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Volumn 110, Issue 42, 2013, Pages

Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding

Author keywords

Atomic force microscopy; Major facilitator superfamily; Membrane transporter; Molecular interactions; Proton dependent oligopeptide transporter

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; DIPEPTIDE; PEPTIDE TRANSPORTER DTPA; PERMEASE; PROTEIN INHIBITOR; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 84885765846     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312959110     Document Type: Article
Times cited : (25)

References (71)
  • 1
    • 0029144324 scopus 로고
    • The PTR family: A new group of peptide transporters
    • Steiner H-Y, Naider F, Becker JM (1995) The PTR family: A new group of peptide transporters. Mol Microbiol 16(5): 825-834.
    • (1995) Mol Microbiol , vol.16 , Issue.5 , pp. 825-834
    • Steiner, H.-Y.1    Naider, F.2    Becker, J.M.3
  • 2
    • 33646720881 scopus 로고    scopus 로고
    • From bacteria to man: Archaic protondependent peptide transporters at work
    • Daniel H, Spanier B, Kottra G, Weitz D (2006) From bacteria to man: Archaic protondependent peptide transporters at work. Physiology (Bethesda) 21(2): 93-102.
    • (2006) Physiology (Bethesda) , vol.21 , Issue.2 , pp. 93-102
    • Daniel, H.1    Spanier, B.2    Kottra, G.3    Weitz, D.4
  • 3
    • 44949101288 scopus 로고    scopus 로고
    • DtpB (YhiP) and DtpA (TppB, YdgR) are prototypical protondependent peptide transporters of Escherichia coli
    • Harder D, et al. (2008) DtpB (YhiP) and DtpA (TppB, YdgR) are prototypical protondependent peptide transporters of Escherichia coli. FEBS J 275(13): 3290-3298.
    • (2008) FEBS J , vol.275 , Issue.13 , pp. 3290-3298
    • Harder, D.1
  • 4
    • 34047265483 scopus 로고    scopus 로고
    • Functional and structural characterization of a prokaryotic peptide transporter with features similar to mammalian PEPT1
    • Weitz D, et al. (2007) Functional and structural characterization of a prokaryotic peptide transporter with features similar to mammalian PEPT1. J Biol Chem 282(5): 2832-2839.
    • (2007) J Biol Chem , vol.282 , Issue.5 , pp. 2832-2839
    • Weitz, D.1
  • 5
    • 0028179387 scopus 로고
    • The di- and tripeptide transport protein of Lactococcus lactis. A new type of bacterial peptide transporter
    • Hagting A, Kunji ERS, Leenhouts KJ, Poolman B, Konings WN (1994) The di- and tripeptide transport protein of Lactococcus lactis. A new type of bacterial peptide transporter. J Biol Chem 269(15): 11391-11399.
    • (1994) J Biol Chem , vol.269 , Issue.15 , pp. 11391-11399
    • Hagting, A.1    Kunji, E.R.S.2    Leenhouts, K.J.3    Poolman, B.4    Konings, W.N.5
  • 6
    • 0030909215 scopus 로고    scopus 로고
    • Cloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus
    • Nakajima H, Hagting A, Kunji ERS, Poolman B, Konings WN (1997) Cloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus. Appl Environ Microbiol 63(6): 2213-2217.
    • (1997) Appl Environ Microbiol , vol.63 , Issue.6 , pp. 2213-2217
    • Nakajima, H.1    Hagting, A.2    Kunji, E.R.S.3    Poolman, B.4    Konings, W.N.5
  • 7
    • 0028115836 scopus 로고
    • Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene
    • Perry JR, Basrai MA, Steiner HY, Naider F, Becker JM (1994) Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene. Mol Cell Biol 14(1): 104-115.
    • (1994) Mol Cell Biol , vol.14 , Issue.1 , pp. 104-115
    • Perry, J.R.1    Basrai, M.A.2    Steiner, H.Y.3    Naider, F.4    Becker, J.M.5
  • 8
    • 33745807413 scopus 로고    scopus 로고
    • The renal type H+/peptide symporter PEPT2: Structure-affinity relationships
    • Biegel A, et al. (2006) The renal type H+/peptide symporter PEPT2: Structure-affinity relationships. Amino Acids 31(2): 137-156.
    • (2006) Amino Acids , vol.31 , Issue.2 , pp. 137-156
    • Biegel, A.1
  • 9
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • Daniel H, Kottra G (2004) The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch 447(5): 610-618.
    • (2004) Pflugers Arch , vol.447 , Issue.5 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 10
    • 78751604619 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2
    • Newstead S, et al. (2011) Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J 30(2): 417-426.
    • (2011) EMBO J , vol.30 , Issue.2 , pp. 417-426
    • Newstead, S.1
  • 11
    • 70349130738 scopus 로고    scopus 로고
    • Ligand binding analyses of the putative peptide transporter YjdL from E coli display a significant selectivity towards dipeptides
    • Ernst HA, et al. (2009) Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides. Biochem Biophys Res Commun 389(1): 112-116.
    • (2009) Biochem Biophys Res Commun , vol.389 , Issue.1 , pp. 112-116
    • Ernst, H.A.1
  • 12
    • 61449455434 scopus 로고    scopus 로고
    • The mammalian proton-coupled peptide cotransporter PepT1: Sitting on the transporter-channel fence?
    • Meredith D (2009) The mammalian proton-coupled peptide cotransporter PepT1: Sitting on the transporter-channel fence? Philos Trans R Soc Lond B Biol Sci 364(1514): 203-207.
    • (2009) Philos Trans R Soc Lond B Biol Sci , vol.364 , Issue.1514 , pp. 203-207
    • Meredith, D.1
  • 13
    • 0036710840 scopus 로고    scopus 로고
    • Mammalian peptide transporters as targets for drug delivery
    • Rubio-Aliaga I, Daniel H (2002) Mammalian peptide transporters as targets for drug delivery. Trends Pharmacol Sci 23(9): 434-440.
    • (2002) Trends Pharmacol Sci , vol.23 , Issue.9 , pp. 434-440
    • Rubio-Aliaga, I.1    Daniel, H.2
  • 14
    • 68149161029 scopus 로고    scopus 로고
    • Transport of drugs by proton-coupled peptide transporters: Pearls and pitfalls
    • Brandsch M (2009) Transport of drugs by proton-coupled peptide transporters: Pearls and pitfalls. Expert Opin Drug Metab Toxicol 5(8): 887-905.
    • (2009) Expert Opin Drug Metab Toxicol , vol.5 , Issue.8 , pp. 887-905
    • Brandsch, M.1
  • 15
    • 0028151656 scopus 로고
    • The POT family of transport proteins
    • Paulsen IT, Skurray RA (1994) The POT family of transport proteins. Trends Biochem Sci 19(10): 404.
    • (1994) Trends Biochem Sci , vol.19 , Issue.10 , pp. 404
    • Paulsen, I.T.1    Skurray, R.A.2
  • 16
    • 22544438743 scopus 로고    scopus 로고
    • Substrate preference is altered by mutations in the fifth transmembrane domain of Ptr2p, the di/tri-peptide transporter of Saccharomyces cerevisiae
    • Hauser M, Kauffman S, Naider F, Becker JM (2005) Substrate preference is altered by mutations in the fifth transmembrane domain of Ptr2p, the di/tri-peptide transporter of Saccharomyces cerevisiae. Mol Membr Biol 22(3): 215-227.
    • (2005) Mol Membr Biol , vol.22 , Issue.3 , pp. 215-227
    • Hauser, M.1    Kauffman, S.2    Naider, F.3    Becker, J.M.4
  • 17
    • 0032497316 scopus 로고    scopus 로고
    • Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton-coupled dipeptide transporter (hPepT1)
    • Yeung AK, et al. (1998) Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton-coupled dipeptide transporter (hPepT1). Biochem Biophys Res Commun 250(1): 103-107.
    • (1998) Biochem Biophys Res Commun , vol.250 , Issue.1 , pp. 103-107
    • Yeung, A.K.1
  • 18
    • 0030952745 scopus 로고    scopus 로고
    • Membrane topology of the diand tripeptide transport protein of Lactococcus lactis
    • Hagting A, vd Velde J, Poolman B, Konings WN (1997) Membrane topology of the diand tripeptide transport protein of Lactococcus lactis. Biochemistry 36(22): 6777-6785.
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6777-6785
    • Hagting, A.1    Vd Velde, J.2    Poolman, B.3    Konings, W.N.4
  • 19
    • 0032573036 scopus 로고    scopus 로고
    • Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions
    • Covitz K-MY, Amidon GL, Sadée W (1998) Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions. Biochemistry 37(43): 15214-15221.
    • (1998) Biochemistry , vol.37 , Issue.43 , pp. 15214-15221
    • K-My, C.1    Amidon, G.L.2    Sadée, W.3
  • 20
    • 84865237281 scopus 로고    scopus 로고
    • Alternating access mechanism in the POT family of oligopeptide transporters
    • Solcan N, et al. (2012) Alternating access mechanism in the POT family of oligopeptide transporters. EMBO J 31(16): 3411-3421.
    • (2012) EMBO J , vol.31 , Issue.16 , pp. 3411-3421
    • Solcan, N.1
  • 21
    • 84879895875 scopus 로고    scopus 로고
    • Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT
    • Doki S, et al. (2013) Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT. Proc Natl Acad Sci USA 110(28): 11343-11348.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.28 , pp. 11343-11348
    • Doki, S.1
  • 22
    • 84883489166 scopus 로고    scopus 로고
    • Structural insights into substrate recognition in protondependent oligopeptide transporters
    • Guettou F, et al. (2013) Structural insights into substrate recognition in protondependent oligopeptide transporters. EMBO Rep 14(9): 804-810.
    • (2013) EMBO Rep , vol.14 , Issue.9 , pp. 804-810
    • Guettou, F.1
  • 23
    • 79959553434 scopus 로고    scopus 로고
    • Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues
    • Malle E, et al. (2011) Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues. J Biol Chem 286(26): 23121-23131.
    • (2011) J Biol Chem , vol.286 , Issue.26 , pp. 23121-23131
    • Malle, E.1
  • 24
    • 84863351083 scopus 로고    scopus 로고
    • Functional investigation of conserved membrane-embedded glutamate residues in the proton-coupled peptide transporter YjdL
    • Jensen JM, et al. (2012) Functional investigation of conserved membrane-embedded glutamate residues in the proton-coupled peptide transporter YjdL. Protein Pept Lett 19(3): 282-287.
    • (2012) Protein Pept Lett , vol.19 , Issue.3 , pp. 282-287
    • Jensen, J.M.1
  • 25
    • 84867704017 scopus 로고    scopus 로고
    • Probing the putative active site of YjdL: An unusual proton-coupled oligopeptide transporter from E coli
    • Jensen JM, Ismat F, Szakonyi G, Rahman M, Mirza O (2012) Probing the putative active site of YjdL: An unusual proton-coupled oligopeptide transporter from E. coli. PLoS ONE 7(10):e47780.
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Jensen, J.M.1    Ismat, F.2    Szakonyi, G.3    Rahman, M.4    Mirza, O.5
  • 26
    • 84866266592 scopus 로고    scopus 로고
    • Biophysical characterization of the proton-coupled oligopeptide transporter YjdL
    • Jensen JM, et al. (2012) Biophysical characterization of the proton-coupled oligopeptide transporter YjdL. Peptides 38(1): 89-93.
    • (2012) Peptides , vol.38 , Issue.1 , pp. 89-93
    • Jensen, J.M.1
  • 27
    • 70449524304 scopus 로고    scopus 로고
    • Projection structure of DtpD (YbgH), a prokaryotic member of the peptide transporter family
    • Casagrande F, et al. (2009) Projection structure of DtpD (YbgH), a prokaryotic member of the peptide transporter family. J Mol Biol 394(4): 708-717.
    • (2009) J Mol Biol , vol.394 , Issue.4 , pp. 708-717
    • Casagrande, F.1
  • 28
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • Kedrov A, Janovjak H, Sapra KT, Müller DJ (2007) Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu Rev Biophys Biomol Struct 36(1): 233-260.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , Issue.1 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Müller, D.J.4
  • 29
    • 50649125304 scopus 로고    scopus 로고
    • Structure and mechanics of membrane proteins
    • Engel A, Gaub HE (2008) Structure and mechanics of membrane proteins. Annu Rev Biochem 77(1): 127-148.
    • (2008) Annu Rev Biochem , vol.77 , Issue.1 , pp. 127-148
    • Engel, A.1    Gaub, H.E.2
  • 30
    • 23744506838 scopus 로고    scopus 로고
    • Locating ligand binding and activation of a single antiporter
    • Kedrov A, Krieg M, Ziegler C, Kuhlbrandt W, Muller DJ (2005) Locating ligand binding and activation of a single antiporter. EMBO Rep 6(7): 668-674.
    • (2005) EMBO Rep , vol.6 , Issue.7 , pp. 668-674
    • Kedrov, A.1    Krieg, M.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 31
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating ligand and inhibitor interactions of a single antiporter
    • Kedrov A, Ziegler C, Muller DJ (2006) Differentiating ligand and inhibitor interactions of a single antiporter. J Mol Biol 362(5): 925-932.
    • (2006) J Mol Biol , vol.362 , Issue.5 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.J.3
  • 32
    • 73449133713 scopus 로고    scopus 로고
    • Probing the interactions of carboxy-atractyloside and atractyloside with the yeast mitochondrial ADP/ATP carrier
    • Kedrov A, et al. (2010) Probing the interactions of carboxy-atractyloside and atractyloside with the yeast mitochondrial ADP/ATP carrier. Structure 18(1): 39-46.
    • (2010) Structure , vol.18 , Issue.1 , pp. 39-46
    • Kedrov, A.1
  • 33
    • 80055077494 scopus 로고    scopus 로고
    • Locating an extracellular K+- dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP
    • Ge L, Perez C, Waclawska I, Ziegler C, Muller DJ (2011) Locating an extracellular K+- dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP. Proc Natl Acad Sci USA 108(43):E890-E898.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.43
    • Ge, L.1    Perez, C.2    Waclawska, I.3    Ziegler, C.4    Muller, D.J.5
  • 34
    • 84864853215 scopus 로고    scopus 로고
    • Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor
    • Zocher M, Fung JJ, Kobilka BK, Müller DJ (2012) Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor. Structure 20(8): 1391-1402.
    • (2012) Structure , vol.20 , Issue.8 , pp. 1391-1402
    • Zocher, M.1    Fung, J.J.2    Kobilka, B.K.3    Müller, D.J.4
  • 35
    • 48149093168 scopus 로고    scopus 로고
    • Transducer binding establishes localized interactions to tune sensory rhodopsin II
    • Cisneros DA, et al. (2008) Transducer binding establishes localized interactions to tune sensory rhodopsin II. Structure 16(8): 1206-1213.
    • (2008) Structure , vol.16 , Issue.8 , pp. 1206-1213
    • Cisneros, D.A.1
  • 36
    • 39049092605 scopus 로고    scopus 로고
    • Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways
    • Sapra KT, Balasubramanian GP, Labudde D, Bowie JU, Muller DJ (2008) Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways. J Mol Biol 376(4): 1076-1090.
    • (2008) J Mol Biol , vol.376 , Issue.4 , pp. 1076-1090
    • Sapra, K.T.1    Balasubramanian, G.P.2    Labudde, D.3    Bowie, J.U.4    Muller, D.J.5
  • 37
    • 48649083203 scopus 로고    scopus 로고
    • Role of extracellular glutamic acids in the stability and energy landscape of bacteriorhodopsin
    • Sapra KT, Doehner J, Renugopalakrishnan V, Padrós E, Muller DJ (2008) Role of extracellular glutamic acids in the stability and energy landscape of bacteriorhodopsin. Biophys J 95(7): 3407-3418.
    • (2008) Biophys J , vol.95 , Issue.7 , pp. 3407-3418
    • Sapra, K.T.1    Doehner, J.2    Renugopalakrishnan, V.3    Padrós, E.4    Muller, D.J.5
  • 38
    • 84862690475 scopus 로고    scopus 로고
    • Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness
    • Kawamura S, Colozo AT, Ge L, Müller DJ, Park PS (2012) Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness. J Biol Chem 287(26): 21826-21835.
    • (2012) J Biol Chem , vol.287 , Issue.26 , pp. 21826-21835
    • Kawamura, S.1    Colozo, A.T.2    Ge, L.3    Müller, D.J.4    Park, P.S.5
  • 39
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra KT, Besir H, Oesterhelt D, Muller DJ (2006) Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J Mol Biol 355(4): 640-650.
    • (2006) J Mol Biol , vol.355 , Issue.4 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 40
    • 84870896671 scopus 로고    scopus 로고
    • Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor
    • Zocher M, Zhang C, Rasmussen SG, Kobilka BK, Müller DJ (2012) Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor. Proc Natl Acad Sci USA 109(50):E3463-E3472.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.50
    • Zocher, M.1    Zhang, C.2    Rasmussen, S.G.3    Kobilka, B.K.4    Müller, D.J.5
  • 41
    • 0347600965 scopus 로고    scopus 로고
    • Analysis of the transport properties of side chain modified dipeptides at the mammalian peptide transporter PEPT1
    • Knütter I, et al. (2004) Analysis of the transport properties of side chain modified dipeptides at the mammalian peptide transporter PEPT1. Eur J Pharm Sci 21(1): 61-67.
    • (2004) Eur J Pharm Sci , vol.21 , Issue.1 , pp. 61-67
    • Knütter, I.1
  • 42
    • 42549117180 scopus 로고    scopus 로고
    • Pharmaceutical and pharmacological importance of peptide transporters
    • Brandsch M, Knütter I, Bosse-Doenecke E (2008) Pharmaceutical and pharmacological importance of peptide transporters. J Pharm Pharmacol 60(5): 543-585.
    • (2008) J Pharm Pharmacol , vol.60 , Issue.5 , pp. 543-585
    • Brandsch, M.1    Knütter, I.2    Bosse-Doenecke, E.3
  • 43
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller DJ, Amrein M, Engel A (1997) Adsorption of biological molecules to a solid support for scanning probe microscopy. J Struct Biol 119(2): 172-188.
    • (1997) J Struct Biol , vol.119 , Issue.2 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 44
    • 79961064868 scopus 로고    scopus 로고
    • High-resolution atomic force microscopy and spectroscopy of native membrane proteins
    • Bippes CA, Muller DJ (2011) High-resolution atomic force microscopy and spectroscopy of native membrane proteins. Rep Prog Phys 74(8): 086601.
    • (2011) Rep Prog Phys , vol.74 , Issue.8 , pp. 086601
    • Bippes, C.A.1    Muller, D.J.2
  • 45
    • 0028071373 scopus 로고
    • Entropic elasticity of lambdaphage DNA
    • Bustamante C, Marko JF, Siggia ED, Smith S (1994) Entropic elasticity of lambdaphage DNA. Science 265(5178): 1599-1600.
    • (1994) Science , vol.265 , Issue.5178 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 46
    • 84874929344 scopus 로고    scopus 로고
    • Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin
    • Kawamura S, et al. (2013) Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin. Structure 21(3): 426-437.
    • (2013) Structure , vol.21 , Issue.3 , pp. 426-437
    • Kawamura, S.1
  • 47
    • 43649083578 scopus 로고    scopus 로고
    • From valleys to ridges: Exploring the dynamic energy landscape of single membrane proteins
    • Janovjak H, Sapra KT, Kedrov A, Müller DJ (2008) From valleys to ridges: Exploring the dynamic energy landscape of single membrane proteins. ChemPhysChem 9(7): 954-966.
    • (2008) ChemPhysChem , vol.9 , Issue.7 , pp. 954-966
    • Janovjak, H.1    Sapra, K.T.2    Kedrov, A.3    Müller, D.J.4
  • 48
    • 0344406716 scopus 로고    scopus 로고
    • Reliability measures for membrane protein topology prediction algorithms
    • Melén K, Krogh A, von Heijne G (2003) Reliability measures for membrane protein topology prediction algorithms. J Mol Biol 327(3): 735-744.
    • (2003) J Mol Biol , vol.327 , Issue.3 , pp. 735-744
    • Melén, K.1    Krogh, A.2    Von Heijne, G.3
  • 49
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy
    • Müller DJ, et al. (2002) Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy. Biophys J 83(6): 3578-3588.
    • (2002) Biophys J , vol.83 , Issue.6 , pp. 3578-3588
    • Müller, D.J.1
  • 50
    • 33644844356 scopus 로고    scopus 로고
    • Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM
    • Kessler M, Gaub HE (2006) Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM. Structure 14(3): 521-527.
    • (2006) Structure , vol.14 , Issue.3 , pp. 521-527
    • Kessler, M.1    Gaub, H.E.2
  • 51
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov A, Ziegler C, Janovjak H, Kühlbrandt W, Müller DJ (2004) Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J Mol Biol 340(5): 1143-1152.
    • (2004) J Mol Biol , vol.340 , Issue.5 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kühlbrandt, W.4    Müller, D.J.5
  • 52
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC (1999) Membrane protein folding and stability: Physical principles. Annu Rev Biophys Biomol Struct 28(1): 319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , Issue.1 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 53
    • 0042508741 scopus 로고    scopus 로고
    • Pulling geometry defines the mechanical resistance of a beta-sheet protein
    • Brockwell DJ, et al. (2003) Pulling geometry defines the mechanical resistance of a beta-sheet protein. Nat Struct Biol 10(9): 731-737.
    • (2003) Nat Struct Biol , vol.10 , Issue.9 , pp. 731-737
    • Brockwell, D.J.1
  • 54
    • 84881476212 scopus 로고    scopus 로고
    • Mechanistic explanation of different unfolding behaviors observed for transmembrane and soluble beta-barrel proteins
    • Hensen U, Müller DJ (2013) Mechanistic explanation of different unfolding behaviors observed for transmembrane and soluble beta-barrel proteins. Structure 21(8): 1317-1324.
    • (2013) Structure , vol.21 , Issue.8 , pp. 1317-1324
    • Hensen, U.1    Müller, D.J.2
  • 55
    • 0031037730 scopus 로고    scopus 로고
    • Identification of the histidyl residue obligatory for the catalytic activity of the human H+/peptide cotransporters PEPT1 and PEPT2
    • Fei Y-J, et al. (1997) Identification of the histidyl residue obligatory for the catalytic activity of the human H+/peptide cotransporters PEPT1 and PEPT2. Biochemistry 36(2): 452-460.
    • (1997) Biochemistry , vol.36 , Issue.2 , pp. 452-460
    • Fei, Y.-J.1
  • 56
    • 0030463324 scopus 로고    scopus 로고
    • Functional analysis of a chimeric mammalian peptide transporter derived from the intestinal and renal isoforms
    • Döring F, et al. (1996) Functional analysis of a chimeric mammalian peptide transporter derived from the intestinal and renal isoforms. J Physiol 497(Pt 3): 773-779.
    • (1996) J Physiol , vol.497 , Issue.PART 3 , pp. 773-779
    • Döring, F.1
  • 57
    • 0030607260 scopus 로고    scopus 로고
    • Identification of the histidine residues involved in substrate recognition by a rat H+/peptide cotransporter, PEPT1
    • Terada T, Saito H, Mukai M, Inui KI (1996) Identification of the histidine residues involved in substrate recognition by a rat H+/peptide cotransporter, PEPT1. FEBS Lett 394(2): 196-200.
    • (1996) FEBS Lett , vol.394 , Issue.2 , pp. 196-200
    • Terada, T.1    Saito, H.2    Mukai, M.3    Inui, K.I.4
  • 58
    • 0033630953 scopus 로고    scopus 로고
    • N-terminal halves of rat H+/peptide transporters are responsible for their substrate recognition
    • Terada T, Saito H, Sawada K, Hashimoto Y, Inui KI (2000) N-terminal halves of rat H+/peptide transporters are responsible for their substrate recognition. Pharm Res 17(1): 15-20.
    • (2000) Pharm Res , vol.17 , Issue.1 , pp. 15-20
    • Terada, T.1    Saito, H.2    Sawada, K.3    Hashimoto, Y.4    Inui, K.I.5
  • 59
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301(5633): 610-615.
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1
  • 60
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y, He X, Szewczyk P, Nguyen T, Chang G (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312(5774): 741-744.
    • (2006) Science , vol.312 , Issue.5774 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 61
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • Dang S, et al. (2010) Structure of a fucose transporter in an outward-open conformation. Nature 467(7316): 734-738.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 734-738
    • Dang, S.1
  • 62
    • 41649112580 scopus 로고    scopus 로고
    • Opening and closing of the periplasmic gate in lactose permease
    • Zhou Y, Guan L, Freites JA, Kaback HR (2008) Opening and closing of the periplasmic gate in lactose permease. Proc Natl Acad Sci USA 105(10): 3774-3778.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3774-3778
    • Zhou, Y.1    Guan, L.2    Freites, J.A.3    Kaback, H.R.4
  • 63
    • 60749115991 scopus 로고    scopus 로고
    • Clogging the periplasmic pathway in LacY
    • Nie Y, Zhou Y, Kaback HR (2009) Clogging the periplasmic pathway in LacY. Biochemistry 48(4): 738-743.
    • (2009) Biochemistry , vol.48 , Issue.4 , pp. 738-743
    • Nie, Y.1    Zhou, Y.2    Kaback, H.R.3
  • 66
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O (1966) Simple allosteric model for membrane pumps. Nature 211(5052): 969-970.
    • (1966) Nature , vol.211 , Issue.5052 , pp. 969-970
    • Jardetzky, O.1
  • 67
    • 51349110046 scopus 로고    scopus 로고
    • Fully automated single-molecule force spectroscopy for screening applications
    • Struckmeier J, et al. (2008) Fully automated single-molecule force spectroscopy for screening applications. Nanotechnology 19(38): 384020.
    • (2008) Nanotechnology , vol.19 , Issue.38 , pp. 384020
    • Struckmeier, J.1
  • 68
    • 51349128150 scopus 로고    scopus 로고
    • High-throughput single-molecule force spectroscopy for membrane proteins
    • Bosshart PD, et al. (2008) High-throughput single-molecule force spectroscopy for membrane proteins. Nanotechnology 19(38): 384014.
    • (2008) Nanotechnology , vol.19 , Issue.38 , pp. 384014
    • Bosshart, P.D.1
  • 69
    • 0034698003 scopus 로고    scopus 로고
    • Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence
    • Fotiadis D, et al. (2000) Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J Mol Biol 300(4): 779-789.
    • (2000) J Mol Biol , vol.300 , Issue.4 , pp. 779-789
    • Fotiadis, D.1
  • 70
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt H-J, Jaschke M (1995) Calculation of thermal noise in atomic force microscopy. Nanotechnology 6(1): 1-7.
    • (1995) Nanotechnology , vol.6 , Issue.1 , pp. 1-7
    • Butt, H.-J.1    Jaschke, M.2
  • 71
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276(5315): 1109-1112.
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5


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