-
1
-
-
0024291657
-
Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence
-
Ikura, K., Nasu, T., Yokota, H., Tsuchiya, Y., Sasaki, R., and Chiba, H. (1988) Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence Biochemistry 27, 2898-2905
-
(1988)
Biochemistry
, vol.27
, pp. 2898-2905
-
-
Ikura, K.1
Nasu, T.2
Yokota, H.3
Tsuchiya, Y.4
Sasaki, R.5
Chiba, H.6
-
2
-
-
0018816617
-
Transglutaminases
-
Folk, J. E. (1980) Transglutaminases Annu. Rev. Biochem. 49, 517-531
-
(1980)
Annu. Rev. Biochem.
, vol.49
, pp. 517-531
-
-
Folk, J.E.1
-
3
-
-
0024801107
-
Purification and characterization of a novel transglutaminase derived from microorganisms
-
Ando, H., Adachi, M., Umeda, K., Matsuura, A., Nonaka, M., Uchio, R., Tanaka, H., and Motoki, M. (1989) Purification and characterization of a novel transglutaminase derived from microorganisms Agric. Biol. Chem. 53, 2613
-
(1989)
Agric. Biol. Chem.
, vol.53
, pp. 2613
-
-
Ando, H.1
Adachi, M.2
Umeda, K.3
Matsuura, A.4
Nonaka, M.5
Uchio, R.6
Tanaka, H.7
Motoki, M.8
-
4
-
-
0024851912
-
2+-independent transglutaminase derived from microorganisms
-
Nonaka, M., Tanaka, H., Okayama, A., Motoki, M., Ando, H., Umeda, K., and Matsuura, A. (1989) Polymerization of several proteins by calcium-independent transglutaminase derived from microorganisms Agric. Biol. Chem. 53, 2619-2623 (Pubitemid 20077526)
-
(1989)
Agricultural and Biological Chemistry
, vol.53
, Issue.10
, pp. 2619-2623
-
-
Nonaka, M.1
Tanaka, H.2
Okiyama, A.3
Motoki, M.4
Ando, H.5
Umeda, K.6
Matsuura, A.7
-
5
-
-
2442610049
-
Properties and applications of microbial transglutaminase
-
DOI 10.1007/s00253-003-1539-5
-
Yokoyama, K., Nio, N., and Kikuchi, Y. (2004) Properties and applications of microbial transglutaminase Appl. Microbiol. Biotechnol. 64, 447-454 (Pubitemid 38686152)
-
(2004)
Applied Microbiology and Biotechnology
, vol.64
, Issue.4
, pp. 447-454
-
-
Yokoyama, K.1
Nio, N.2
Kikuchi, Y.3
-
6
-
-
0027223075
-
Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112
-
Kanaji, T., Ozaki, H., Takao, T., Kawajiri, H., Ide, H., Motoki, M., and Shimonishi, Y. (1993) Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112 J. Biol. Chem. 268, 11565-11572 (Pubitemid 23168101)
-
(1993)
Journal of Biological Chemistry
, vol.268
, Issue.16
, pp. 11565-11572
-
-
Kanaji, T.1
Ozaki, H.2
Takao, T.3
Kawajiri, H.4
Ide, H.5
Motoki, M.6
Shimonishi, Y.7
-
7
-
-
0032212390
-
Bacterial pro-transglutaminase from Streptoverticillium mobaraense - Purification, characterisation and sequence of the zymogen
-
DOI 10.1046/j.1432-1327.1998.2570570.x
-
Pasternack, R., Dorsch, S., Otterbach, J. T., Robenek, I. R., Wolf, S., and Fuchsbauer, H. L. (1998) Bacterial pro-transglutaminase from Streptoverticillium mobaraense -purification, characterisation and sequence of the zymogen Eur. J. Biochem. 257, 570-576 (Pubitemid 28512124)
-
(1998)
European Journal of Biochemistry
, vol.257
, Issue.3
, pp. 570-576
-
-
Pasternack, R.1
Dorsch, S.2
Otterbach, J.T.3
Robenek, I.R.4
Wolf, S.5
Fuchsbauer, H.-L.6
-
8
-
-
0037114005
-
Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense
-
DOI 10.1074/jbc.M203933200
-
Kashiwagi, T., Yokoyama, K., Ishikawa, K., Ono, K., Ejima, D., Matsui, H., and Suzuki, E. (2002) Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense J. Biol. Chem. 277, 44252-44260 (Pubitemid 36157858)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.46
, pp. 44252-44260
-
-
Kashiwagi, T.1
Yokoyama, K.-I.2
Ishikawa, K.3
Ono, K.4
Ejima, D.5
Matsui, H.6
Suzuki, E.-I.7
-
9
-
-
0034201598
-
Overproduction of microbial transglutaminase in Escherichia coli, in vitro refolding, and characterization of the refolded form
-
Yokoyama, K. I., Nakamura, N., Seguro, K., and Kubota, K. (2000) Overproduction of microbial transglutaminase in Escherichia coli, in vitro refolding, and characterization of the refolded form Biosci. Biotechnol. Biochem. 64, 1263-1270
-
(2000)
Biosci. Biotechnol. Biochem.
, vol.64
, pp. 1263-1270
-
-
Yokoyama, K.I.1
Nakamura, N.2
Seguro, K.3
Kubota, K.4
-
10
-
-
0036421202
-
In vitro refolding process of urea-denatured microbial transglutaminase without pro-peptide sequence
-
DOI 10.1016/S1046-5928(02)00536-3, PII S1046592802005363
-
Yokoyama, K., Kunio, O., Ohtsuka, T., Nakamura, N., Seguro, K., and Ejima, D. (2002) In vitro refolding process of urea-denatured microbial transglutaminase without pro-peptide sequence Protein Expression Purif. 26, 329-335 (Pubitemid 35326551)
-
(2002)
Protein Expression and Purification
, vol.26
, Issue.2
, pp. 329-335
-
-
Yokoyama, K.-I.1
Kunio, O.2
Ohtsuka, T.3
Nakamura, N.4
Seguro, K.5
Ejima, D.6
-
11
-
-
0027995384
-
Classification of acid denaturation of proteins: Intermediates and unfolded states
-
DOI 10.1021/bi00207a018
-
Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T., and Palleros, D. R. (1994) Classification of acid denaturation of proteins: intermediates and unfolded states Biochemistry 33, 12504-12511 (Pubitemid 24340457)
-
(1994)
Biochemistry
, vol.33
, Issue.41
, pp. 12504-12511
-
-
Fink, A.L.1
Calciano, L.J.2
Goto, Y.3
Kurotsu, T.4
Palleros, D.R.5
-
12
-
-
0021114569
-
Molten-globule state': A compact form of globular proteins with mobile side-chains
-
Ohgushi, M. and Wada, A. (1983) Molten-globule state': a compact form of globular proteins with mobile side-chains FEBS Lett. 164, 21-24
-
(1983)
FEBS Lett.
, vol.164
, pp. 21-24
-
-
Ohgushi, M.1
Wada, A.2
-
13
-
-
0023657937
-
Sequential mechanism of refolding of carbonic anhydrase B
-
Semisotnov, G. V., Rodionova, N. A., Kutyshenko, V. P., Ebert, B., Blanck, J., and Ptitsyn, O. B. (1987) Sequential mechanism of refolding of carbonic anhydrase B FEBS Lett. 224, 9-13
-
(1987)
FEBS Lett.
, vol.224
, pp. 9-13
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Kutyshenko, V.P.3
Ebert, B.4
Blanck, J.5
Ptitsyn, O.B.6
-
14
-
-
0034581327
-
Role of the molten globule state in protein folding
-
DOI 10.1016/S0065-3233(00)53005-8
-
Arai, M. and Kuwajima, K. (2000) Role of the molten globule state in protein folding Adv. Protein Chem. 53, 209-282 (Pubitemid 34194295)
-
(2000)
Advances in Protein Chemistry
, vol.53
, pp. 209-282
-
-
Arai, M.1
Kuwajima, K.2
-
15
-
-
0014011698
-
Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: Identification of a functional cysteine essential for activity
-
Folk, J. E. and Cole, P. W. (1966) Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity J. Biol. Chem. 241, 5518-5525
-
(1966)
J. Biol. Chem.
, vol.241
, pp. 5518-5525
-
-
Folk, J.E.1
Cole, P.W.2
-
16
-
-
0028871804
-
How to measure and predict the molar absorption coefficient of a protein
-
Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4, 2411-2423
-
(1995)
Protein Sci.
, vol.4
, pp. 2411-2423
-
-
Pace, C.N.1
Vajdos, F.2
Fee, L.3
Grimsley, G.4
Gray, T.5
-
17
-
-
0042127167
-
Structure of folding intermediates at pH 4.0 and native state of microbial transglutaminase
-
Yokoyama, K., Ejima, D., Kita, Y., Philo, J. S., and Arakawa, T. (2003) Structure of folding intermediates at pH 4.0 and native state of microbial transglutaminase Biosci. Biotechnol. Biochem. 67, 291-294 (Pubitemid 39251980)
-
(2003)
Bioscience, Biotechnology and Biochemistry
, vol.67
, Issue.2
, pp. 291-294
-
-
Yokoyama, K.-I.1
Ejima, D.2
Kita, Y.3
Philo, J.S.4
Arakawa, T.5
-
18
-
-
0013800421
-
The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
-
Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites J. Mol. Biol. 13, 482-495
-
(1965)
J. Mol. Biol.
, vol.13
, pp. 482-495
-
-
Stryer, L.1
-
19
-
-
0014342841
-
Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates
-
Turner, D. C. and Brand, L. (1968) Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates Biochemistry 7, 3381-3390
-
(1968)
Biochemistry
, vol.7
, pp. 3381-3390
-
-
Turner, D.C.1
Brand, L.2
-
21
-
-
0024963570
-
Conformational states of β-lactamase: Molten-globule states at acidic and alkaline pH with high salt
-
Goto, Y. and Fink, A. L. (1989) Conformational states of β-lactamase: molten-globule states at acidic and alkaline pH with high salt Biochemistry 28, 945-952
-
(1989)
Biochemistry
, vol.28
, pp. 945-952
-
-
Goto, Y.1
Fink, A.L.2
-
22
-
-
34247103661
-
+ reductase revealed by hydrogen/deuterium exchange
-
DOI 10.1074/jbc.M608417200
-
+ reductase revealed by hydrogen/deuterium exchange J. Biol. Chem. 282, 5959-5967 (Pubitemid 47093743)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.8
, pp. 5959-5967
-
-
Lee, Y.-H.1
Tamura, K.2
Maeda, M.3
Hoshino, M.4
Sakurai, K.5
Takahashi, S.6
Ikegami, T.7
Hase, T.8
Goto, Y.9
-
23
-
-
0037184934
-
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle
-
DOI 10.1074/jbc.M209183200
-
Miyazaki, T., Yoshimi, T., Furutsu, Y., Hongo, K., Mizobata, T., Kanemori, M., and Kawata, Y. (2002) GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle J. Biol. Chem. 277, 50621-50628 (Pubitemid 36042222)
-
(2002)
Journal of Biological Chemistry
, vol.277
, Issue.52
, pp. 50621-50628
-
-
Miyazaki, T.1
Yoshimi, T.2
Furutsu, Y.3
Hongo, K.4
Mizobata, T.5
Kanemori, M.6
Kawata, Y.7
-
24
-
-
1142269567
-
Solid-phase refolding of cyclodextrin glycosyltransferase adsorbed on cation-exchange resin
-
Kweon, D. H., Lee, D. H., Han, N. S., and Seo, J. H. (2004) Solid-phase refolding of cyclodextrin glycosyltransferase adsorbed on cation-exchange resin Biotechnol. Prog. 20, 277-283
-
(2004)
Biotechnol. Prog.
, vol.20
, pp. 277-283
-
-
Kweon, D.H.1
Lee, D.H.2
Han, N.S.3
Seo, J.H.4
-
25
-
-
0141922991
-
A Novel Lipase from Pseudomonas fluorescens HU380: Gene Cloning, Overproduction, Renaturation-Activation, Two-Step Purification, and Characterization
-
DOI 10.1016/S1389-1723(03)80188-3
-
Kojima, Y., Kobayashi, M., and Shimizu, S. (2003) A novel lipase from Pseudomonas fluorescens HU380: gene cloning, overproduction, renaturation-activation, two-step purification, and characterization J. Biosci. Bioeng. 96, 242-249 (Pubitemid 37249210)
-
(2003)
Journal of Bioscience and Bioengineering
, vol.96
, Issue.3
, pp. 242-249
-
-
Kojima, Y.1
Kobayashi, M.2
Shimizu, S.3
-
26
-
-
0016711868
-
Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
-
Brandts, J. F., Halvorson, H. R., and Brennan, M. (1975) Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues Biochemistry 14, 4953-4963
-
(1975)
Biochemistry
, vol.14
, pp. 4953-4963
-
-
Brandts, J.F.1
Halvorson, H.R.2
Brennan, M.3
-
27
-
-
84889841716
-
Prolyl isomerization in protein folding
-
in (Buchner, J. and Kiefhaber, T. Eds.) pp, Wiley-VCH, Weinheim
-
Schmid, F. X. (2005) Prolyl isomerization in protein folding, in Protein Folding Handbook (Buchner, J. and Kiefhaber, T., Eds.) pp 916-945, Wiley-VCH, Weinheim.
-
(2005)
Protein Folding Handbook
, pp. 916-945
-
-
Schmid, F.X.1
-
28
-
-
0019958156
-
Unfolding and refolding of the constant fragment of the immunoglobulin light chain
-
DOI 10.1016/0022-2836(82)90146-2
-
Goto, Y. and Hamaguchi, K. (1982) Unfolding and refolding of the constant fragment of the immunoglobulin light chain J. Mol. Biol. 156, 891-910 (Pubitemid 12055136)
-
(1982)
Journal of Molecular Biology
, vol.156
, Issue.4
, pp. 891-910
-
-
Goto, Y.1
Hamaguchi, K.2
-
29
-
-
0026584375
-
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate
-
Kiefhaber, T., Grunert, H. P., Hahn, U., and Schmid, F. X. (1992) Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate Proteins 12, 171-179
-
(1992)
Proteins
, vol.12
, pp. 171-179
-
-
Kiefhaber, T.1
Grunert, H.P.2
Hahn, U.3
Schmid, F.X.4
-
30
-
-
0025949415
-
Reexamination of the folding of BPTI: Predominance of native intermediates
-
Weissman, J. S. and Kim, P. S. (1991) Reexamination of the folding of BPTI: predominance of native intermediates Science 253, 1386-1393 (Pubitemid 21917286)
-
(1991)
Science
, vol.253
, Issue.5026
, pp. 1386-1393
-
-
Weissman, J.S.1
Kim, P.S.2
-
31
-
-
0013001642
-
How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system: Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment
-
DOI 10.1074/jbc.M212247200
-
Umetsu, M., Tsumoto, K., Hara, M., Ashish, K., Goda, S., Adschiri, T., and Kumagai, I. (2003) How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment J. Biol. Chem. 278, 8979-8987 (Pubitemid 36800375)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.11
, pp. 8979-8987
-
-
Umetsu, M.1
Tsumoto, K.2
Hara, M.3
Ashish, K.4
Goda, S.5
Adschiri, T.6
Kumagai, I.7
-
32
-
-
77950905331
-
Step-wise refolding of recombinant proteins
-
Tsumoto, K., Arakawa, T., and Chen, L. (2010) Step-wise refolding of recombinant proteins Curr. Pharm. Biotechnol. 11, 285-288
-
(2010)
Curr. Pharm. Biotechnol.
, vol.11
, pp. 285-288
-
-
Tsumoto, K.1
Arakawa, T.2
Chen, L.3
-
33
-
-
44449152167
-
Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape
-
DOI 10.1021/bi8001715
-
Yagi, M., Kameda, A., Sakurai, K., Nishimura, C., and Goto, Y. (2008) Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape Biochemistry 47, 5996-6006 (Pubitemid 351770029)
-
(2008)
Biochemistry
, vol.47
, Issue.22
, pp. 5996-6006
-
-
Yagi, M.1
Kameda, A.2
Sakurai, K.3
Nishimura, C.4
Goto, Y.5
-
34
-
-
33751406658
-
On-column refolding and purification of transglutaminase from Streptomyces fradiae expressed as inclusion bodies in Escherichia coli
-
Liu, X. Q., Yang, X. Q., Xie, F. H., Song, L. Y., Zhang, G. Q., and Qian, S. J. (2007) On-column refolding and purification of transglutaminase from Streptomyces fradiae expressed as inclusion bodies in Escherichia coli Protein Expression Purif. 51, 179-186
-
(2007)
Protein Expression Purif.
, vol.51
, pp. 179-186
-
-
Liu, X.Q.1
Yang, X.Q.2
Xie, F.H.3
Song, L.Y.4
Zhang, G.Q.5
Qian, S.J.6
-
35
-
-
0026703205
-
Acid pH-induced conformational changes in bovine liver rhodanese
-
Horowitz, P. M. and Xu, R. (1992) Acid pH-induced conformational changes in bovine liver rhodanese J. Biol. Chem. 267, 19464-19469
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 19464-19469
-
-
Horowitz, P.M.1
Xu, R.2
-
36
-
-
0142169397
-
Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
-
DOI 10.1016/S0014-5793(03)01028-7
-
Nomura, Y., Ikeda, M., Yamaguchi, N., Aoyama, Y., and Akiyoshi, K. (2003) Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone FEBS Lett. 553, 271-276 (Pubitemid 37315616)
-
(2003)
FEBS Letters
, vol.553
, Issue.3
, pp. 271-276
-
-
Nomura, Y.1
Ikeda, M.2
Yamaguchi, N.3
Aoyama, Y.4
Akiyoshi, K.5
-
37
-
-
0029136831
-
Artificial chaperons: Protein refolding via sequential use of detergent and cyclodextrin
-
Rozema, D. and Gellman, S. H. (1995) Artificial chaperons: Protein refolding via sequential use of detergent and cyclodextrin J. Am. Chem. Soc. 117, 2373-2374
-
(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 2373-2374
-
-
Rozema, D.1
Gellman, S.H.2
-
38
-
-
78049277219
-
A novel protein refolding system using lauroyl- l -glutamate as a solubilizing detergent and arginine as a folding assisting agent
-
Kudou, M., Yumioka, R., Ejima, D., Arakawa, T., and Tsumoto, K. (2011) A novel protein refolding system using lauroyl- l -glutamate as a solubilizing detergent and arginine as a folding assisting agent Protein Expression Purif. 75, 46-54
-
(2011)
Protein Expression Purif.
, vol.75
, pp. 46-54
-
-
Kudou, M.1
Yumioka, R.2
Ejima, D.3
Arakawa, T.4
Tsumoto, K.5
|