메뉴 건너뛰기




Volumn 290, Issue 3, 2015, Pages 1752-1759

Efflux by small multidrug resistance proteins is inhibited by membrane-interactive helix-stapled peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BLOOD; CELL MEMBRANES; CELLS; CYTOLOGY; OLIGOMERS; PEPTIDES;

EID: 84922174583     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.616185     Document Type: Article
Times cited : (25)

References (36)
  • 1
    • 70450169243 scopus 로고    scopus 로고
    • Inhibition of protein-protein interactions using designed molecules
    • Wilson, A. J. (2009) Inhibition of protein-protein interactions using designed molecules. Chem. Soc. Rev. 38, 3289-3300
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 3289-3300
    • Wilson, A.J.1
  • 2
    • 84893018543 scopus 로고    scopus 로고
    • Protein-protein interactions as druggable targets: Recent technological advances
    • Higueruelo, A. P., Jubb, H., and Blundell, T. L. (2013) Protein-protein interactions as druggable targets: recent technological advances. Curr. Opin. Pharmacol. 13, 791-796
    • (2013) Curr. Opin. Pharmacol. , vol.13 , pp. 791-796
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, T.L.3
  • 3
    • 0036298185 scopus 로고    scopus 로고
    • Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophage
    • Melnyk, R. A., Partridge, A. W., and Deber, C. M. (2002) Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophage. J. Mol. Biol. 315, 63-72
    • (2002) J. Mol. Biol. , vol.315 , pp. 63-72
    • Melnyk, R.A.1    Partridge, A.W.2    Deber, C.M.3
  • 4
    • 84857652632 scopus 로고    scopus 로고
    • Transmembrane domains interactions within the membrane milieu: Principles, advances and challenges
    • Fink, A., Sal-Man, N., Gerber, D., and Shai, Y. (2012) Transmembrane domains interactions within the membrane milieu: principles, advances and challenges. Biochim. Biophys. Acta 1818, 974-983
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 974-983
    • Fink, A.1    Sal-Man, N.2    Gerber, D.3    Shai, Y.4
  • 5
    • 84857656752 scopus 로고    scopus 로고
    • Membrane protein misassembly in disease
    • Ng, D. P., Poulsen, B. E., and Deber, C. M. (2012) Membrane protein misassembly in disease. Biochim. Biophys. Acta 1818, 1115-1122
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1115-1122
    • Ng, D.P.1    Poulsen, B.E.2    Deber, C.M.3
  • 6
    • 34547857813 scopus 로고    scopus 로고
    • Aromatic and cation-π interactions enhance helix-helix association in a membrane environment
    • Johnson, R. M., Hecht, K., and Deber, C. M. (2007) Aromatic and cation-π interactions enhance helix-helix association in a membrane environment. Biochemistry 46, 9208-9214
    • (2007) Biochemistry , vol.46 , pp. 9208-9214
    • Johnson, R.M.1    Hecht, K.2    Deber, C.M.3
  • 7
    • 35649028687 scopus 로고    scopus 로고
    • Transmembrane segment IV contributes a functionally important interface for oligomerization of the Class II G protein-coupled secretin receptor
    • Harikumar, K. G., Pinon, D. I., and Miller, L. J. (2007) Transmembrane segment IV contributes a functionally important interface for oligomerization of the Class II G protein-coupled secretin receptor. J. Biol. Chem. 282, 30363-30372
    • (2007) J. Biol. Chem. , vol.282 , pp. 30363-30372
    • Harikumar, K.G.1    Pinon, D.I.2    Miller, L.J.3
  • 8
    • 84878765907 scopus 로고    scopus 로고
    • Rationally designed transmembrane peptide mimics of the multidrug transporter protein Cdr1 act as antagonists to selectively block drug efflux and chemosensitize azole-resistant clinical isolates of Candida albicans
    • Maurya, I. K., Thota, C. K., Verma, S. D., Sharma, J., Rawal, M. K., Ravikumar, B., Sen, S., Chauhan, N., Lynn, A. M., Chauhan, V. S., and Prasad, R. (2013) Rationally designed transmembrane peptide mimics of the multidrug transporter protein Cdr1 act as antagonists to selectively block drug efflux and chemosensitize azole-resistant clinical isolates of Candida albicans. J. Biol. Chem. 288, 16775-16787
    • (2013) J. Biol. Chem. , vol.288 , pp. 16775-16787
    • Maurya, I.K.1    Thota, C.K.2    Verma, S.D.3    Sharma, J.4    Rawal, M.K.5    Ravikumar, B.6    Sen, S.7    Chauhan, N.8    Lynn, A.M.9    Chauhan, V.S.10    Prasad, R.11
  • 9
    • 84855584802 scopus 로고    scopus 로고
    • Stapled peptides for intracellular drug targets
    • Verdine, G. L., and Hilinski, G. J. (2012) Stapled peptides for intracellular drug targets. Methods Enzymol. 503, 3-33
    • (2012) Methods Enzymol. , vol.503 , pp. 3-33
    • Verdine, G.L.1    Hilinski, G.J.2
  • 12
    • 84868131345 scopus 로고    scopus 로고
    • Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera
    • Chapuis, H., Slaninová, J., Bednárová, L., Monincová, L., Buděšínský, M., and Čeřovský, V. (2012) Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids 43, 2047-2058
    • (2012) Amino Acids , vol.43 , pp. 2047-2058
    • Chapuis, H.1    Slaninová, J.2    Bednárová, L.3    Monincová, L.4    Buděšínský, M.5    Čeřovský, V.6
  • 13
    • 84888866276 scopus 로고    scopus 로고
    • Truncated and constrained helical analogs of antimicrobial esculentin-2EM
    • Pham, T. K., Kim, D. H., Lee, B. J., and Kim, Y. W. (2013) Truncated and constrained helical analogs of antimicrobial esculentin-2EM. Bioorg. Med. Chem. Lett. 23, 6717-6720
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 6717-6720
    • Pham, T.K.1    Kim, D.H.2    Lee, B.J.3    Kim, Y.W.4
  • 14
    • 84901681947 scopus 로고    scopus 로고
    • Hydrocarbon-stapled peptides: Principles, practice, and progress
    • Walensky, L. D., and Bird, G. H. (2014) Hydrocarbon-stapled peptides: principles, practice, and progress. J. Med. Chem. 57, 6275-6288
    • (2014) J. Med. Chem. , vol.57 , pp. 6275-6288
    • Walensky, L.D.1    Bird, G.H.2
  • 15
    • 33747154459 scopus 로고    scopus 로고
    • Multidrug-resistance efflux pumps: Not just for resistance
    • Piddock, L. J. (2006) Multidrug-resistance efflux pumps: not just for resistance. Nat. Rev. Microbiol. 4, 629-636
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 629-636
    • Piddock, L.J.1
  • 16
    • 84870700313 scopus 로고    scopus 로고
    • New substrates on the block: Clinically relevant resistances for EmrE and homologues
    • Nasie, I., Steiner-Mordoch, S., and Schuldiner, S. (2012) New substrates on the block: clinically relevant resistances for EmrE and homologues. J. Bacteriol. 194, 6766-6770
    • (2012) J. Bacteriol. , vol.194 , pp. 6766-6770
    • Nasie, I.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 17
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz, Y., Steiner-Mordoch, S., Danieli, T., and Schuldiner, S. (2004) In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. U.S.A. 101, 1519-1524
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 18
    • 84868516360 scopus 로고    scopus 로고
    • Role of individual positive charges in the membrane orientation and activity of transporters of the small multidrug resistance family
    • Kolbusz, M. A., Slotboom, D. J., and Lolkema, J. S. (2012) Role of individual positive charges in the membrane orientation and activity of transporters of the small multidrug resistance family. Biochemistry 51, 8867-8876
    • (2012) Biochemistry , vol.51 , pp. 8867-8876
    • Kolbusz, M.A.1    Slotboom, D.J.2    Lolkema, J.S.3
  • 20
    • 33847611939 scopus 로고    scopus 로고
    • Emulating membrane protein evolution by rational design
    • Rapp, M., Seppälä, S., Granseth, E., and von Heijne, G. (2007) Emulating membrane protein evolution by rational design. Science 315, 1282-1284
    • (2007) Science , vol.315 , pp. 1282-1284
    • Rapp, M.1    Seppälä, S.2    Granseth, E.3    Von Heijne, G.4
  • 21
    • 77954070546 scopus 로고    scopus 로고
    • Control of membrane protein topology by a single C-terminal residue
    • Seppälä, S., Slusky, J. S., Lloris-Garcerá, P., Rapp, M., and von Heijne, G. (2010) Control of membrane protein topology by a single C-terminal residue. Science 328, 1698-1700
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppälä, S.1    Slusky, J.S.2    Lloris-Garcerá, P.3    Rapp, M.4    Von Heijne, G.5
  • 22
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth, T. R., and Schuldiner, S. (2000) A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19, 234-240
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 23
    • 45549084924 scopus 로고    scopus 로고
    • Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli
    • Elbaz, Y., Salomon, T., and Schuldiner, S. (2008) Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli. J. Biol. Chem. 283, 12276-12283
    • (2008) J. Biol. Chem. , vol.283 , pp. 12276-12283
    • Elbaz, Y.1    Salomon, T.2    Schuldiner, S.3
  • 24
    • 65649088665 scopus 로고    scopus 로고
    • The assembly motif of a bacterial small multidrug resistance protein
    • Poulsen, B. E., Rath, A., and Deber, C. M. (2009) The assembly motif of a bacterial small multidrug resistance protein. J. Biol. Chem. 284, 9870-9875
    • (2009) J. Biol. Chem. , vol.284 , pp. 9870-9875
    • Poulsen, B.E.1    Rath, A.2    Deber, C.M.3
  • 25
    • 84862544656 scopus 로고    scopus 로고
    • Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide
    • Poulsen, B. E., and Deber, C. M. (2012) Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide. Antimicrob. Agents Chemother. 56, 3911-3916
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 3911-3916
    • Poulsen, B.E.1    Deber, C.M.2
  • 26
    • 79958086652 scopus 로고    scopus 로고
    • Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis
    • Kim, Y. W., Grossmann, T. N., and Verdine, G. L. (2011) Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis. Nat. Protoc. 6, 761-771
    • (2011) Nat. Protoc. , vol.6 , pp. 761-771
    • Kim, Y.W.1    Grossmann, T.N.2    Verdine, G.L.3
  • 27
    • 84863230302 scopus 로고    scopus 로고
    • Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions
    • Yin, L. M., Edwards, M. A., Li, J., Yip, C. M., and Deber, C. M. (2012) Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions. J. Biol. Chem. 287, 7738-7745
    • (2012) J. Biol. Chem. , vol.287 , pp. 7738-7745
    • Yin, L.M.1    Edwards, M.A.2    Li, J.3    Yip, C.M.4    Deber, C.M.5
  • 28
    • 78650574596 scopus 로고    scopus 로고
    • Palmitoylated SDF1α shows increased resistance against proteolytic degradation in liver homogenates
    • Bellmann-Sickert, K., and Beck-Sickinger, A. G. (2011) Palmitoylated SDF1α shows increased resistance against proteolytic degradation in liver homogenates. ChemMedChem 6, 193-200
    • (2011) ChemMedChem , vol.6 , pp. 193-200
    • Bellmann-Sickert, K.1    Beck-Sickinger, A.G.2
  • 30
    • 0038146916 scopus 로고    scopus 로고
    • Characterization of an archaeal multidrug transporter with a unique amino acid composition
    • Ninio, S., and Schuldiner, S. (2003) Characterization of an archaeal multidrug transporter with a unique amino acid composition. J. Biol. Chem. 278, 12000-12005
    • (2003) J. Biol. Chem. , vol.278 , pp. 12000-12005
    • Ninio, S.1    Schuldiner, S.2
  • 32
    • 47749118037 scopus 로고    scopus 로고
    • Membrane interactions of designed cationic antimicrobial peptides: The two thresholds
    • Glukhov, E., Burrows, L. L., and Deber, C. M. (2008) Membrane interactions of designed cationic antimicrobial peptides: the two thresholds. Biopolymers 89, 360-371
    • (2008) Biopolymers , vol.89 , pp. 360-371
    • Glukhov, E.1    Burrows, L.L.2    Deber, C.M.3
  • 33
    • 50249116226 scopus 로고    scopus 로고
    • Small multidrug resistance proteins: A multidrug transporter family that continues to grow
    • Bay, D. C., Rommens, K. L., and Turner, R. J. (2008) Small multidrug resistance proteins: a multidrug transporter family that continues to grow. Biochim. Biophys. Acta 1778, 1814-1838
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1814-1838
    • Bay, D.C.1    Rommens, K.L.2    Turner, R.J.3
  • 35
    • 84882840901 scopus 로고    scopus 로고
    • Epidermal growth factor receptor targeting in cancer: A review of trends and strategies
    • Yewale, C., Baradia, D., Vhora, I., Patil, S., and Misra, A. (2013) Epidermal growth factor receptor targeting in cancer: a review of trends and strategies. Biomaterials 34, 8690-8707
    • (2013) Biomaterials , vol.34 , pp. 8690-8707
    • Yewale, C.1    Baradia, D.2    Vhora, I.3    Patil, S.4    Misra, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.