메뉴 건너뛰기




Volumn 3, Issue 4, 2006, Pages 399-408

Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics

Author keywords

Mass spectrometry; Molecular modeling; Photoaffinity labeling; Photolabeling; Protein drug interactions; Protein peptide interactions; Stoichiometry; Structural proteomics; Structure based drug design

Indexed keywords

BENZOPHENONE; LIGAND; OLIGONUCLEOTIDE;

EID: 33747190864     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.3.4.399     Document Type: Review
Times cited : (67)

References (46)
  • 1
    • 73849163777 scopus 로고
    • The photolysis of diazoacetylchymotrypsin
    • Sing A, Thornton ER, Westheimer FH. The photolysis of diazoacetylchymotrypsin. J. Biol. Chem. 237(9), PC3006-PC3008 (1962). • Earliest report of the use of photoaffinity chemistry in biochemistry.
    • (1962) J. Biol. Chem. , vol.237 , Issue.9
    • Sing, A.1    Thornton, E.R.2    Westheimer, F.H.3
  • 2
    • 0028808348 scopus 로고
    • Chemical reagents in photoaffinity labeling
    • Fleming SA. Chemical reagents in photoaffinity labeling. Tetrahedron 51(46), 12479-12520 (1995).
    • (1995) Tetrahedron , vol.51 , Issue.46 , pp. 12479-12520
    • Fleming, S.A.1
  • 3
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner J. New photolabeling and crosslinking methods. Ann. Rev. Biochem. 62, 483-514 (1993).
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 483-514
    • Brunner, J.1
  • 4
    • 0033951038 scopus 로고    scopus 로고
    • Using photolabile ligands in drug discovery and development
    • Dormán G, Prestwich GD. Using photolabile ligands in drug discovery and development. Trends Biotechnol. 18, 64-77 (2000). •• Focuses on how photoaffinity labeling techniques are used in drug discovery, but does not delve deeply into mass spectrometry.
    • (2000) Trends Biotechnol. , vol.18 , pp. 64-77
    • Dormán, G.1    Prestwich, G.D.2
  • 5
    • 0030959062 scopus 로고    scopus 로고
    • Comparison of the photochemical behavior of four different photo-activatable probes
    • Weber PJ, Beck-Sickinger AG. Comparison of the photochemical behavior of four different photo-activatable probes. J. Peptide Res. 49(5), 375-383 (1997). • Useful information for those researchers contemplating the use of photoaffinity techniques.
    • (1997) J. Peptide Res. , vol.49 , Issue.5 , pp. 375-383
    • Weber, P.J.1    Beck-Sickinger, A.G.2
  • 6
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dormán G, Prestwich GD. Benzophenone photophores in biochemistry. Biochem. 33(19), 5661-5673 (1994).
    • (1994) Biochem. , vol.33 , Issue.19 , pp. 5661-5673
    • Dormán, G.1    Prestwich, G.D.2
  • 7
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mader AW, Richmond RK et al. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3
  • 8
    • 0035901537 scopus 로고    scopus 로고
    • The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR
    • van Aalten DM, DiRusso CC, Knudsen J. The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR. EMBO J. 20, 2041-2050 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2041-2050
    • Van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3
  • 9
    • 0036882288 scopus 로고    scopus 로고
    • Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry
    • Steen H, Jensen ON. Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry. Mass Spect. Rev. 21, 163-182 (2002).
    • (2002) Mass Spect. Rev. , vol.21 , pp. 163-182
    • Steen, H.1    Jensen, O.N.2
  • 10
    • 0032482990 scopus 로고    scopus 로고
    • RNA-binding site in T7 RNA polymerase
    • Sastry S, Ross BM. RNA-binding site in T7 RNA polymerase. Proc. Natl Acad. Sci. USA 95, 9111-9116 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9111-9116
    • Sastry, S.1    Ross, B.M.2
  • 11
    • 0030979415 scopus 로고    scopus 로고
    • Photocross-linking of nucleic acids to associated proteins
    • Meisenheimer K, Koch T. Photocross-linking of nucleic acids to associated proteins. Crit. Rev. Biochem. Mol. Biol. 32, 101-140 (1997).
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 101-140
    • Meisenheimer, K.1    Koch, T.2
  • 12
    • 0033435101 scopus 로고    scopus 로고
    • Mass spectral characterization of a protein-nucleic acid photocrosslink
    • Golden MC, Resing KA, Collins BD et al. Mass spectral characterization of a protein-nucleic acid photocrosslink. Protein Sci. 8, 2806-2812 (1999).
    • (1999) Protein Sci. , vol.8 , pp. 2806-2812
    • Golden, M.C.1    Resing, K.A.2    Collins, B.D.3
  • 13
    • 0034812113 scopus 로고    scopus 로고
    • Mass spectrometric analysis of a UV-cross-linked protein-DNA complex: Tryptophans 54 and 88 of E. coli SSB cross-link to DNA
    • Steen H, Petersen J, Mann M et al. Mass spectrometric analysis of a UV-cross-linked protein-DNA complex: tryptophans 54 and 88 of E. coli SSB cross-link to DNA. Protein Sci. 10, 1989-2001 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 1989-2001
    • Steen, H.1    Petersen, J.2    Mann, M.3
  • 14
    • 19444371218 scopus 로고    scopus 로고
    • A novel strategy for the identification of protein-DNA contacts by photocrosslinking and mass spectrometry
    • Geyer H, Geyer R, Pingoud V. A novel strategy for the identification of protein-DNA contacts by photocrosslinking and mass spectrometry. Nucleic Acids Res. 32(16), e132 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , Issue.16
    • Geyer, H.1    Geyer, R.2    Pingoud, V.3
  • 15
    • 27744567556 scopus 로고    scopus 로고
    • Interactome: Gateway into systems biology
    • Cusick ME, Klitgord N, Vidal M et al. Interactome: gateway into systems biology. Human Mol. Gen. 14(2), R171-R181 (2005). • Highlights the importance of methods such as photoaffinity labeling and mass spectrometry that can enhance our ability to define biomolecule interactions on the molecular level.
    • (2005) Human Mol. Gen. , vol.14 , Issue.2
    • Cusick, M.E.1    Klitgord, N.2    Vidal, M.3
  • 16
    • 0036514084 scopus 로고    scopus 로고
    • Photoaffinity labeling in drug discovery and developments: Chemical gateway for entering proteomic frontier
    • Hatanaka Y, Sadakane Y. Photoaffinity labeling in drug discovery and developments: chemical gateway for entering proteomic frontier. Curr. Topics Med. Chem. 2, 271-288 (2002).
    • (2002) Curr. Topics Med. Chem. , vol.2 , pp. 271-288
    • Hatanaka, Y.1    Sadakane, Y.2
  • 17
    • 0037259060 scopus 로고    scopus 로고
    • Methods for the study of protein-protein interactions in cancer cell biology
    • Price D, Park I, Avraham H. Methods for the study of protein-protein interactions in cancer cell biology. Methods Mol. Biol. 218, 255-267 (2003).
    • (2003) Methods Mol. Biol. , vol.218 , pp. 255-267
    • Price, D.1    Park, I.2    Avraham, H.3
  • 18
    • 16544376028 scopus 로고    scopus 로고
    • Characterization of peptide-protein interactions using photoaffinity labeling and LC/MS
    • Jahn O, Eckart K, Tezval H et al. Characterization of peptide-protein interactions using photoaffinity labeling and LC/MS. Anal. BioAnal. Chem. 378, 1031-1036 (2004).
    • (2004) Anal. BioAnal. Chem. , vol.378 , pp. 1031-1036
    • Jahn, O.1    Eckart, K.2    Tezval, H.3
  • 19
    • 0032562690 scopus 로고    scopus 로고
    • Identification of a ligand binding site in the human neutrophil formyl peptide receptor using a site-specific fluorescent photoaffinity label and mass spectrometry
    • Mills JS, Miettinen HM, Barnidge D et al. Identification of a ligand binding site in the human neutrophil formyl peptide receptor using a site-specific fluorescent photoaffinity label and mass spectrometry. J. Biol. Chem. 273(17), 10428-10435 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.17 , pp. 10428-10435
    • Mills, J.S.1    Miettinen, H.M.2    Barnidge, D.3
  • 20
    • 0029842449 scopus 로고    scopus 로고
    • The use of photolabelled peptides to localize the substance-P-binding site in the human neurokinin-1 tachykinin receptor
    • Girault S, Sagan S, Bolbach G et al. The use of photolabelled peptides to localize the substance-P-binding site in the human neurokinin-1 tachykinin receptor. Eur. J. Biochem. 240, 215-222 (1996).
    • (1996) Eur. J. Biochem. , vol.240 , pp. 215-222
    • Girault, S.1    Sagan, S.2    Bolbach, G.3
  • 21
    • 0032564309 scopus 로고    scopus 로고
    • Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site
    • Ploug M. Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site. Biochemistry 37, 16494-16505 (1998).
    • (1998) Biochemistry , vol.37 , pp. 16494-16505
    • Ploug, M.1
  • 22
    • 0035943635 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a soluble form of the first extracellular domain of the human type 1 corticotropin realeasing factor receptor
    • Perrin MH, Fischer WH, Kunitake KS et al. Expression, purification, and characterization of a soluble form of the first extracellular domain of the human type 1 corticotropin realeasing factor receptor. J. Biol. Chem. 276(34), 31528-31534 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 31528-31534
    • Perrin, M.H.1    Fischer, W.H.2    Kunitake, K.S.3
  • 23
    • 0037126034 scopus 로고    scopus 로고
    • The binding protein of corticotrophin-releasing factor: Ligand-binding site and subunit structure
    • Jahn O, Eckart K, Brauns O et al. The binding protein of corticotrophin-releasing factor: ligand-binding site and subunit structure. Proc. Natl Acad. Sci. USA 99(19), 12055-12060 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.19 , pp. 12055-12060
    • Jahn, O.1    Eckart, K.2    Brauns, O.3
  • 24
    • 0041706085 scopus 로고    scopus 로고
    • Tandem mass spectrometric characterization of branched peptides derived from photoaffinity labeling
    • Jahn O, Tezval H, Spiess J et al. Tandem mass spectrometric characterization of branched peptides derived from photoaffinity labeling. Int. J. Mass Spec. 228, 527-540 (2003).
    • (2003) Int. J. Mass Spec. , vol.228 , pp. 527-540
    • Jahn, O.1    Tezval, H.2    Spiess, J.3
  • 25
    • 0038695000 scopus 로고    scopus 로고
    • Met174 side chain is the site of photoinsertion of a substance P competitive peptide antagonist photoreactive in position 8
    • Sachon E, Bolbach G, Lavielle S et al. Met174 side chain is the site of photoinsertion of a substance P competitive peptide antagonist photoreactive in position 8. FEBS Lett. 544, 45-49 (2003).
    • (2003) FEBS Lett. , vol.544 , pp. 45-49
    • Sachon, E.1    Bolbach, G.2    Lavielle, S.3
  • 26
    • 0345168214 scopus 로고    scopus 로고
    • Isotope and affinity tags in photoreactive substance P analogues to identify the covalent linkage within the NK-1 receptor by MALDI-TOF analysis
    • Sachon E, Tasseau O, Lavielle S et al. Isotope and affinity tags in photoreactive substance P analogues to identify the covalent linkage within the NK-1 receptor by MALDI-TOF analysis. Anal. Chem. 75, 6536-6543 (2003).
    • (2003) Anal. Chem. , vol.75 , pp. 6536-6543
    • Sachon, E.1    Tasseau, O.2    Lavielle, S.3
  • 27
    • 0037307837 scopus 로고    scopus 로고
    • Stable isotope-coded proteomic mass spectrometry
    • Goshe MB, Smith RD. Stable isotope-coded proteomic mass spectrometry. Curr. Opin. Biotech. 14, 101-109 (2003).
    • (2003) Curr. Opin. Biotech. , vol.14 , pp. 101-109
    • Goshe, M.B.1    Smith, R.D.2
  • 28
    • 0037084124 scopus 로고    scopus 로고
    • The use of multiple ion chromatograms in on-line HPLC-MS for the characterization of post-translational and chemical modifications of proteins
    • Jahn O, Hofmann B, Brauns O et al. The use of multiple ion chromatograms in on-line HPLC-MS for the characterization of post-translational and chemical modifications of proteins. Int. J. Mass Spec. 214, 37-51 (2002).
    • (2002) Int. J. Mass Spec. , vol.214 , pp. 37-51
    • Jahn, O.1    Hofmann, B.2    Brauns, O.3
  • 29
    • 0032544581 scopus 로고    scopus 로고
    • Localization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4
    • Olcott MC, Andersson J, Sjöberg B-M. Localization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4. J. Biol. Chem. 273(38), 24853-24860 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.38 , pp. 24853-24860
    • Olcott, M.C.1    Andersson, J.2    Sjöberg, B.-M.3
  • 30
    • 0035831545 scopus 로고    scopus 로고
    • Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure
    • Kramer W, Sauber K, Baringhaus K-H et al. Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J. Biol. Chem. 276(10), 7291-7301 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.10 , pp. 7291-7301
    • Kramer, W.1    Sauber, K.2    Baringhaus, K.-H.3
  • 31
    • 4644248833 scopus 로고    scopus 로고
    • + glucose cotransporter SGLT1 contains a binding site for alkyl glucosides
    • + glucose cotransporter SGLT1 contains a binding site for alkyl glucosides. Biochem. 43, 10944-10951 (2004).
    • (2004) Biochem. , vol.43 , pp. 10944-10951
    • Raja, M.M.1    Kipp, H.2    Kinne, R.K.H.3
  • 32
    • 0034816320 scopus 로고    scopus 로고
    • Binding site elucidation of hydantoin-based antagonists of LFA-1 using multidisciplinary technologies: Evidence for the allosteric inhibition of a protein-protein interaction
    • Last-Barney K, Davidson W, Cardozo M et al. Binding site elucidation of hydantoin-based antagonists of LFA-1 using multidisciplinary technologies: evidence for the allosteric inhibition of a protein-protein interaction. J. Am. Chem. Soc. 123, 5643-5650 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5643-5650
    • Last-Barney, K.1    Davidson, W.2    Cardozo, M.3
  • 33
    • 8444221564 scopus 로고    scopus 로고
    • Using mass spectrometry to study the photo-affinity labeling of protein tyrosine phosphatase 1B
    • LeRiche T, Skorey K, Roy P et al. Using mass spectrometry to study the photo-affinity labeling of protein tyrosine phosphatase 1B. Int. J. Mass Spec. 238, 99-106 (2004).
    • (2004) Int. J. Mass Spec. , vol.238 , pp. 99-106
    • LeRiche, T.1    Skorey, K.2    Roy, P.3
  • 34
    • 3042639764 scopus 로고    scopus 로고
    • Identification of CRALBP ligand interactions by photoaffinity labeling, hydrogen/deuterium exchange, and structural modeling
    • Wu Z, Hasan A, Liu T, Teller D, Crabb J. Identification of CRALBP ligand interactions by photoaffinity labeling, hydrogen/deuterium exchange, and structural modeling. J. Biol. Chem. 279 (26), 27357-27364 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.26 , pp. 27357-27364
    • Wu, Z.1    Hasan, A.2    Liu, T.3    Teller, D.4    Crabb, J.5
  • 35
    • 13544275575 scopus 로고    scopus 로고
    • Fluorescent photoaffinity labeling of cytochrome P450 3A4 by lapechenole: Identification of modification sites by mass spectrometry
    • Wen B, Doneanu CE, Gartner CA, Roberts AG, Atkins WM, Nelson SD. Fluorescent photoaffinity labeling of cytochrome P450 3A4 by lapechenole: identification of modification sites by mass spectrometry. Biochem. 44, 1833-1845 (2005).
    • (2005) Biochem. , vol.44 , pp. 1833-1845
    • Wen, B.1    Doneanu, C.E.2    Gartner, C.A.3    Roberts, A.G.4    Atkins, W.M.5    Nelson, S.D.6
  • 36
    • 0036265334 scopus 로고    scopus 로고
    • Characterization of the dexniguldipine binding site in the multidrug resistance-related transport protein P-glycoprotein by photoaffinity labeling and mass spectrometry
    • Borchers C, Boer R, Klemm K et al. Characterization of the dexniguldipine binding site in the multidrug resistance-related transport protein P-glycoprotein by photoaffinity labeling and mass spectrometry. Mol. Pharm. 61(6), 1366-1376 (2002).
    • (2002) Mol. Pharm. , vol.61 , Issue.6 , pp. 1366-1376
    • Borchers, C.1    Boer, R.2    Klemm, K.3
  • 37
    • 0036176213 scopus 로고    scopus 로고
    • Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization mass spectrometry
    • Ecker GF, Csaszar E, Kopp S et al. Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization mass spectrometry. Mol. Pharm. 61(3), 637-648 (2002).
    • (2002) Mol. Pharm. , vol.61 , Issue.3 , pp. 637-648
    • Ecker, G.F.1    Csaszar, E.2    Kopp, S.3
  • 38
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach
    • Pleban K, Kopp S, Csaszar E et al. P-glycoprotein substrate binding domains are located at the transmembrane domain interfaces: a combined photoaffinity labeling-protein homology modeling approach. Mol. Pharm. 67(2), 365-374 (2005).
    • (2005) Mol. Pharm. , vol.67 , Issue.2 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3
  • 39
    • 0033553493 scopus 로고    scopus 로고
    • Photoaffinity labeling and mass spectrometry identify ribosomal protein S3 as a potential target for hybrid polar cytodifferentiation agents
    • Webb Y, Zhou X, Ngo L et al. Photoaffinity labeling and mass spectrometry identify ribosomal protein S3 as a potential target for hybrid polar cytodifferentiation agents. J. Biol. Chem. 274(20), 14280-14287 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.20 , pp. 14280-14287
    • Webb, Y.1    Zhou, X.2    Ngo, L.3
  • 40
    • 4844221319 scopus 로고    scopus 로고
    • 14C]Carboplatin-binding proteins reveals reduced expression and disorganization of actin and filamin in cisplatin-resistant cell lines
    • 14C]Carboplatin-binding proteins reveals reduced expression and disorganization of actin and filamin in cisplatin-resistant cell lines. Mol. Pharm. 66(4), 789-793 (2004).
    • (2004) Mol. Pharm. , vol.66 , Issue.4 , pp. 789-793
    • Shen, D.-W.1    Liang, X.-J.2    Gawinowicz, M.3    Gottesman, M.M.4
  • 41
    • 11144357573 scopus 로고    scopus 로고
    • Characterization of the binding site for inhibitors of the HPV11 E1-E2 protein interaction on the E2 transactivation domain by photoaffinity labeling and mass spectrometry
    • Davidson W, McGibbon G, White P et al. Characterization of the binding site for inhibitors of the HPV11 E1-E2 protein interaction on the E2 transactivation domain by photoaffinity labeling and mass spectrometry. Anal. Chem. 76(7), 2095-2102 (2004).
    • (2004) Anal. Chem. , vol.76 , Issue.7 , pp. 2095-2102
    • Davidson, W.1    McGibbon, G.2    White, P.3
  • 42
    • 14744304574 scopus 로고    scopus 로고
    • Proteomics by FTICR mass spectrometry: Top down and bottom up
    • Bogdanov B, Smith RD. Proteomics by FTICR mass spectrometry: top down and bottom up. Mass Spec. Rev. 24, 168-200 (2005). •• Provides an informative broad overview of recent technological developments and applications of Fourier transform ion cyclotron resonance (FTICR) mass spectrometry (MS) involving proteins and peptides.
    • (2005) Mass Spec. Rev. , vol.24 , pp. 168-200
    • Bogdanov, B.1    Smith, R.D.2
  • 43
    • 0034665968 scopus 로고    scopus 로고
    • Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fouier Transform Ion Cyclotron Resonance Mass Spectrometry
    • Martin SE, Shabanowitz J, Hunt DF, Marto JA. Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fouier Transform Ion Cyclotron Resonance Mass Spectrometry. Anal. Chem. 72, 4266-4274 (2000). • Example of the tremendous analytical sensitivity achievable with FTICR-MS combined with nano-scale liquid chromatography for the analysis of peptides.
    • (2000) Anal. Chem. , vol.72 , pp. 4266-4274
    • Martin, S.E.1    Shabanowitz, J.2    Hunt, D.F.3    Marto, J.A.4
  • 44
    • 0031022343 scopus 로고    scopus 로고
    • Characterization of low affinity complexes between calmodulin and pyrazine derivatives by electrospray ionization mass spectrometry
    • Lafitte D, Benezech V, Bompart J et al. Characterization of low affinity complexes between calmodulin and pyrazine derivatives by electrospray ionization mass spectrometry. J. Mass Spec. 32, 87-93 (1997).
    • (1997) J. Mass Spec. , vol.32 , pp. 87-93
    • Lafitte, D.1    Benezech, V.2    Bompart, J.3
  • 45
    • 33745623119 scopus 로고    scopus 로고
    • Discovery of a small-molecule HIV-1 integrase inhibitor-binding site
    • Al-Mawsawi LQ, Fikkert, V, Dayam R et al. Discovery of a small-molecule HIV-1 integrase inhibitor-binding site. Proc. Natl Acad. Sci. USA 103(26), 10080-10085 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.26 , pp. 10080-10085
    • Al-Mawsawi, L.Q.1    Fikkert, V.2    Dayam, R.3
  • 46
    • 6944243952 scopus 로고    scopus 로고
    • A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA
    • Ecker GF, Pleban K, Kopp S et al. A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA. Mol. Pharm. 66(5), 1169-1179 (2004).
    • (2004) Mol. Pharm. , vol.66 , Issue.5 , pp. 1169-1179
    • Ecker, G.F.1    Pleban, K.2    Kopp, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.