-
1
-
-
0024295023
-
Triosephosphate isomerase catalysis is diffusion controlled
-
Blacklow S.C., Raines R.T., Lim W.A., Zamore P.D., and Knowles J.R. Triosephosphate isomerase catalysis is diffusion controlled. Biochemistry 27 (1988) 1158-1167
-
(1988)
Biochemistry
, vol.27
, pp. 1158-1167
-
-
Blacklow, S.C.1
Raines, R.T.2
Lim, W.A.3
Zamore, P.D.4
Knowles, J.R.5
-
2
-
-
0025276041
-
Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase
-
Pompliano D.L., Peyman A., and Knowles J.R. Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry 29 (1990) 3186-3194
-
(1990)
Biochemistry
, vol.29
, pp. 3186-3194
-
-
Pompliano, D.L.1
Peyman, A.2
Knowles, J.R.3
-
3
-
-
0022981913
-
Loops in globular-proteins - a novel category of secondary structure
-
Leszczynski J.F., and Rose G.D. Loops in globular-proteins - a novel category of secondary structure. Science 234 (1986) 849-855
-
(1986)
Science
, vol.234
, pp. 849-855
-
-
Leszczynski, J.F.1
Rose, G.D.2
-
4
-
-
0029070171
-
Protein motifs .6. omega-loops - nonregular secondary structures significant in protein function and stability
-
Fetrow J.S. Protein motifs .6. omega-loops - nonregular secondary structures significant in protein function and stability. FASEB J. 9 (1995) 708-717
-
(1995)
FASEB J.
, vol.9
, pp. 708-717
-
-
Fetrow, J.S.1
-
5
-
-
0025882959
-
Structure of the triosephosphate isomerase-phosphoglycohydroxamate complex: an analog of the intermediate on the reaction pathway
-
Davenport R.C., Bash P.A., Seaton B.A., Karplus M., Petsko G.A., and Ringe D. Structure of the triosephosphate isomerase-phosphoglycohydroxamate complex: an analog of the intermediate on the reaction pathway. Biochemistry 30 (1991) 5821-5826
-
(1991)
Biochemistry
, vol.30
, pp. 5821-5826
-
-
Davenport, R.C.1
Bash, P.A.2
Seaton, B.A.3
Karplus, M.4
Petsko, G.A.5
Ringe, D.6
-
6
-
-
0037422593
-
Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2 Å resolution
-
Jogl G., Rozovsky S., McDermott A.E., and Tong L. Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2 Å resolution. Proc. Natl Acad. Sci. USA 100 (2003) 50-55
-
(2003)
Proc. Natl Acad. Sci. USA
, vol.100
, pp. 50-55
-
-
Jogl, G.1
Rozovsky, S.2
McDermott, A.E.3
Tong, L.4
-
7
-
-
0037984337
-
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83 Å resolution
-
Kursula I., and Wierenga R.K. Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83 Å resolution. J. Biol. Chem. 278 (2003) 9544-9551
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 9544-9551
-
-
Kursula, I.1
Wierenga, R.K.2
-
8
-
-
0031972864
-
The loop opening/closing motion of the enzyme triosephosphate isomerase
-
Derreumaux P., and Schlick T. The loop opening/closing motion of the enzyme triosephosphate isomerase. Biophys. J. 74 (1998) 72-81
-
(1998)
Biophys. J.
, vol.74
, pp. 72-81
-
-
Derreumaux, P.1
Schlick, T.2
-
9
-
-
1442277682
-
Computational modeling of the catalytic reaction in triosephosphate isomerase
-
Guallar V., Jacobson M., McDermott A., and Friesner R.A. Computational modeling of the catalytic reaction in triosephosphate isomerase. J. Mol. Biol. 337 (2004) 227-239
-
(2004)
J. Mol. Biol.
, vol.337
, pp. 227-239
-
-
Guallar, V.1
Jacobson, M.2
McDermott, A.3
Friesner, R.A.4
-
10
-
-
0029000872
-
Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated
-
Williams J.C., and McDermott A.E. Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34 (1995) 8309-8319
-
(1995)
Biochemistry
, vol.34
, pp. 8309-8319
-
-
Williams, J.C.1
McDermott, A.E.2
-
11
-
-
0035967901
-
The time scale of the catalytic loop motion in triosephosphate isomerase
-
Rozovsky S., and McDermott A.E. The time scale of the catalytic loop motion in triosephosphate isomerase. J. Mol. Biol. 310 (2001) 259-270
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 259-270
-
-
Rozovsky, S.1
McDermott, A.E.2
-
12
-
-
0035967856
-
Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics
-
Rozovsky S., Jogl G., Tong L., and McDermott A.E. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310 (2001) 271-280
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 271-280
-
-
Rozovsky, S.1
Jogl, G.2
Tong, L.3
McDermott, A.E.4
-
13
-
-
0345894320
-
Active site loop motion in triosephosphate isomerase: T-jump relaxation spectrsocopy of thermal activation
-
Desamero R., Rozovsky S., Zhadin N., McDermott A., and Callender R. Active site loop motion in triosephosphate isomerase: T-jump relaxation spectrsocopy of thermal activation. Biochemistry 42 (2003) 2941-2951
-
(2003)
Biochemistry
, vol.42
, pp. 2941-2951
-
-
Desamero, R.1
Rozovsky, S.2
Zhadin, N.3
McDermott, A.4
Callender, R.5
-
14
-
-
0041866694
-
Mapping chemical exchange in proteins with MW > 50 kDa
-
Wang C., Rance M., and Palmer A.G. Mapping chemical exchange in proteins with MW > 50 kDa. J. Am. Chem. Soc. 125 (2003) 8968-8969
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 8968-8969
-
-
Wang, C.1
Rance, M.2
Palmer, A.G.3
-
15
-
-
33748511877
-
Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase
-
Massi F., Wang C., and Palmer A.G. Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry 45 (2006) 10787-10794
-
(2006)
Biochemistry
, vol.45
, pp. 10787-10794
-
-
Massi, F.1
Wang, C.2
Palmer, A.G.3
-
16
-
-
0025015392
-
Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop
-
Joseph D., Petsko G.A., and Karplus M. Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science 249 (1990) 1425-1428
-
(1990)
Science
, vol.249
, pp. 1425-1428
-
-
Joseph, D.1
Petsko, G.A.2
Karplus, M.3
-
17
-
-
0025882523
-
The adaptability of the active-site of trypanosomal triosephosphate isomerase as observed in the crystal-structures of 3 different complexes
-
Noble M.E.M., Wierenga R.K., Lambeir A.M., Opperdoes F.R., Thunnissen A., Kalk K.H., et al. The adaptability of the active-site of trypanosomal triosephosphate isomerase as observed in the crystal-structures of 3 different complexes. Proteins: Struct. Funct. Genet. 10 (1991) 50-69
-
(1991)
Proteins: Struct. Funct. Genet.
, vol.10
, pp. 50-69
-
-
Noble, M.E.M.1
Wierenga, R.K.2
Lambeir, A.M.3
Opperdoes, F.R.4
Thunnissen, A.5
Kalk, K.H.6
-
18
-
-
0025331920
-
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5 Å resolution: implications for catalysis
-
Lolis E., and Petsko G.A. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5 Å resolution: implications for catalysis. Biochemistry 29 (1990) 6619-6625
-
(1990)
Biochemistry
, vol.29
, pp. 6619-6625
-
-
Lolis, E.1
Petsko, G.A.2
-
19
-
-
0026782489
-
Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase
-
Sampson N.S., and Knowles J.R. Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry 31 (1992) 8488-8494
-
(1992)
Biochemistry
, vol.31
, pp. 8488-8494
-
-
Sampson, N.S.1
Knowles, J.R.2
-
20
-
-
4143134253
-
Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
-
Kursula I., Salin M., Sun J., Norledge B.V., Haapalainen A.M., Sampson N.S., and Wierenga R.K. Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. Protein Eng. Des. Select. 17 (2004) 375-382
-
(2004)
Protein Eng. Des. Select.
, vol.17
, pp. 375-382
-
-
Kursula, I.1
Salin, M.2
Sun, J.3
Norledge, B.V.4
Haapalainen, A.M.5
Sampson, N.S.6
Wierenga, R.K.7
-
21
-
-
0031820040
-
Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase
-
Sun J., and Sampson N.S. Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase. Protein Sci. 7 (1998) 1495-1505
-
(1998)
Protein Sci.
, vol.7
, pp. 1495-1505
-
-
Sun, J.1
Sampson, N.S.2
-
22
-
-
0035815109
-
The importance of hinge sequences for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase
-
Xiang J., Sun J., and Sampson N.S. The importance of hinge sequences for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. J. Mol. Biol. 307 (2001) 1103-1112
-
(2001)
J. Mol. Biol.
, vol.307
, pp. 1103-1112
-
-
Xiang, J.1
Sun, J.2
Sampson, N.S.3
-
23
-
-
0033621030
-
Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase
-
Sun J., and Sampson N.S. Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase. Biochemistry 38 (1999) 11474-11481
-
(1999)
Biochemistry
, vol.38
, pp. 11474-11481
-
-
Sun, J.1
Sampson, N.S.2
-
24
-
-
4444321214
-
Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase
-
Xiang J., Jung J., and Sampson N.S. Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase. Biochemistry 43 (2004) 11436-11445
-
(2004)
Biochemistry
, vol.43
, pp. 11436-11445
-
-
Xiang, J.1
Jung, J.2
Sampson, N.S.3
-
25
-
-
49549135300
-
Atomic coordinates for triose phosphate isomerase from chicken muscle
-
Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., and Wilson I.A. Atomic coordinates for triose phosphate isomerase from chicken muscle. Biochem. Biophys. Res. Commun. 72 (1976) 146-155
-
(1976)
Biochem. Biophys. Res. Commun.
, vol.72
, pp. 146-155
-
-
Banner, D.W.1
Bloomer, A.C.2
Petsko, G.A.3
Phillips, D.C.4
Wilson, I.A.5
-
26
-
-
0028209049
-
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycohydroxamate complex at 1.8 Å resolution
-
Zhang Z., Sugio S., Komives E.A., Liu K.D., Knowles J.R., Petsko G.A., and Ringe D. Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycohydroxamate complex at 1.8 Å resolution. Biochemistry 33 (1994) 2830-2837
-
(1994)
Biochemistry
, vol.33
, pp. 2830-2837
-
-
Zhang, Z.1
Sugio, S.2
Komives, E.A.3
Liu, K.D.4
Knowles, J.R.5
Petsko, G.A.6
Ringe, D.7
-
27
-
-
0030612833
-
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
-
Pervushin K., Riek R., Wider G., and Wuthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl Acad. Sci. USA 94 (1997) 12366-12371
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 12366-12371
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wuthrich, K.4
-
28
-
-
0033226859
-
Transverse-relaxation-optimized (TROSY) gradient-enhnaced triple-resonance NMR spectroscopy
-
Loria J.P., Rance M., and Palmer A.G. Transverse-relaxation-optimized (TROSY) gradient-enhnaced triple-resonance NMR spectroscopy. J. Magn. Reson. 141 (1999) 180-184
-
(1999)
J. Magn. Reson.
, vol.141
, pp. 180-184
-
-
Loria, J.P.1
Rance, M.2
Palmer, A.G.3
-
29
-
-
0034836367
-
Sequence-dependent correction of random coil NMR chemical shifts
-
Schwarzinger S., Kroon G.J.A., Foss T.R., Chung J., Wright P.E., and Dyson H.J. Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123 (2001) 2970-2978
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 2970-2978
-
-
Schwarzinger, S.1
Kroon, G.J.A.2
Foss, T.R.3
Chung, J.4
Wright, P.E.5
Dyson, H.J.6
-
30
-
-
0033794319
-
Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView
-
Schwarzinger S., Kroon G.J.A., 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.A.2
Foss, T.R.3
Wright, P.E.4
Dyson, H.J.5
-
31
-
-
0029795040
-
The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR
-
Grzesiek S., Stahl S.J., Wingfield P.T., and Bax A. The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry 35 (1996) 10256-10261
-
(1996)
Biochemistry
, vol.35
, pp. 10256-10261
-
-
Grzesiek, S.1
Stahl, S.J.2
Wingfield, P.T.3
Bax, A.4
-
32
-
-
0027242141
-
Structures of the 'open' and 'closed' state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
-
Noble M.E.M., Zeelen J.P., and Wierenga R.K. Structures of the 'open' and 'closed' state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism. Proteins: Struct. Funct. Genet. 16 (1993) 311-326
-
(1993)
Proteins: Struct. Funct. Genet.
, vol.16
, pp. 311-326
-
-
Noble, M.E.M.1
Zeelen, J.P.2
Wierenga, R.K.3
-
33
-
-
0141611780
-
Protein dynamics from solution NMR: theory and applications
-
Kempf J.G., and Loria J.P. Protein dynamics from solution NMR: theory and applications. Cell Biochem. Biophys. 39 (2002) 187-212
-
(2002)
Cell Biochem. Biophys.
, vol.39
, pp. 187-212
-
-
Kempf, J.G.1
Loria, J.P.2
-
34
-
-
0034328380
-
HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
-
de la Torre J.G., Huertas M.L., and Carrasco B. HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. J. Magn. Reson. 147 (2000) 138-146
-
(2000)
J. Magn. Reson.
, vol.147
, pp. 138-146
-
-
de la Torre, J.G.1
Huertas, M.L.2
Carrasco, B.3
-
36
-
-
0032719427
-
A TROSY CPMG Sequence for characterizing chemical exchange in large proteins
-
Loria J.P., Rance M., and Palmer A.G. A TROSY CPMG Sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15 (1999) 151-155
-
(1999)
J. Biomol. NMR
, vol.15
, pp. 151-155
-
-
Loria, J.P.1
Rance, M.2
Palmer, A.G.3
-
39
-
-
0034868445
-
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
-
Stone M.J. NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding. Acc. Chem. Res. 34 (2001) 379-388
-
(2001)
Acc. Chem. Res.
, vol.34
, pp. 379-388
-
-
Stone, M.J.1
-
40
-
-
33646911358
-
Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
-
Jarymowycz V.A., and Stone M.J. Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem. Rev. 106 (2006) 1624-1671
-
(2006)
Chem. Rev.
, vol.106
, pp. 1624-1671
-
-
Jarymowycz, V.A.1
Stone, M.J.2
-
41
-
-
2542487312
-
Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes
-
Butterwick J.A., Loria J.P., Astrof N.S., Kroenke C.D., Cole R., Rance M., and Palmer III A.G. Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes. J. Mol. Biol. 339 (2004) 855-871
-
(2004)
J. Mol. Biol.
, vol.339
, pp. 855-871
-
-
Butterwick, J.A.1
Loria, J.P.2
Astrof, N.S.3
Kroenke, C.D.4
Cole, R.5
Rance, M.6
Palmer III, A.G.7
-
42
-
-
0015956852
-
Studies on subunit structure and amino-acid sequence of triose phosphate isomerase from chicken breast muscle
-
Furth A.J., Milman J.D., Priddle J.D., and Offord R.E. Studies on subunit structure and amino-acid sequence of triose phosphate isomerase from chicken breast muscle. Biochem. J. 139 (1974) 11-25
-
(1974)
Biochem. J.
, vol.139
, pp. 11-25
-
-
Furth, A.J.1
Milman, J.D.2
Priddle, J.D.3
Offord, R.E.4
-
43
-
-
0000154206
-
The colorimetric determination of phosphorous
-
Fiske C.H., and Subbarow Y. The colorimetric determination of phosphorous. J. Biol. Chem. 66 (1925) 375-400
-
(1925)
J. Biol. Chem.
, vol.66
, pp. 375-400
-
-
Fiske, C.H.1
Subbarow, Y.2
-
44
-
-
0014681301
-
Transition state analogues for enzyme catalysis
-
Wolfenden R. Transition state analogues for enzyme catalysis. Nature 223 (1969) 704-705
-
(1969)
Nature
, vol.223
, pp. 704-705
-
-
Wolfenden, R.1
-
45
-
-
21244440196
-
Conservation of mu s-ms enzyme motions in the apo- and substrate-mimicked state
-
Beach H., Cole R., Gill M.L., and Loria J.P. Conservation of mu s-ms enzyme motions in the apo- and substrate-mimicked state. J. Am. Chem. Soc. 127 (2005) 9167-9176
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 9167-9176
-
-
Beach, H.1
Cole, R.2
Gill, M.L.3
Loria, J.P.4
-
46
-
-
0029400480
-
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
-
Delaglio F., Grzesiak S., Vuister G., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiak, S.2
Vuister, G.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
48
-
-
24344440618
-
Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO)
-
Eghbalnia H.R., Bahrami A., Wang L.Y., Assadi A., and Markley J.L. Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO). J. Biomol. NMR 32 (2005) 219-233
-
(2005)
J. Biomol. NMR
, vol.32
, pp. 219-233
-
-
Eghbalnia, H.R.1
Bahrami, A.2
Wang, L.Y.3
Assadi, A.4
Markley, J.L.5
-
49
-
-
0034170879
-
Protein dynamics measurements by TROSY-based NMR experiments
-
Zhu G., Xia Y., Nicholson L.K., and Sze K.H. Protein dynamics measurements by TROSY-based NMR experiments. J. Magn. Reson. 143 (2000) 423-426
-
(2000)
J. Magn. Reson.
, vol.143
, pp. 423-426
-
-
Zhu, G.1
Xia, Y.2
Nicholson, L.K.3
Sze, K.H.4
-
51
-
-
33745362452
-
Variability of the N-15 chemical shielding tensors in the B3 domain of protein G from N-15 relaxation measurements at several fields. Implications for backbone order parameters
-
Hall J.B., and Fushman D. Variability of the N-15 chemical shielding tensors in the B3 domain of protein G from N-15 relaxation measurements at several fields. Implications for backbone order parameters. J. Am. Chem. Soc. 128 (2006) 7855-7870
-
(2006)
J. Am. Chem. Soc.
, vol.128
, pp. 7855-7870
-
-
Hall, J.B.1
Fushman, D.2
-
52
-
-
0033520723
-
15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution
-
15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution. J. Am. Chem. Soc. 121 (1999) 10119-10125
-
(1999)
J. Am. Chem. Soc.
, vol.121
, pp. 10119-10125
-
-
Kroenke, C.D.1
Rance, M.2
Palmer, A.G.3
-
53
-
-
0024449503
-
Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
-
Kay L.E., Torchia D.A., and Bax A. Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28 (1989) 8972-8979
-
(1989)
Biochemistry
, vol.28
, pp. 8972-8979
-
-
Kay, L.E.1
Torchia, D.A.2
Bax, A.3
|