca2+ is inhibited by Hsp90
    • CrossRef PubMed
    • Edlich, F., Erdmann, F., Jarczowski, F., Moutty, M.-C., Weiwad, M. and Fischer, G. (2007) The Bcl-2 regulator FKBP38-calmodulin-Ca2+ is inhibited by Hsp90. J. Biol. Chem. 282, 15341-15348 CrossRef PubMed
    • (2007) J. Biol. Chem. , vol.282 , pp. 15341-15348
    • Edlich, F.1    Erdmann, F.2    Jarczowski, F.3    Moutty, M.-C.4    Weiwad, M.5    Fischer, G.6
  • 64
    • 73949113446 scopus 로고    scopus 로고
    • Chaperone domains convert prolyl isomerases into generic catalysts of protein folding
    • CrossRef PubMed
    • Jakob, R.P., Zoldák, G., Aumüller, T. and Schmid, F.X. (2009) Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc. Natl. Acad. Sci. U.S.A. 106, 20282-20287 CrossRef PubMed
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20282-20287
    • Jakob, R.P.1    Zoldák, G.2    Aumüller, T.3    Schmid, F.X.4
  • 65
    • 0347918856 scopus 로고    scopus 로고
    • Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP-binding cassette transporter A1 for the high density lipoprotein assembly
    • CrossRef PubMed
    • Yamauchi, Y., Hayashi, M., Abe-Dohmae, S. and Yokoyama, S. (2003). Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP-binding cassette transporter A1 for the high density lipoprotein assembly. J. Biol. Chem. 278, 47890-47897 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 47890-47897
    • Yamauchi, Y.1    Hayashi, M.2    Abe-Dohmae, S.3    Yokoyama, S.4
  • 66
    • 0141844589 scopus 로고    scopus 로고
    • Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I
    • CrossRef PubMed
    • Martinez, L.O., Agerholm-Larsen, B., Wang, N., Chen, W. and Tall, A.R. (2003) Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I. J. Biol. Chem. 278, 37368-37374 CrossRef PubMed
    • (2003) J. Biol. Chem. , vol.278 , pp. 37368-37374
    • Martinez, L.O.1    Agerholm-Larsen, B.2    Wang, N.3    Chen, W.4    Tall, A.R.5
  • 67
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate "export" pump in the vacuolar membrane of plants
    • CrossRef
    • Martinoia, E., Grill, E., Tommasini, R., Kreuz, K. and Amrhein, N. (1993). ATP-dependent glutathione S-conjugate "export" pump in the vacuolar membrane of plants. Nature 364, 247-249 CrossRef
    • (1993) Nature , vol.364 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 69
    • 0028129854 scopus 로고
    • A herbicide antidote (safener) induces the activity of both the herbicide detoxifying enzyme and of a vacuolar transporter for the detoxified herbicide
    • CrossRef PubMed
    • Gaillard, C., Dufaud, A., Tommasini, R., Kreuz, K., Amrhein, N. and Martinoia, E. (1994) A herbicide antidote (safener) induces the activity of both the herbicide detoxifying enzyme and of a vacuolar transporter for the detoxified herbicide. FEBS Lett. 352, 219-221 CrossRef PubMed
    • (1994) FEBS Lett. , vol.352 , pp. 219-221
    • Gaillard, C.1    Dufaud, A.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5    Martinoia, E.6
  • 72
    • 0347683331 scopus 로고    scopus 로고
    • An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis
    • CrossRef PubMed
    • Sparkes, I.A., Brandizzi, F., Slocombe, S.P., El-Shami, M., Hawes, C. and Baker, A. (2003) An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis. Plant Physiol. 133, 1809-1819 CrossRef PubMed
    • (2003) Plant Physiol. , vol.133 , pp. 1809-1819
    • Sparkes, I.A.1    Brandizzi, F.2    Slocombe, S.P.3    El-Shami, M.4    Hawes, C.5    Baker, A.6
  • 74
    • 0035839555 scopus 로고    scopus 로고
    • The Arabidopsis thaliana ABC protein superfamily, a complete inventory
    • CrossRef PubMed
    • Sánchez-Fernández, R., Davies, T.G., Coleman, J.O. and Rea, P.A. (2001) The Arabidopsis thaliana ABC protein superfamily, a complete inventory. J. Biol. Chem. 276, 30231-302344 CrossRef PubMed
    • (2001) J. Biol. Chem. , vol.276 , pp. 30231-302344
    • Sánchez-Fernández, R.1    Davies, T.G.2    Coleman, J.O.3    Rea, P.A.4
  • 75
    • 0035209943 scopus 로고    scopus 로고
    • Multidrug resistance-like genes of Arabidopsis required for auxin transport and auxin-mediated development
    • CrossRef PubMed
    • Noh, B., Murphy, A.S. and Spalding, E.P. (2001) Multidrug resistance-like genes of Arabidopsis required for auxin transport and auxin-mediated development. Plant Cell 13, 2441-2454 CrossRef PubMed
    • (2001) Plant Cell , vol.13 , pp. 2441-2454
    • Noh, B.1    Murphy, A.S.2    Spalding, E.P.3
  • 78
    • 0037295840 scopus 로고    scopus 로고
    • Auxin transport - Shaping the plant
    • CrossRef PubMed
    • Friml, J. (2003) Auxin transport - shaping the plant. Curr. Opin. Plant Biol. 6, 7-12 CrossRef PubMed
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 7-12
    • Friml, J.1
  • 79
    • 34347387045 scopus 로고    scopus 로고
    • Polar transport of the plant hormone auxin - The role of PIN-FORMED (PIN) proteins
    • CrossRef PubMed
    • Zazímalová, E., Krecek, P., Skůpa, P., Hoyerová, K. and Petrásek, J. (2007) Polar transport of the plant hormone auxin - the role of PIN-FORMED (PIN) proteins. Cell. Mol. Life Sci. 64, 1621-1637 CrossRef PubMed
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1621-1637
    • Zazímalová, E.1    Krecek, P.2    Skůpa, P.3    Hoyerová, K.4    Petrásek, J.5
  • 82
  • 84
    • 84863840544 scopus 로고    scopus 로고
    • Plant lessons: Exploring ABCB functionality through structural modeling
    • PubMed
    • Bailly, A., Yang, H., Martinoia, E., Geisler, M. and Murphy, AS. (2012). Plant lessons: exploring ABCB functionality through structural modeling. Front. Plant Sci. 2, 108 PubMed
    • (2012) Front. Plant Sci. , vol.2 , pp. 108
    • Bailly, A.1    Yang, H.2    Martinoia, E.3    Geisler, M.4    Murphy, A.S.5
  • 85
    • 10744223685 scopus 로고    scopus 로고
    • TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19
    • CrossRef PubMed
    • Geisler, M., Kolukisaoglu, H.U., Bouchard, R., Billion, K., Berger, J., Saal, B., Frangne, N., Koncz-Kalman, Z., Koncz, C., Dudler, R. et al. (2003). TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol. Biol. Cell 14, 4238-4249 CrossRef PubMed
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4238-4249
    • Geisler, M.1    Kolukisaoglu, H.U.2    Bouchard, R.3    Billion, K.4    Berger, J.5    Saal, B.6    Frangne, N.7    Koncz-Kalman, Z.8    Koncz, C.9    Dudler, R.10
  • 87
    • 33646831086 scopus 로고    scopus 로고
    • Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, contributes to nonhost resistance to inappropriate pathogens that enter by direct penetration
    • CrossRef PubMed
    • Stein, M., Dittgen, J., Sánchez-Rodríguez, C., Hou, B.-H., Molina, A., Schulze-Lefert, P., Lipka, V. and Somerville, S. (2006) Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, contributes to nonhost resistance to inappropriate pathogens that enter by direct penetration. Plant Cell 18, 731-746 CrossRef PubMed
    • (2006) Plant Cell , vol.18 , pp. 731-746
    • Stein, M.1    Dittgen, J.2    Sánchez-Rodríguez, C.3    Hou, B.-H.4    Molina, A.5    Schulze-Lefert, P.6    Lipka, V.7    Somerville, S.8
  • 88
    • 34247270870 scopus 로고    scopus 로고
    • The ABC transporter AtPDR8 is a cadmium extrusion pump conferring heavy metal resistance
    • CrossRef PubMed
    • Kim, D.-Y., Bovet, L., Maeshima, M., Martinoia, E. and Lee, Y. (2007). The ABC transporter AtPDR8 is a cadmium extrusion pump conferring heavy metal resistance. Plant J. 50, 207-218 CrossRef PubMed
    • (2007) Plant J. , vol.50 , pp. 207-218
    • Kim, D.-Y.1    Bovet, L.2    Maeshima, M.3    Martinoia, E.4    Lee, Y.5
  • 91
    • 84907741829 scopus 로고    scopus 로고
    • ATP-dependent binding cassette transporter G family member 16 increases plant tolerance to abscisic acid and assists in basal resistance against pseudomonas syringae DC3000
    • CrossRef PubMed
    • Ji, H., Peng, Y., Meckes, N., Allen, S., Stewart, C.N. and Traw, M.B. (2014) ATP-dependent binding cassette transporter G family member 16 increases plant tolerance to abscisic acid and assists in basal resistance against pseudomonas syringae DC3000. Plant Physiol. 166, 879-888 CrossRef PubMed
    • (2014) Plant Physiol. , vol.166 , pp. 879-888
    • Ji, H.1    Peng, Y.2    Meckes, N.3    Allen, S.4    Stewart, C.N.5    Traw, M.B.6
  • 93
    • 0032479995 scopus 로고    scopus 로고
    • The pdr12 ABC transporter is required for the development of weak organic acid resistance in yeast
    • CrossRef PubMed
    • Piper, P., Mahé, Y., Thompson, S., Pandjaitan, R., Holyoak, C., Egner, R., Mühlbauer, M., Coote, P. and Kuchler, K. (1998) The pdr12 ABC transporter is required for the development of weak organic acid resistance in yeast. EMBO J. 17, 4257-4265 CrossRef PubMed
    • (1998) EMBO J. , vol.17 , pp. 4257-4265
    • Piper, P.1    Mahé, Y.2    Thompson, S.3    Pandjaitan, R.4    Holyoak, C.5    Egner, R.6    Mühlbauer, M.7    Coote, P.8    Kuchler, K.9
  • 94
    • 0031056684 scopus 로고    scopus 로고
    • Complete inventory of the yeast ABC proteins
    • CrossRef PubMed
    • Decottignies, A. and Goffeau, A. (1997) Complete inventory of the yeast ABC proteins. Nat. Genet. 15, 137-145 CrossRef PubMed
    • (1997) Nat. Genet. , vol.15 , pp. 137-145
    • Decottignies, A.1    Goffeau, A.2
  • 95
    • 33645709418 scopus 로고    scopus 로고
    • Loss of AtPDR8, a plasma membrane ABC transporter of Arabidopsis thaliana, causes hypersensitive cell death upon pathogen infection
    • CrossRef PubMed
    • Kobae, Y., Sekino, T., Yoshioka, H., Nakagawa, T., Martinoia, E. and Maeshima, M. (2006) Loss of AtPDR8, a plasma membrane ABC transporter of Arabidopsis thaliana, causes hypersensitive cell death upon pathogen infection. Plant Cell Physiol. 47, 309-318 CrossRef PubMed
    • (2006) Plant Cell Physiol. , vol.47 , pp. 309-318
    • Kobae, Y.1    Sekino, T.2    Yoshioka, H.3    Nakagawa, T.4    Martinoia, E.5    Maeshima, M.6
  • 97
    • 33646271601 scopus 로고    scopus 로고
    • Phosphoproteomics in Arabidopsis: Moving from empirical to predictive science
    • CrossRef PubMed
    • Peck, S.C. (2006) Phosphoproteomics in Arabidopsis: moving from empirical to predictive science. J. Exp. Bot. 57, 1523-1527 CrossRef PubMed
    • (2006) J. Exp. Bot. , vol.57 , pp. 1523-1527
    • Peck, S.C.1
  • 99
    • 36549031157 scopus 로고    scopus 로고
    • Plant evolution: AGC kinases tell the auxin tale
    • CrossRef PubMed
    • Galván-Ampudia, C.S. and Offringa, R. (2007) Plant evolution: AGC kinases tell the auxin tale. Trends Plant Sci. 12, 541-547 CrossRef PubMed
    • (2007) Trends Plant Sci. , vol.12 , pp. 541-547
    • Galván-Ampudia, C.S.1    Offringa, R.2
  • 101
    • 36549026787 scopus 로고    scopus 로고
    • Flavonoids and auxin transport: Modulators or regulators?
    • CrossRef PubMed
    • Peer, W.A. and Murphy, A.S. (2007) Flavonoids and auxin transport: modulators or regulators? Trends Plant Sci. 12, 556-563 CrossRef PubMed
    • (2007) Trends Plant Sci. , vol.12 , pp. 556-563
    • Peer, W.A.1    Murphy, A.S.2
  • 103
    • 0032912589 scopus 로고    scopus 로고
    • Structure and function of the CFTR chloride channel
    • PubMed
    • Sheppard, D.N. and Welsh, M.J. (1999) Structure and function of the CFTR chloride channel. Physiol. Rev. 79, S23-S45 PubMed
    • (1999) Physiol. Rev. , vol.79 , pp. S23-S45
    • Sheppard, D.N.1    Welsh, M.J.2
  • 104
    • 84914158342 scopus 로고    scopus 로고
    • Block of ATP-binding cassette B19 ion channel activity by 5-nitro-2-(3-phenylpropylamino)-benzoic acid impairs polar auxin transport and root gravitropism
    • CrossRef PubMed
    • Cho, M., Henry, E.M., Lewis, D.R., Wu, G., Muday, G.K. and Spalding, E.P. (2014) Block of ATP-binding cassette B19 ion channel activity by 5-nitro-2-(3-phenylpropylamino)-benzoic acid impairs polar auxin transport and root gravitropism. Plant Physiol. 166, 2091-2099 CrossRef PubMed
    • (2014) Plant Physiol. , vol.166 , pp. 2091-2099
    • Cho, M.1    Henry, E.M.2    Lewis, D.R.3    Wu, G.4    Muday, G.K.5    Spalding, E.P.6
  • 105
    • 0036847334 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana at FKBP42 that is membrane-bound and interacts with Hsp90
    • CrossRef PubMed
    • Kamphausen, T., Fanghä nel, J., Neumann, D., Schulz, B. and Rahfeld, J.-U. (2002) Characterization of Arabidopsis thaliana At FKBP42 that is membrane-bound and interacts with Hsp90. Plant J. 32, 263-276 CrossRef PubMed
    • (2002) Plant J. , vol.32 , pp. 263-276
    • Kamphausen, T.1    Fanghä Nel, J.2    Neumann, D.3    Schulz, B.4    Rahfeld, J.-U.5
  • 106
    • 34648816541 scopus 로고    scopus 로고
    • Tête-à-tête: The function of FKBPs in plant development
    • CrossRef PubMed
    • Geisler, M. and Bailly, A. (2007) Tête-à-tête: the function of FKBPs in plant development. Trends Plant Sci. 12, 465-473 CrossRef PubMed
    • (2007) Trends Plant Sci. , vol.12 , pp. 465-473
    • Geisler, M.1    Bailly, A.2
  • 109
    • 84871256005 scopus 로고    scopus 로고
    • The AGC kinase, PINOID, blocks interactive ABCB/PIN auxin transport
    • CrossRef PubMed
    • Wang, B., Henrichs, S. and Geisler, M. (2012) The AGC kinase, PINOID, blocks interactive ABCB/PIN auxin transport. Plant Signal. Behav. 7, 1515-1517 CrossRef PubMed
    • (2012) Plant Signal. Behav. , vol.7 , pp. 1515-1517
    • Wang, B.1    Henrichs, S.2    Geisler, M.3
  • 110
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • CrossRef PubMed
    • Nühse, T.S., Stensballe, A., Jensen, O.N. and Peck, S.C. (2004). Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16, 2394-3405 CrossRef PubMed
    • (2004) Plant Cell , vol.16 , pp. 2394-3405
    • Nühse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.