메뉴 건너뛰기




Volumn 89, Issue 1, 2007, Pages 117-134

Equilibrium unfolding of DLC8 monomer by urea and guanidine hydrochloride: Distinctive global and residue level features

Author keywords

15N relaxation; Circular dichroism; Denaturants; DLC8; Fluorescence; Near native states; NMR; Protein unfolding; Secondary chemical shifts; Torsion angle predictions

Indexed keywords

AMIDE; ASPARAGINE; DYNEIN ADENOSINE TRIPHOSPHATASE; GLUTAMINE; GUANIDINE; LYSINE; MONOMER; NITROGEN 15; RECOMBINANT PROTEIN; TRYPTOPHAN; UREA;

EID: 33845679781     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.09.007     Document Type: Article
Times cited : (26)

References (89)
  • 1
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen C.B., and Scheraga H.A. Experimental and theoretical aspects of protein folding. Adv. Protein Chem. 29 (1975) 205-300
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 2
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • Dobson C.M. Experimental investigation of protein folding and misfolding. Methods 34 (2004) 4-14
    • (2004) Methods , vol.34 , pp. 4-14
    • Dobson, C.M.1
  • 4
    • 11244260589 scopus 로고    scopus 로고
    • Monitoring protein folding at atomic resolution
    • Kumar T.K., and Yu C. Monitoring protein folding at atomic resolution. Acc. Chem. Res. 37 (2004) 929-936
    • (2004) Acc. Chem. Res. , vol.37 , pp. 929-936
    • Kumar, T.K.1    Yu, C.2
  • 5
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 6
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: bringing together theory and experiment
    • Dobson C.M., and Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9 (1999) 92-101
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 7
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson H.J., and Wright P.E. Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394 (2005) 299-321
    • (2005) Methods Enzymol. , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 8
    • 4444362186 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
    • Foguel D., and Silva J.L. New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies. Biochemistry 43 (2004) 11361-11370
    • (2004) Biochemistry , vol.43 , pp. 11361-11370
    • Foguel, D.1    Silva, J.L.2
  • 9
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: the rate-limiting step in two-state cytochrome c folding
    • Sosnick T.R., Mayne L., and Englander S.W. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins 24 (1996) 413-426
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 10
    • 0035812628 scopus 로고    scopus 로고
    • Folding of horse cytochrome c in the reduced state
    • Bhuyan A.K., and Udgaonkar J.B. Folding of horse cytochrome c in the reduced state. J. Mol. Biol. 312 (2001) 1135-1160
    • (2001) J. Mol. Biol. , vol.312 , pp. 1135-1160
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 12
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 13
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
    • Selkoe D.J. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 6 (2004) 1054-1061
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 14
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 15
    • 0027402748 scopus 로고
    • A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies
    • Pappa H.S., and Cass A.E. A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies. Eur. J. Biochem. 212 (1993) 227-235
    • (1993) Eur. J. Biochem. , vol.212 , pp. 227-235
    • Pappa, H.S.1    Cass, A.E.2
  • 16
  • 17
    • 0029198907 scopus 로고
    • Fluorescence spectroscopy
    • Royer C.A. Fluorescence spectroscopy. Methods Mol. Biol. 40 (1995) 65-89
    • (1995) Methods Mol. Biol. , vol.40 , pp. 65-89
    • Royer, C.A.1
  • 18
    • 0034717064 scopus 로고    scopus 로고
    • Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
    • van Mierlo C.P., and Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J. Biotechnol. 79 (2000) 281-298
    • (2000) J. Biotechnol. , vol.79 , pp. 281-298
    • van Mierlo, C.P.1    Steensma, E.2
  • 19
    • 0033980811 scopus 로고    scopus 로고
    • Apoflavodoxin (un)folding followed at the residue level by NMR
    • van Mierlo C.P., van den Oever J.M., and Steensma E. Apoflavodoxin (un)folding followed at the residue level by NMR. Protein Sci. 9 (2000) 145-157
    • (2000) Protein Sci. , vol.9 , pp. 145-157
    • van Mierlo, C.P.1    van den Oever, J.M.2    Steensma, E.3
  • 20
    • 3342936435 scopus 로고    scopus 로고
    • High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins
    • Kamatari Y.O., Kitahara R., Yamada H., Yokoyama S., and Akasaka K. High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods 34 (2004) 133-143
    • (2004) Methods , vol.34 , pp. 133-143
    • Kamatari, Y.O.1    Kitahara, R.2    Yamada, H.3    Yokoyama, S.4    Akasaka, K.5
  • 21
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht A.R., and Daggett V. Protein folding and unfolding at atomic resolution. Cell 108 (2002) 573-582
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 22
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander S.W. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 213-238
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 23
    • 0037174849 scopus 로고    scopus 로고
    • Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters
    • Kamal J.K., Nazeerunnisa M., and Behere D.V. Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters. J. Biol. Chem. 277 (2002) 40717-40721
    • (2002) J. Biol. Chem. , vol.277 , pp. 40717-40721
    • Kamal, J.K.1    Nazeerunnisa, M.2    Behere, D.V.3
  • 24
    • 0037162406 scopus 로고    scopus 로고
    • Thermal and conformational stability of seed coat soybean peroxidase
    • Kamal J.K., and Behere D.V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 41 (2002) 9034-9042
    • (2002) Biochemistry , vol.41 , pp. 9034-9042
    • Kamal, J.K.1    Behere, D.V.2
  • 25
    • 0027438393 scopus 로고
    • Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models
    • Mann C.J., Royer C.A., and Matthews C.R. Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Sci. 2 (1993) 1853-1861
    • (1993) Protein Sci. , vol.2 , pp. 1853-1861
    • Mann, C.J.1    Royer, C.A.2    Matthews, C.R.3
  • 26
    • 0025033667 scopus 로고
    • Dynamic Monte Carlo simulations of globular protein folding. Model studies of in vivo assembly of four helix bundles and four member beta-barrels
    • Sikorski A., and Skolnick J. Dynamic Monte Carlo simulations of globular protein folding. Model studies of in vivo assembly of four helix bundles and four member beta-barrels. J. Mol. Biol. 215 (1990) 183-198
    • (1990) J. Mol. Biol. , vol.215 , pp. 183-198
    • Sikorski, A.1    Skolnick, J.2
  • 27
    • 0025271503 scopus 로고
    • Dynamic Monte Carlo simulations of globular protein folding/unfolding pathways. II. Alpha-helical motifs
    • Sikorski A., and Skolnick J. Dynamic Monte Carlo simulations of globular protein folding/unfolding pathways. II. Alpha-helical motifs. J. Mol. Biol. 212 (1990) 819-836
    • (1990) J. Mol. Biol. , vol.212 , pp. 819-836
    • Sikorski, A.1    Skolnick, J.2
  • 28
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus M., and Sali A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5 (1995) 58-73
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 29
    • 0030601851 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein
    • Guo Z., and Thirumalai D. Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein. J. Mol. Biol. 263 (1996) 323-343
    • (1996) J. Mol. Biol. , vol.263 , pp. 323-343
    • Guo, Z.1    Thirumalai, D.2
  • 30
    • 23244433815 scopus 로고    scopus 로고
    • Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape
    • Finke J.M., and Onuchic J.N. Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape. Biophys. J. 89 (2005) 488-505
    • (2005) Biophys. J. , vol.89 , pp. 488-505
    • Finke, J.M.1    Onuchic, J.N.2
  • 32
    • 0037414459 scopus 로고    scopus 로고
    • Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta
    • Roy M., and Jennings P.A. Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta. J. Mol. Biol. 328 (2003) 693-703
    • (2003) J. Mol. Biol. , vol.328 , pp. 693-703
    • Roy, M.1    Jennings, P.A.2
  • 33
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman B.A., Kim P.S., Dobson C.M., and Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat. Struct. Biol. 4 (1997) 630-634
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 34
    • 0034733386 scopus 로고    scopus 로고
    • Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain
    • Arrington C.B., and Robertson A.D. Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain. J. Mol. Biol. 300 (2000) 221-232
    • (2000) J. Mol. Biol. , vol.300 , pp. 221-232
    • Arrington, C.B.1    Robertson, A.D.2
  • 35
    • 0034628897 scopus 로고    scopus 로고
    • Microsecond to minute dynamics revealed by EX1-type hydrogen exchange at nearly every backbone hydrogen bond in a native protein
    • Arrington C.B., and Robertson A.D. Microsecond to minute dynamics revealed by EX1-type hydrogen exchange at nearly every backbone hydrogen bond in a native protein. J. Mol. Biol. 296 (2000) 1307-1317
    • (2000) J. Mol. Biol. , vol.296 , pp. 1307-1317
    • Arrington, C.B.1    Robertson, A.D.2
  • 36
    • 0037176861 scopus 로고    scopus 로고
    • Characterization of the unfolding of ribonuclease a by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding
    • Juneja J., and Udgaonkar J.B. Characterization of the unfolding of ribonuclease a by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding. Biochemistry 41 (2002) 2641-2654
    • (2002) Biochemistry , vol.41 , pp. 2641-2654
    • Juneja, J.1    Udgaonkar, J.B.2
  • 37
    • 0034737304 scopus 로고    scopus 로고
    • Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways
    • Ramachandran S., Rami B.R., and Udgaonkar J.B. Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways. J. Mol. Biol. 297 (2000) 733-745
    • (2000) J. Mol. Biol. , vol.297 , pp. 733-745
    • Ramachandran, S.1    Rami, B.R.2    Udgaonkar, J.B.3
  • 38
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi F.N., Nath U., and Udgaonkar J.B. Multiple intermediates and transition states during protein unfolding. Nat. Struct. Biol. 4 (1997) 1016-1024
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1016-1024
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 39
    • 33746890530 scopus 로고    scopus 로고
    • Following autolysis in proteases by NMR: insights into multiple unfolding pathways and mutational plasticities
    • Chatterjee A., and Hosur R.V. Following autolysis in proteases by NMR: insights into multiple unfolding pathways and mutational plasticities. Biophys. Chem. (2006)
    • (2006) Biophys. Chem.
    • Chatterjee, A.1    Hosur, R.V.2
  • 41
    • 0037144504 scopus 로고    scopus 로고
    • Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein
    • Chi Y.H., Kumar T.K., Chiu I.M., and Yu C. Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein. J. Biol. Chem. 277 (2002) 34941-34948
    • (2002) J. Biol. Chem. , vol.277 , pp. 34941-34948
    • Chi, Y.H.1    Kumar, T.K.2    Chiu, I.M.3    Yu, C.4
  • 42
    • 12144259012 scopus 로고    scopus 로고
    • Dissecting contributions to the denaturant sensitivities of proteins
    • Dempsey C.E., Piggot T.J., and Mason P.E. Dissecting contributions to the denaturant sensitivities of proteins. Biochemistry 44 (2005) 775-781
    • (2005) Biochemistry , vol.44 , pp. 775-781
    • Dempsey, C.E.1    Piggot, T.J.2    Mason, P.E.3
  • 43
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (1995) 2138-2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 44
    • 18444410750 scopus 로고    scopus 로고
    • Guanidinium chloride- and urea-induced unfolding of FprA, a mycobacterium NADPH-ferredoxin reductase: stabilization of an apo-protein by GdmCl
    • Shukla N., Bhatt A.N., Aliverti A., Zanetti G., and Bhakuni V. Guanidinium chloride- and urea-induced unfolding of FprA, a mycobacterium NADPH-ferredoxin reductase: stabilization of an apo-protein by GdmCl. FEBS J. 272 (2005) 2216-2224
    • (2005) FEBS J. , vol.272 , pp. 2216-2224
    • Shukla, N.1    Bhatt, A.N.2    Aliverti, A.3    Zanetti, G.4    Bhakuni, V.5
  • 45
    • 2442567941 scopus 로고    scopus 로고
    • Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase
    • Boren K., Grankvist H., Hammarstrom P., and Carlsson U. Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase. FEBS Lett. 566 (2004) 95-99
    • (2004) FEBS Lett. , vol.566 , pp. 95-99
    • Boren, K.1    Grankvist, H.2    Hammarstrom, P.3    Carlsson, U.4
  • 46
    • 0032879344 scopus 로고    scopus 로고
    • New evidence for the denaturant binding model
    • Wu J.W., and Wang Z.X. New evidence for the denaturant binding model. Protein Sci. 8 (1999) 2090-2097
    • (1999) Protein Sci. , vol.8 , pp. 2090-2097
    • Wu, J.W.1    Wang, Z.X.2
  • 47
    • 0037133522 scopus 로고    scopus 로고
    • Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase
    • Akhtar M.S., Ahmad A., and Bhakuni V. Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase. Biochemistry 41 (2002) 3819-3827
    • (2002) Biochemistry , vol.41 , pp. 3819-3827
    • Akhtar, M.S.1    Ahmad, A.2    Bhakuni, V.3
  • 48
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera O.D., Kay C.M., and Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3 (1994) 1984-1991
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 49
    • 0028170819 scopus 로고
    • DYNEINS: molecular structure and cellular function
    • Holzbaur E.L., and Vallee R.B. DYNEINS: molecular structure and cellular function. Annu. Rev. Cell Biol. 10 (1994) 339-372
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 50
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar E., Kleinman B., Imhoff D., Li M., Hays T.S., and Hare M. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 40 (2001) 1596-1605
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 51
    • 31344449610 scopus 로고    scopus 로고
    • pH driven conformational dynamics and dimer-to-monomer transition in DLC8
    • Mohan P.M., Barve M., Chatterjee A., and Hosur R.V. pH driven conformational dynamics and dimer-to-monomer transition in DLC8. Protein Sci. 15 (2006) 335-342
    • (2006) Protein Sci. , vol.15 , pp. 335-342
    • Mohan, P.M.1    Barve, M.2    Chatterjee, A.3    Hosur, R.V.4
  • 53
    • 1342331844 scopus 로고    scopus 로고
    • The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila
    • Makokha M., Huang Y.J., Montelione G., Edison A.S., and Barbar E. The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila. Protein Sci. 13 (2004) 727-734
    • (2004) Protein Sci. , vol.13 , pp. 727-734
    • Makokha, M.1    Huang, Y.J.2    Montelione, G.3    Edison, A.S.4    Barbar, E.5
  • 54
    • 0032509467 scopus 로고    scopus 로고
    • Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme
    • Fan J.S., Zhang Q., Li M., Tochio H., Yamazaki T., Shimizu M., and Zhang M. Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme. J. Biol. Chem. 273 (1998) 33472-33481
    • (1998) J. Biol. Chem. , vol.273 , pp. 33472-33481
    • Fan, J.S.1    Zhang, Q.2    Li, M.3    Tochio, H.4    Yamazaki, T.5    Shimizu, M.6    Zhang, M.7
  • 55
    • 0029858301 scopus 로고    scopus 로고
    • PIN: an associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey S.R., and Snyder S.H. PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science 274 (1996) 774-777
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 56
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., and Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cells 3 (1999) 287-296
    • (1999) Mol. Cells , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 57
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L., Cheney R.E., Huang D.C., and Strasser A. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293 (2001) 1829-1832
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 58
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer F., Bohmann K., and Nusslein-Volhard C. The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nat. Cell Biol. 2 (2000) 185-190
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 59
    • 2342526589 scopus 로고    scopus 로고
    • Cytoplasmic dynein-dynactin complex is required for spermatid growth but not axoneme assembly in Drosophila
    • Ghosh-Roy A., Kulkarni M., Kumar V., Shirolikar S., and Ray K. Cytoplasmic dynein-dynactin complex is required for spermatid growth but not axoneme assembly in Drosophila. Mol. Biol. Cell 15 (2004) 2470-2483
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2470-2483
    • Ghosh-Roy, A.1    Kulkarni, M.2    Kumar, V.3    Shirolikar, S.4    Ray, K.5
  • 60
    • 3042755600 scopus 로고    scopus 로고
    • Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants
    • Murugan R., and Mazumdar S. Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants. J. Biol. Inorg. Chem. 9 (2004) 477-488
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 477-488
    • Murugan, R.1    Mazumdar, S.2
  • 61
    • 1042265192 scopus 로고    scopus 로고
    • Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study
    • Patel S., Chaffotte A.F., Goubard F., and Pauthe E. Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. Biochemistry 43 (2004) 1724-1735
    • (2004) Biochemistry , vol.43 , pp. 1724-1735
    • Patel, S.1    Chaffotte, A.F.2    Goubard, F.3    Pauthe, E.4
  • 62
    • 0034919873 scopus 로고    scopus 로고
    • Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins
    • Panchal S.C., Bhavesh N.S., and Hosur R.V. Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins. J. Biomol. NMR 20 (2001) 135-147
    • (2001) J. Biomol. NMR , vol.20 , pp. 135-147
    • Panchal, S.C.1    Bhavesh, N.S.2    Hosur, R.V.3
  • 64
    • 0035846574 scopus 로고    scopus 로고
    • An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR
    • Bhavesh N.S., Panchal S.C., and Hosur R.V. An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR. Biochemistry 40 (2001) 14727-14735
    • (2001) Biochemistry , vol.40 , pp. 14727-14735
    • Bhavesh, N.S.1    Panchal, S.C.2    Hosur, R.V.3
  • 65
    • 0036295404 scopus 로고    scopus 로고
    • A novel protocol based on HN(C)N for rapid resonance assignment in ((15)N, (13)C) labeled proteins: implications to structural genomics
    • Chatterjee A., Bhavesh N.S., Panchal S.C., and Hosur R.V. A novel protocol based on HN(C)N for rapid resonance assignment in ((15)N, (13)C) labeled proteins: implications to structural genomics. Biochem. Biophys. Res. Commun. 293 (2002) 427-432
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 427-432
    • Chatterjee, A.1    Bhavesh, N.S.2    Panchal, S.C.3    Hosur, R.V.4
  • 66
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: a multifaceted approach to macromolecular structure
    • Ferentz A.E., and Wagner G. NMR spectroscopy: a multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33 (2000) 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 67
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • Lefevre J.F., Dayie K.T., Peng J.W., and Wagner G. Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry 35 (1996) 2674-2686
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefevre, J.F.1    Dayie, K.T.2    Peng, J.W.3    Wagner, G.4
  • 68
    • 0031587294 scopus 로고    scopus 로고
    • Unusual lack of internal mobility and fast overall tumbling in oxidized flavodoxin from Anacystis nidulans
    • Zhang P., Dayie K.T., and Wagner G. Unusual lack of internal mobility and fast overall tumbling in oxidized flavodoxin from Anacystis nidulans. J. Mol. Biol. 272 (1997) 443-455
    • (1997) J. Mol. Biol. , vol.272 , pp. 443-455
    • Zhang, P.1    Dayie, K.T.2    Wagner, G.3
  • 69
    • 0034642225 scopus 로고    scopus 로고
    • Effects of guanidine hydrochloride on the proton inventory of proteins: implications on interpretations of protein stability
    • Bolen D.W., and Yang M. Effects of guanidine hydrochloride on the proton inventory of proteins: implications on interpretations of protein stability. Biochemistry 39 (2000) 15208-15216
    • (2000) Biochemistry , vol.39 , pp. 15208-15216
    • Bolen, D.W.1    Yang, M.2
  • 70
    • 27744533599 scopus 로고    scopus 로고
    • Comparison of guanidine hydrochloride (GdnHCl) and urea denaturation on inactivation and unfolding of human placental cystatin (HPC)
    • Rashid F., Sharma S., and Bano B. Comparison of guanidine hydrochloride (GdnHCl) and urea denaturation on inactivation and unfolding of human placental cystatin (HPC). Protein J. 24 (2005) 283-292
    • (2005) Protein J. , vol.24 , pp. 283-292
    • Rashid, F.1    Sharma, S.2    Bano, B.3
  • 71
    • 0038504067 scopus 로고    scopus 로고
    • NMR elucidation of early folding hierarchy in HIV-1 protease
    • Bhavesh N.S., Sinha R., Mohan P.M., and Hosur R.V. NMR elucidation of early folding hierarchy in HIV-1 protease. J. Biol. Chem. 278 (2003) 19980-19985
    • (2003) J. Biol. Chem. , vol.278 , pp. 19980-19985
    • Bhavesh, N.S.1    Sinha, R.2    Mohan, P.M.3    Hosur, R.V.4
  • 72
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer D., Yao J., Dyson H.J., and Wright P.E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5 (1998) 148-155
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 73
    • 0034696675 scopus 로고    scopus 로고
    • Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin
    • Eliezer D., Chung J., Dyson H.J., and Wright P.E. Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry 39 (2000) 2894-2901
    • (2000) Biochemistry , vol.39 , pp. 2894-2901
    • Eliezer, D.1    Chung, J.2    Dyson, H.J.3    Wright, P.E.4
  • 74
    • 0036639910 scopus 로고    scopus 로고
    • Parameter optimized surfaces (POPS): analysis of key interactions and conformational changes in the ribosome
    • Fraternali F., and Cavallo L. Parameter optimized surfaces (POPS): analysis of key interactions and conformational changes in the ribosome. Nucleic Acids Res. 30 (2002) 2950-2960
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2950-2960
    • Fraternali, F.1    Cavallo, L.2
  • 75
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 76
    • 27444442808 scopus 로고    scopus 로고
    • Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation
    • Nyarko A., Cochrun L., Norwood S., Pursifull N., Voth A., and Barbar E. Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation. Biochemistry 44 (2005) 14248-14255
    • (2005) Biochemistry , vol.44 , pp. 14248-14255
    • Nyarko, A.1    Cochrun, L.2    Norwood, S.3    Pursifull, N.4    Voth, A.5    Barbar, E.6
  • 77
    • 27744471390 scopus 로고    scopus 로고
    • a shifts of titratable residues at high denaturant concentration and the impact on protein stability
    • a shifts of titratable residues at high denaturant concentration and the impact on protein stability. Biophys. Chem. 118 (2005) 88-92
    • (2005) Biophys. Chem. , vol.118 , pp. 88-92
    • Marti, D.N.1
  • 79
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView
    • Schwarzinger S., Kroon G.J., Foss T.R., Wright P.E., and Dyson H.J. Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J. Biomol. NMR 18 (2000) 43-48
    • (2000) J. Biomol. NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 80
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart D.S., and Sykes B.D. Chemical shifts as a tool for structure determination. Methods Enzymol. 239 (1994) 363-392
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 81
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • Wishart D.S., Bigam C.G., Holm A., Hodges R.S., and Sykes B.D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5 (1995) 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 82
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 83
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
    • Peng J.W., and Wagner G. Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31 (1992) 8571-8586
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 84
    • 16244417212 scopus 로고    scopus 로고
    • The native energy landscape for interleukin-1beta. Modulation of the population ensemble through native-state topology
    • Roy M., Chavez L.L., Finke J.M., Heidary D.K., Onuchic J.N., and Jennings P.A. The native energy landscape for interleukin-1beta. Modulation of the population ensemble through native-state topology. J. Mol. Biol. 348 (2005) 335-347
    • (2005) J. Mol. Biol. , vol.348 , pp. 335-347
    • Roy, M.1    Chavez, L.L.2    Finke, J.M.3    Heidary, D.K.4    Onuchic, J.N.5    Jennings, P.A.6
  • 85
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari G., and Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104 (1982) 4559-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 86
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G., and Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104 (1982) 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 88
    • 0142031484 scopus 로고    scopus 로고
    • Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature
    • Dubey V.K., and Jagannadham M.V. Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature. Biochemistry 42 (2003) 12287-12297
    • (2003) Biochemistry , vol.42 , pp. 12287-12297
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 89
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.