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Volumn 12, Issue 9, 2003, Pages 1980-1990

Dissecting interdomain communication within cAPK regulatory subunit type IIβ using enhanced amide hydrogen/deuterium exchange mass spectrometry (DXMS)

Author keywords

Amide hydrogen exchange; cAPK; Mass spectrometry; PKA; Regulatory subunit

Indexed keywords

AMIDE; ARGININE; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIMER; LYSINE; MUTANT PROTEIN; PROTEIN SUBUNIT; REGULATOR PROTEIN;

EID: 0042010184     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03166903     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 0037178847 scopus 로고    scopus 로고
    • Increased basal PKA activity inhibits the formation of mesoderm-derived structures in the developing mouse embryo
    • Amieux, P.S., Howe, D.G., Knickerbocker, H., Lee, D.C., Su, T., Laslo, G.S., Idzerda, R.L., and McKnight, G.S. 2002. Increased basal PKA activity inhibits the formation of mesoderm-derived structures in the developing mouse embryo. J. Biol. Chem. 277: 27294-27304.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27294-27304
    • Amieux, P.S.1    Howe, D.G.2    Knickerbocker, H.3    Lee, D.C.4    Su, T.5    Laslo, G.S.6    Idzerda, R.L.7    McKnight, G.S.8
  • 2
    • 0036025308 scopus 로고    scopus 로고
    • Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the RIα subunit of protein kinase A
    • Anand, G.S., Hughes, C.A., Jones, J.M., Taylor, S.S., and Komives, E.A. 2002. Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the RIα subunit of protein kinase A. J. Mol. Biol. 323: 377-386.
    • (2002) J. Mol. Biol. , vol.323 , pp. 377-386
    • Anand, G.S.1    Hughes, C.A.2    Jones, J.M.3    Taylor, S.S.4    Komives, E.A.5
  • 3
    • 0035958029 scopus 로고    scopus 로고
    • Structural characterization of protein kinase A as a function of nucleotide binding: Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection
    • Andersen, M.D., Shaffer, J., Jennings, P.A., and Adams, J.A. 2001. Structural characterization of protein kinase A as a function of nucleotide binding: Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection. J. Biol. Chem. 276: 14204-14211.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14204-14211
    • Andersen, M.D.1    Shaffer, J.2    Jennings, P.A.3    Adams, J.A.4
  • 4
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L.C., and Englander, S.W. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17: 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.C.3    Englander, S.W.4
  • 7
    • 0023645782 scopus 로고
    • Antiparallel alignment of the two protomers of the regulatory subunit dimer of cyclic AMP-dependent protein kinase I
    • Bubis, J., Vedvick, T.S., and Taylor, S.S. 1987. Antiparallel alignment of the two protomers of the regulatory subunit dimer of cyclic AMP-dependent protein kinase I. J. Biol. Chem. 262: 14961-14966.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14961-14966
    • Bubis, J.1    Vedvick, T.S.2    Taylor, S.S.3
  • 8
    • 0023718389 scopus 로고
    • A point mutation abolishes binding of cyclic AMP to site A in the regulatory subunit of cyclic AMP-dependent protein kinase
    • Bubis, J., Neitzel, J.J., Saraswat, L.D., and Taylor, S.S. 1988. A point mutation abolishes binding of cyclic AMP to site A in the regulatory subunit of cyclic AMP-dependent protein kinase. J. Biol. Chem. 263: 9668-9673.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9668-9673
    • Bubis, J.1    Neitzel, J.J.2    Saraswat, L.D.3    Taylor, S.S.4
  • 9
    • 0036132994 scopus 로고    scopus 로고
    • Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family
    • Canaves, J.M. and Taylor, S.S. 2002. Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family. J. Mol. Evol. 54: 17-29.
    • (2002) J. Mol. Evol. , vol.54 , pp. 17-29
    • Canaves, J.M.1    Taylor, S.S.2
  • 10
    • 0034642224 scopus 로고    scopus 로고
    • Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase
    • Canaves, J.M., Leon, D.A., and Taylor, S.S. 2000. Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase. Biochemistry 39: 15022-15031.
    • (2000) Biochemistry , vol.39 , pp. 15022-15031
    • Canaves, J.M.1    Leon, D.A.2    Taylor, S.S.3
  • 11
    • 0031454332 scopus 로고    scopus 로고
    • Activation by cyclic GMP binding causes an apparent conformational change in cGMP-dependent protein kinase
    • Chu, D.M., Corbin, J.D., Grimes, K.A., and Francis S.H. 1997. Activation by cyclic GMP binding causes an apparent conformational change in cGMP-dependent protein kinase. J Biol. Chem. 272: 31922-31928.
    • (1997) J Biol. Chem. , vol.272 , pp. 31922-31928
    • Chu, D.M.1    Corbin, J.D.2    Grimes, K.A.3    Francis, S.H.4
  • 12
    • 0011564219 scopus 로고
    • Genetic characterization of a brain-specific form of the type I regulatory subunit of cyclic AMP-dependent protein kinase
    • Clegg, C.H., Cadd, G.G., and McKnight, G.S. 1988. Genetic characterization of a brain-specific form of the type I regulatory subunit of cyclic AMP-dependent protein kinase. Proc. Natl. Acad. Sci. 85: 3703-3707.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 3703-3707
    • Clegg, C.H.1    Cadd, G.G.2    McKnight, G.S.3
  • 13
    • 12444262921 scopus 로고
    • Utilization of fusion systems and protein-protein interactions for production and purification of mutant subunits of cAMP-dependent protein kinase
    • Cox, S., Bell, S.M., Herberg, F.W., and Taylor, S.S. 1994. Utilization of fusion systems and protein-protein interactions for production and purification of mutant subunits of cAMP-dependent protein kinase. FASEB J. 8: A1226.
    • (1994) FASEB J. , vol.8
    • Cox, S.1    Bell, S.M.2    Herberg, F.W.3    Taylor, S.S.4
  • 14
    • 0029737861 scopus 로고    scopus 로고
    • Genetically lean mice result from targeted disruption of the RII β subunit of protein kinase A
    • Cummings, D.E., Brandon, E.P., Planas, J.V., Motamed, K., Idzerda, R.L., and McKnight, G.S. 1996. Genetically lean mice result from targeted disruption of the RII β subunit of protein kinase A. Nature 382: 622-626.
    • (1996) Nature , vol.382 , pp. 622-626
    • Cummings, D.E.1    Brandon, E.P.2    Planas, J.V.3    Motamed, K.4    Idzerda, R.L.5    McKnight, G.S.6
  • 15
    • 0035148589 scopus 로고    scopus 로고
    • Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: Crystal structure of the type IIb regulatory subunit
    • Diller, T.C., Madhusudan, Xuong, N.-H., and Taylor, S.S. 2001. Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: Crystal structure of the type IIb regulatory subunit. Structure 9: 73-82.
    • (2001) Structure , vol.9 , pp. 73-82
    • Diller, T.C.1    Madhusudan2    Xuong, N.-H.3    Taylor, S.S.4
  • 16
    • 0033557450 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions
    • Ehring, H. 1999. Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions. Anal. Biochem. 267: 252-259.
    • (1999) Anal. Biochem. , vol.267 , pp. 252-259
    • Ehring, H.1
  • 17
    • 0035326304 scopus 로고    scopus 로고
    • Investigating protein structure and dynamics by hydrogen exchange MS
    • Engen, J.R. and Smith, D.L. 2001. Investigating protein structure and dynamics by hydrogen exchange MS. Anal. Chem. 73: 256A-265A.
    • (2001) Anal. Chem. , vol.73
    • Engen, J.R.1    Smith, D.L.2
  • 18
    • 0033551496 scopus 로고    scopus 로고
    • Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2
    • Erigen, J.R., Gmeiner, W.H., Smithgall, T.E., and Smith, D.L. 1999. Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2. Biochemistry 38: 8926-8935.
    • (1999) Biochemistry , vol.38 , pp. 8926-8935
    • Erigen, J.R.1    Gmeiner, W.H.2    Smithgall, T.E.3    Smith, D.L.4
  • 20
  • 21
    • 0036428762 scopus 로고    scopus 로고
    • Phosphorylation-driven motion in the COOH-terminal Src kinase, Csk, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS)
    • Hamuro, Y., Wong, L., Shaffer, J., Kim, J.S., Stranz, D.D., Jennings, P.A., Adams, J.A., and Woods Jr., V.L. 2002b. Phosphorylation-driven motion in the COOH-terminal Src kinase, Csk, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS). J. Mol. Biol. 323: 871-881.
    • (2002) J. Mol. Biol. , vol.323 , pp. 871-881
    • Hamuro, Y.1    Wong, L.2    Shaffer, J.3    Kim, J.S.4    Stranz, D.D.5    Jennings, P.A.6    Adams, J.A.7    Woods V.L., Jr.8
  • 22
    • 0344405702 scopus 로고    scopus 로고
    • Dynamics of cAPK type IIβ activation revealed by enhanced amide H/ 2H exchange mass spectrometry (DXMS)
    • Hamuro, Y., Zawadzki, K.M., Kim, J.S., Stranz, D.D., Taylor, S.S., and Woods Jr., V.L. 2003. Dynamics of cAPK type IIβ activation revealed by enhanced amide H/2H exchange mass spectrometry (DXMS). J. Mol. Biol. 327: 1065-1076.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1065-1076
    • Hamuro, Y.1    Zawadzki, K.M.2    Kim, J.S.3    Stranz, D.D.4    Taylor, S.S.5    Woods V.L., Jr.6
  • 23
    • 0029932259 scopus 로고    scopus 로고
    • Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase
    • Herberg, F.W., Taylor, S.S., and Dostmann, W.R.G. 1996. Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase. Biochemistry 35: 2934-2942.
    • (1996) Biochemistry , vol.35 , pp. 2934-2942
    • Herberg, F.W.1    Taylor, S.S.2    Dostmann, W.R.G.3
  • 24
    • 0016772776 scopus 로고
    • Comparison of adenosine 3′:5′-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle
    • Hofmann, F., Beavo, J.A., Bechtel, P.J., and Krebs, E.G. 1975. Comparison of adenosine 3′:5′-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle. J. Biol. Chem. 250: 7795-7801.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7795-7801
    • Hofmann, F.1    Beavo, J.A.2    Bechtel, P.J.3    Krebs, E.G.4
  • 25
    • 0017359323 scopus 로고
    • Concentrations of cyclic AMP-dependent protein kinase subunits in various tissues
    • Hofmann, F., Bechtel, P.J., and Krebs, E.G. 1977. Concentrations of cyclic AMP-dependent protein kinase subunits in various tissues. J. Biol. Chem. 252: 1441-1447.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1441-1447
    • Hofmann, F.1    Bechtel, P.J.2    Krebs, E.G.3
  • 26
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • Hoofnagle, A.N., Resing, K.A., Goldsmith, E.J., and Ahn, N.G. 2001. Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. Proc. Natl. Acad. Sci. 98: 956-961.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 27
    • 0022826745 scopus 로고
    • The neutral type II regulatory subunit of cyclic AMP-dependent protein kinase is present and regulated by hormones in the rat ovary
    • Jahnsen, T., Hedin, L., Lohmann, S.M., Walter, U., and Richards, J.S. 1986. The neutral type II regulatory subunit of cyclic AMP-dependent protein kinase is present and regulated by hormones in the rat ovary. J. Biol. Chem. 261: 6637-6639.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6637-6639
    • Jahnsen, T.1    Hedin, L.2    Lohmann, S.M.3    Walter, U.4    Richards, J.S.5
  • 28
    • 0028910357 scopus 로고
    • Mutagenesis of the regulatory subunit (RII-β) of cAMP-dependent protein kinase ii-β reveals hydrophobic amino acids that are essential for RII-β dimerization and/or anchoring RII-β to the cytoskeleton
    • Li, Y. and Rubin, C.S. 1995. Mutagenesis of the regulatory subunit (RII-β) of cAMP-dependent protein kinase ii-β reveals hydrophobic amino acids that are essential for RII-β dimerization and/or anchoring RII-β to the cytoskeleton. J. Biol. Chem. 270: 1935-1944.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1935-1944
    • Li, Y.1    Rubin, C.S.2
  • 29
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell, J.G., Falick, A.M., and Komives, E.A. 1998. Identification of protein-protein interfaces by decreased amide proton solvent accessibility. Proc. Natl. Acad. Sci. 95: 14705-14710.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 31
    • 0026084838 scopus 로고
    • Role of magnesium ATP in the activation and reassociation of cyclic AMP-dependent protein kinase I: Consequences of replacing the essential arginine in cyclic AMP binding site A
    • Neitzel, J.J., Dostmann, W.R.G., and Taylor, S.S. 1991. Role of magnesium ATP in the activation and reassociation of cyclic AMP-dependent protein kinase I: Consequences of replacing the essential arginine in cyclic AMP binding site A. Biochemistry 30: 733-739.
    • (1991) Biochemistry , vol.30 , pp. 733-739
    • Neitzel, J.J.1    Dostmann, W.R.G.2    Taylor, S.S.3
  • 32
    • 0030907866 scopus 로고    scopus 로고
    • Monitoring calcium-induced conformational changes in Recoverin by electrospray mass spectrometry
    • Neubert, T.A., Walsh, K.A., Hurley, J.B., and Johnson, R.S. 1997. Monitoring calcium-induced conformational changes in Recoverin by electrospray mass spectrometry. Protein Sci. 6: 843-850.
    • (1997) Protein Sci. , vol.6 , pp. 843-850
    • Neubert, T.A.1    Walsh, K.A.2    Hurley, J.B.3    Johnson, R.S.4
  • 33
    • 0035794551 scopus 로고    scopus 로고
    • A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes
    • Newlon, M., Roy, M., Morikis, D., Carr, D.W., Westphal, R., Scott, J.D., and Jennings, P.A. 2001. A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J. 20: 1651-1662.
    • (2001) EMBO J. , vol.20 , pp. 1651-1662
    • Newlon, M.1    Roy, M.2    Morikis, D.3    Carr, D.W.4    Westphal, R.5    Scott, J.D.6    Jennings, P.A.7
  • 34
    • 0019518152 scopus 로고
    • The kinetics of the interaction between cyclic AMP and the regulatory moiety of protein kinase II: Evidence for interaction between the binding sites for cyclic AMP
    • Ogreid, D. and Døskeland, S.O. 1981a. The kinetics of the interaction between cyclic AMP and the regulatory moiety of protein kinase II: Evidence for interaction between the binding sites for cyclic AMP. FEBS Lett. 129: 282-286.
    • (1981) FEBS Lett. , vol.129 , pp. 282-286
    • Ogreid, D.1    Døskeland, S.O.2
  • 35
    • 0019410695 scopus 로고
    • The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium
    • -. 1981b. The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium. FEBS Lett. 129: 287-292.
    • (1981) FEBS Lett. , vol.129 , pp. 287-292
  • 36
    • 0033474495 scopus 로고    scopus 로고
    • Modeling deuterium exchange behavior of Erk2 using pepsin mapping to probe secondary structure
    • Resing, K.A., Hoofnagle, A.N., and Ahn, N.G. 1999. Modeling deuterium exchange behavior of Erk2 using pepsin mapping to probe secondary structure. J. Am. Soc. Mass Spectrom. 10: 685-702.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 685-702
    • Resing, K.A.1    Hoofnagle, A.N.2    Ahn, N.G.3
  • 37
    • 0016703354 scopus 로고
    • Reversible autophosphorylation of a cyclic 3′:5′-AMP-dependent protein kinase from bovine cardiac muscle
    • Rosen, O.M. and Erlichman, J. 1975. Reversible autophosphorylation of a cyclic 3′:5′-AMP-dependent protein kinase from bovine cardiac muscle. J. Biol. Chem. 250: 7788-7794.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7788-7794
    • Rosen, O.M.1    Erlichman, J.2
  • 38
    • 0018801622 scopus 로고
    • Characterization and comparison of membrane-associated and cytosolic cAMP-dependent protein kinases: Studies on human erythrocyte protein kinases
    • Rubin, C.S. 1979. Characterization and comparison of membrane-associated and cytosolic cAMP-dependent protein kinases: Studies on human erythrocyte protein kinases. J. Biol. Chem. 254: 12439-12449.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12439-12449
    • Rubin, C.S.1
  • 39
    • 0024203555 scopus 로고    scopus 로고
    • Deletion mutants as probes for localizing regions of subunit interaction in cyclic AMP-dependent protein kinase
    • Saraswat, L.D., Ringheim, G.E., Bubis, J., and Taylor, S.S. 1998. Deletion mutants as probes for localizing regions of subunit interaction in cyclic AMP-dependent protein kinase. J. Biol. Chem. 263: 18241-18246.
    • (1998) J. Biol. Chem. , vol.263 , pp. 18241-18246
    • Saraswat, L.D.1    Ringheim, G.E.2    Bubis, J.3    Taylor, S.S.4
  • 40
    • 0035516189 scopus 로고    scopus 로고
    • Mutation of the RIIβ subunit of protein kinase A prevents diet-induced insulin resistance and dyslipidemia in mice
    • Schreyer, S.A., Cummings, D.E., McKnight, G.S., and LeBoeuf, R.C. 2001. Mutation of the RIIβ subunit of protein kinase A prevents diet-induced insulin resistance and dyslipidemia in mice. Diabetes 50: 2555-2562.
    • (2001) Diabetes , vol.50 , pp. 2555-2562
    • Schreyer, S.A.1    Cummings, D.E.2    McKnight, G.S.3    LeBoeuf, R.C.4
  • 41
    • 0023644616 scopus 로고
    • Differential expression of isoforms of the regulatory subunit of type II cyclic AMP-dependent protein kinase in rat neurons, astrocytes, and oligodendrocytes
    • Stein, J.C., Farooq, M., Norton, W.T., and Rubin, C.S. 1987. Differential expression of isoforms of the regulatory subunit of type II cyclic AMP-dependent protein kinase in rat neurons, astrocytes, and oligodendrocytes. J. Biol. Chem. 262: 3002-3006.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3002-3006
    • Stein, J.C.1    Farooq, M.2    Norton, W.T.3    Rubin, C.S.4
  • 42
    • 0029910145 scopus 로고    scopus 로고
    • Arginine 210 is not a critical residue for the allosteric interactions mediated by binding of cyclic AMP to site A of regulatory (RI-α) subunit of cyclic AMP-dependent protein kinase
    • Steinberg, R.A., Symcox, M.M., Sollid, S., and Ogreid, D. 1996. Arginine 210 is not a critical residue for the allosteric interactions mediated by binding of cyclic AMP to site A of regulatory (RI-α) subunit of cyclic AMP-dependent protein kinase. J. Biol. Chem. 271: 27630-27636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27630-27636
    • Steinberg, R.A.1    Symcox, M.M.2    Sollid, S.3    Ogreid, D.4
  • 44
    • 0028100725 scopus 로고
    • Arg-242 is necessary for allosteric coupling of cyclic AMP-binding sites A and B of RI subunit of cyclic AMP-dependent protein kinase
    • Symcox, M.M., Cauthron, R.D., Ogreid, D., and Steinberg, R.A. 1994. Arg-242 is necessary for allosteric coupling of cyclic AMP-binding sites A and B of RI subunit of cyclic AMP-dependent protein kinase. J. Biol. Chem. 269: 23025-23031.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23025-23031
    • Symcox, M.M.1    Cauthron, R.D.2    Ogreid, D.3    Steinberg, R.A.4
  • 45
    • 12444297153 scopus 로고    scopus 로고
    • 1997. Method for characterization of the fine structure of protein binding sites. US patent no. 5,658,739
    • Woods Jr., V.L. 1997. Method for characterization of the fine structure of protein binding sites. US patent no. 5,658,739.
    • Woods V.L., Jr.1
  • 46
    • 12444270721 scopus 로고    scopus 로고
    • 2001a. Method for characterization of the fine structure of protein binding sites. US patent no. 6331,400
    • -. 2001a. Method for characterization of the fine structure of protein binding sites. US patent no. 6331,400.
  • 47
    • 12444278602 scopus 로고    scopus 로고
    • 2001b. Methods for the high-resolution identification of solvent-accessible amide hydrogens in polypeptides or proteins and for the characterization of the fine structure of protein binding sites. US patent no. 6,291,189
    • -. 2001b. Methods for the high-resolution identification of solvent-accessible amide hydrogens in polypeptides or proteins and for the characterization of the fine structure of protein binding sites. US patent no. 6,291,189.
  • 48
    • 0035753065 scopus 로고    scopus 로고
    • High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: Utility in pharmaceutical design
    • Woods, V.L. and Hamuro, Y. 2001. High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: Utility in pharmaceutical design. J. Cell Biochem. Suppl. 37: 89-98.
    • (2001) J. Cell Biochem. Suppl. , vol.37 , pp. 89-98
    • Woods, V.L.1    Hamuro, Y.2
  • 49
    • 0012580091 scopus 로고    scopus 로고
    • Endogenous tryptophan residues of cAPK regulatory subunit type IIb reveal local variations in environment and dynamics
    • Zawadzki, K.M., Pan, C.-P., Johnson, D., Barkley, M.D., and Taylor, S.S. 2003. Endogenous tryptophan residues of cAPK regulatory subunit type IIb reveal local variations in environment and dynamics. Proteins 51: 552-561
    • (2003) Proteins , vol.51 , pp. 552-561
    • Zawadzki, K.M.1    Pan, C.-P.2    Johnson, D.3    Barkley, M.D.4    Taylor, S.S.5
  • 50
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z. and Smith, D.L. 1993. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2: 522-531.
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 51
    • 0020478750 scopus 로고
    • Interchain disulfide bonding in the regulatory subunit of cAMP-dependent protein kinase I
    • Zick, S.K. and Taylor, S.S. 1982. Interchain disulfide bonding in the regulatory subunit of cAMP-dependent protein kinase I. J. Biol. Chem. 257: 2287-2293.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2287-2293
    • Zick, S.K.1    Taylor, S.S.2
  • 52
    • 0018786526 scopus 로고
    • Structural comparisons of cAMP-dependent protein kinases I and II from porcine skeletal muscle
    • Zoller, M.J., Kerlavage, A.R., and Taylor, S.S. 1979. Structural comparisons of cAMP-dependent protein kinases I and II from porcine skeletal muscle. J. Biol. Chem. 254: 2408-2412.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2408-2412
    • Zoller, M.J.1    Kerlavage, A.R.2    Taylor, S.S.3


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