-
1
-
-
0032508046
-
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
-
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry III C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 6685 (1998) 537-544
-
(1998)
Nature
, vol.393
, Issue.6685
, pp. 537-544
-
-
Cole, S.T.1
Brosch, R.2
Parkhill, J.3
Garnier, T.4
Churcher, C.5
Harris, D.6
Gordon, S.V.7
Eiglmeier, K.8
Gas, S.9
Barry III, C.E.10
Tekaia, F.11
Badcock, K.12
Basham, D.13
Brown, D.14
Chillingworth, T.15
Connor, R.16
Davies, R.17
Devlin, K.18
Feltwell, T.19
Gentles, S.20
Hamlin, N.21
Holroyd, S.22
Hornsby, T.23
Jagels, K.24
Krogh, A.25
McLean, J.26
Moule, S.27
Murphy, L.28
Oliver, K.29
Osborne, J.30
Quail, M.A.31
Rajandream, M.A.32
Rogers, J.33
Rutter, S.34
Seeger, K.35
Skelton, J.36
Squares, R.37
Squares, S.38
Sulston, J.E.39
Taylor, K.40
Whitehead, S.41
Barrell, B.G.42
more..
-
2
-
-
0024959449
-
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
-
Fischer G., Wittmann-Liebold B., Lang K., Kiefhaber T., and Schmid F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337 (1989) 476-478
-
(1989)
Nature
, vol.337
, pp. 476-478
-
-
Fischer, G.1
Wittmann-Liebold, B.2
Lang, K.3
Kiefhaber, T.4
Schmid, F.X.5
-
3
-
-
0024959451
-
Peptidyl-prolyl cis-trans isomerase is the cyclosporin-A-binding protein cyclophilin
-
Takahashi N., Hayano T., and Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin-A-binding protein cyclophilin. Nature 337 (1989) 473-475
-
(1989)
Nature
, vol.337
, pp. 473-475
-
-
Takahashi, N.1
Hayano, T.2
Suzuki, M.3
-
5
-
-
20044396197
-
Roles of cyclophilins in cancers and other organ systems
-
Yao Q., Li M., Yang H., Chai H., Fisher W., and Chen C. Roles of cyclophilins in cancers and other organ systems. World J. Surg. 29 3 (2005) 276-280
-
(2005)
World J. Surg.
, vol.29
, Issue.3
, pp. 276-280
-
-
Yao, Q.1
Li, M.2
Yang, H.3
Chai, H.4
Fisher, W.5
Chen, C.6
-
6
-
-
0025005939
-
Cyclosporin A: new insights for cell biologists and biochemists
-
Hohman R.J., and Hultsch T. Cyclosporin A: new insights for cell biologists and biochemists. New Biol. 2 8 (1990) 663-672
-
(1990)
New Biol.
, vol.2
, Issue.8
, pp. 663-672
-
-
Hohman, R.J.1
Hultsch, T.2
-
7
-
-
33745316971
-
Novel activities of cyclophilin A and cyclosporin A during HIV-1 infection of primary lymphocytes and macrophages
-
Saini M., and Potash M.J. Novel activities of cyclophilin A and cyclosporin A during HIV-1 infection of primary lymphocytes and macrophages. J. Immunol. 177 1 (2006) 443-449
-
(2006)
J. Immunol.
, vol.177
, Issue.1
, pp. 443-449
-
-
Saini, M.1
Potash, M.J.2
-
8
-
-
0032918010
-
Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry
-
Wong D.K., Lee B.Y., Horwitz M.A., and Gibson B.W. Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect. Immun. 67 (1999) 327-336
-
(1999)
Infect. Immun.
, vol.67
, pp. 327-336
-
-
Wong, D.K.1
Lee, B.Y.2
Horwitz, M.A.3
Gibson, B.W.4
-
9
-
-
7044220836
-
X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis
-
Henricksson L.M., Johansson P., Unge T., and Mowbray S.L. X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis. Eur. J. Biochem. 271 (2004) 4107-4113
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 4107-4113
-
-
Henricksson, L.M.1
Johansson, P.2
Unge, T.3
Mowbray, S.L.4
-
10
-
-
0027492164
-
Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment
-
Surewicz W.K., Mantsch H.H., and Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32 (1993) 389-394
-
(1993)
Biochemistry
, vol.32
, pp. 389-394
-
-
Surewicz, W.K.1
Mantsch, H.H.2
Chapman, D.3
-
11
-
-
0023837785
-
New insight into protein secondary structure from resolution-enhanced infrared spectra
-
Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952 (1988) 115-130
-
(1988)
Biochim. Biophys. Acta
, vol.952
, pp. 115-130
-
-
Surewicz, W.K.1
Mantsch, H.H.2
-
12
-
-
0027354020
-
Quantitative studies of the structure of proteins in solution by Fourier transform infrared spectroscopy
-
Arrondo J.L.R., Muga A., Castresana J., and Goni F.M. Quantitative studies of the structure of proteins in solution by Fourier transform infrared spectroscopy. Progr. Biophys. Mol. Biol. 59 (1992) 23-56
-
(1992)
Progr. Biophys. Mol. Biol.
, vol.59
, pp. 23-56
-
-
Arrondo, J.L.R.1
Muga, A.2
Castresana, J.3
Goni, F.M.4
-
13
-
-
0026491207
-
Structural and functional relationships in DnaK and Dnak756 heat-shock proteins from Escherichia coli
-
Banecki B., Zylicz M., Bertoli E., and Tanfani F. Structural and functional relationships in DnaK and Dnak756 heat-shock proteins from Escherichia coli. J. Biol. Chem. 267 (1992) 25051-25058
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 25051-25058
-
-
Banecki, B.1
Zylicz, M.2
Bertoli, E.3
Tanfani, F.4
-
14
-
-
0026547252
-
Structural and functional relationships in 5′-nucleotidase from bull seminal plasma. A Fourier transform infrared study
-
Fini C., Bertoli E., Albertini G., Floridi A., and Tanfani F. Structural and functional relationships in 5′-nucleotidase from bull seminal plasma. A Fourier transform infrared study. Biochim. Biophys. Acta 118 (1992) 187-193
-
(1992)
Biochim. Biophys. Acta
, vol.118
, pp. 187-193
-
-
Fini, C.1
Bertoli, E.2
Albertini, G.3
Floridi, A.4
Tanfani, F.5
-
15
-
-
0026443750
-
Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studies by Fourier-transform infrared spectroscopy
-
Fernandez-Ballester G., Castresana J., Arrondo J.L.R., Ferragut J.A., and Gonzalez-Ros J.M. Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studies by Fourier-transform infrared spectroscopy. Biochem. J. 288 (1992) 421-426
-
(1992)
Biochem. J.
, vol.288
, pp. 421-426
-
-
Fernandez-Ballester, G.1
Castresana, J.2
Arrondo, J.L.R.3
Ferragut, J.A.4
Gonzalez-Ros, J.M.5
-
16
-
-
1642546383
-
Computation and analysis of protein circular dichroism spectra
-
Sreerama N., and Woody R.W. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 383 (2004) 318-351
-
(2004)
Methods Enzymol.
, vol.383
, pp. 318-351
-
-
Sreerama, N.1
Woody, R.W.2
-
17
-
-
0027958069
-
The use of fluorescence methods to monitor unfolding transitions in proteins
-
Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66 (1994) 482-501
-
(1994)
Biophys. J.
, vol.66
, pp. 482-501
-
-
Eftink, M.R.1
-
18
-
-
33845405623
-
-
Mitra, D. and Das, A.K. (2006) Site directed mutagenesis and kinetic analysis of Peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis reveal Cyclosporin A sensitivity on its catalytic activity. Biochem. J. (submitted).
-
-
-
-
19
-
-
0003286597
-
DICHROWEB: a website for the analysis of protein secondary structure from circular dichroism spectra
-
Lobley A., and Wallace B.A. DICHROWEB: a website for the analysis of protein secondary structure from circular dichroism spectra. Biophys. J. 80 (2001) 373a
-
(2001)
Biophys. J.
, vol.80
-
-
Lobley, A.1
Wallace, B.A.2
-
20
-
-
3242877618
-
DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
-
Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acid Res. 32 (2004) 668-673
-
(2004)
Nucleic Acid Res.
, vol.32
, pp. 668-673
-
-
Whitmore, L.1
Wallace, B.A.2
-
21
-
-
0036168995
-
DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism data
-
Lobley A., Whitmore L., and Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism data. Bioinformatics 18 (2002) 211-212
-
(2002)
Bioinformatics
, vol.18
, pp. 211-212
-
-
Lobley, A.1
Whitmore, L.2
Wallace, B.A.3
-
22
-
-
0025271463
-
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
-
Pace C.N., Laurents D.V., and Thomson J.A. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29 (1990) 2564-2572
-
(1990)
Biochemistry
, vol.29
, pp. 2564-2572
-
-
Pace, C.N.1
Laurents, D.V.2
Thomson, J.A.3
-
23
-
-
0027407353
-
Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase
-
Morjana N.A., McKeone B.J., and Gilbert H.F. Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Proc. Natl. Acad. Sci. USA 90 (1993) 2107-2111
-
(1993)
Proc. Natl. Acad. Sci. USA
, vol.90
, pp. 2107-2111
-
-
Morjana, N.A.1
McKeone, B.J.2
Gilbert, H.F.3
-
24
-
-
0031852954
-
Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
-
Flora K., Brennan J.D., Baker G.A., Doody M.A., and Bright F.V. Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys. J. 75 (1998) 1084-1096
-
(1998)
Biophys. J.
, vol.75
, pp. 1084-1096
-
-
Flora, K.1
Brennan, J.D.2
Baker, G.A.3
Doody, M.A.4
Bright, F.V.5
-
26
-
-
0029018548
-
The use and misuse of FTIR in the determination of protein structure
-
Jackson M., and Mantsch H.H. The use and misuse of FTIR in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30 2 (1995) 95-120
-
(1995)
Crit. Rev. Biochem. Mol. Biol.
, vol.30
, Issue.2
, pp. 95-120
-
-
Jackson, M.1
Mantsch, H.H.2
-
27
-
-
10844275618
-
Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability
-
D'Auria S., Scire A., Varriale A., Scognamiglio V., Staiano M., Ausili A., Marabotti A., Rossi M., and Tanfani F. Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability. Proteins 58 (2005) 80-87
-
(2005)
Proteins
, vol.58
, pp. 80-87
-
-
D'Auria, S.1
Scire, A.2
Varriale, A.3
Scognamiglio, V.4
Staiano, M.5
Ausili, A.6
Marabotti, A.7
Rossi, M.8
Tanfani, F.9
-
28
-
-
0025357111
-
Protein secondary structures in water from second-derivative amide I infrared spectra
-
Dong A.C., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
-
(1990)
Biochemistry
, vol.29
, pp. 3303-3308
-
-
Dong, A.C.1
Huang, P.2
Caughey, W.S.3
-
29
-
-
0021115861
-
Protein structure by Fourier transform infrared spectroscopy: second derivative spectra
-
Susi H., and Byler D.M. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Biochem. Biophys. Res. Commun. 115 (1983) 391-397
-
(1983)
Biochem. Biophys. Res. Commun.
, vol.115
, pp. 391-397
-
-
Susi, H.1
Byler, D.M.2
-
30
-
-
0022463740
-
Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
-
Susi H., and Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130 (1986) 290-311
-
(1986)
Methods Enzymol.
, vol.130
, pp. 290-311
-
-
Susi, H.1
Byler, D.M.2
-
31
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
-
Santoro M.M., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
32
-
-
0019593952
-
Fluorescence quenching studies with proteins
-
Eftink M.R., and Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114 (1981) 199-227
-
(1981)
Anal. Biochem.
, vol.114
, pp. 199-227
-
-
Eftink, M.R.1
Ghiron, C.A.2
-
34
-
-
0022691315
-
Examination of the secondary structure of proteins by deconvolved FT-IR spectra
-
Byler D., and Susi H. Examination of the secondary structure of proteins by deconvolved FT-IR spectra. Biopolymers 25 (1986) 469-487
-
(1986)
Biopolymers
, vol.25
, pp. 469-487
-
-
Byler, D.1
Susi, H.2
-
35
-
-
0027141955
-
Structural investigation of transglutaminase by Fourier transform infrared spectroscopy
-
Tanfani F., Bertoli E., Signorini M., and Bergamini C.M. Structural investigation of transglutaminase by Fourier transform infrared spectroscopy. Eur. J. Biochem. 218 (1993) 499-505
-
(1993)
Eur. J. Biochem.
, vol.218
, pp. 499-505
-
-
Tanfani, F.1
Bertoli, E.2
Signorini, M.3
Bergamini, C.M.4
-
36
-
-
0028948157
-
Surface-core relationships in human low-density lipoprotein as studied by infrared spectroscopy
-
Banuelos S., Arrondo J.L., Goni F.M., and Pifat G. Surface-core relationships in human low-density lipoprotein as studied by infrared spectroscopy. J. Biol. Chem. 270 (1995) 9192-9196
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 9192-9196
-
-
Banuelos, S.1
Arrondo, J.L.2
Goni, F.M.3
Pifat, G.4
-
38
-
-
0026516588
-
Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies
-
Jackson M., and Mantsch H.H. Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochem. Biophys. Acta 1118 (1992) 139-143
-
(1992)
Biochem. Biophys. Acta
, vol.1118
, pp. 139-143
-
-
Jackson, M.1
Mantsch, H.H.2
-
39
-
-
0015230409
-
Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion
-
Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10 (1971) 3254-3263
-
(1971)
Biochemistry
, vol.10
, pp. 3254-3263
-
-
Lehrer, S.S.1
-
40
-
-
0001917250
-
Fluorescence quenching
-
Lacowicz J.R. (Ed), Plenum Press, New York
-
Eftink M.R. Fluorescence quenching. In: Lacowicz J.R. (Ed). Topics in Fluorescence Spectroscopy Vol. II (2000), Plenum Press, New York 53-85
-
(2000)
Topics in Fluorescence Spectroscopy
, vol.II
, pp. 53-85
-
-
Eftink, M.R.1
-
41
-
-
0032569033
-
Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process
-
Cordier-Ochsenbein F., Guerois R., Russo-Marie F.E., Neumann J.M., and Sanson A. Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process. J. Mol. Biol. 279 (1998) 1177-1185
-
(1998)
J. Mol. Biol.
, vol.279
, pp. 1177-1185
-
-
Cordier-Ochsenbein, F.1
Guerois, R.2
Russo-Marie, F.E.3
Neumann, J.M.4
Sanson, A.5
-
42
-
-
29644435021
-
Multiple unfolding states of glutathione transferase from Physa acuta (Gastropoda: Physidae)
-
Abdalla A.-M., and Hamed R.R. Multiple unfolding states of glutathione transferase from Physa acuta (Gastropoda: Physidae). Biochem. Biophys. Res. Commun. 340 (2006) 625-632
-
(2006)
Biochem. Biophys. Res. Commun.
, vol.340
, pp. 625-632
-
-
Abdalla, A.-M.1
Hamed, R.R.2
-
43
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfisen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfisen, C.B.1
-
44
-
-
0028606077
-
Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation
-
Neet K.E., and Timm D.E. Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci. 3 (1994) 2167-2174
-
(1994)
Protein Sci.
, vol.3
, pp. 2167-2174
-
-
Neet, K.E.1
Timm, D.E.2
-
45
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-217
-
(1995)
Adv. Protein Chem.
, vol.47
, pp. 83-217
-
-
Ptitsyn, O.B.1
-
46
-
-
0028917296
-
Structure of folding intermediates
-
Ptitsyn O.B. Structure of folding intermediates. Curr. Opin. Struct. Biol. 5 (1995) 74-78
-
(1995)
Curr. Opin. Struct. Biol.
, vol.5
, pp. 74-78
-
-
Ptitsyn, O.B.1
-
47
-
-
0032498239
-
Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding
-
Staniforth R.A., Bigotti M.G., Cutruzzola F., Travaglini C., and Brunori M. Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding. J. Mol. Biol. 275 (1998) 133-148
-
(1998)
J. Mol. Biol.
, vol.275
, pp. 133-148
-
-
Staniforth, R.A.1
Bigotti, M.G.2
Cutruzzola, F.3
Travaglini, C.4
Brunori, M.5
|