-
1
-
-
0001062020
-
Metabolism of amino-acids III. Deamination of amino-acids
-
Krebs HA. Metabolism of amino-acids III. Deamination of amino-acids. Biochem J. 29:1935;1620-1625.
-
(1935)
Biochem J
, vol.29
, pp. 1620-1625
-
-
Krebs, H.A.1
-
2
-
-
0000958883
-
Isolierung der prosthetischen gruppe der D-aminosaure oxydase
-
Purification of the prosthetic group of D-amino acid oxidase
-
Warburg O, Christian W. Isolierung der prosthetischen gruppe der D-aminosaure oxydase. Biochem Z. 298:1938;150-155. Purification of the prosthetic group of D-amino acid oxidase.
-
(1938)
Biochem Z
, vol.298
, pp. 150-155
-
-
Warburg, O.1
Christian, W.2
-
3
-
-
0002994415
-
Role of semiquinones in flavoprotein catalysis
-
Massey V, Gibson QH. Role of semiquinones in flavoprotein catalysis. Fed Proc. 23:1964;18-25.
-
(1964)
Fed Proc
, vol.23
, pp. 18-25
-
-
Massey, V.1
Gibson, Q.H.2
-
5
-
-
0029839452
-
2
-
2.
-
2.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 7496-7501
-
-
Mattevi, A.1
Vanoni, M.A.2
Todone, F.3
Rizzi, M.4
Teplyakov, A.5
Coda, A.6
Bolognesi, M.7
Curti, B.8
-
6
-
-
0029780471
-
Three-dimensional structure of porcine kidney D-amino acid oxidase at 3 Å resolution
-
of outstanding interest. The structure of recombinant porcine D-amino acid oxidase is described. The authors emphasise the absence of a residue that could function as the catalytic base postulated in the carboanion mechanism. Although the crystals employed for the crystallographic analysis have different symmetry and are grown under different conditions, the structures of the pig kidney and recombinant enzymes are identical.
-
Mizutani H, Miyahara I, Hirotsu K, Nishima Y, Shiga K, Setoyama C, Miura R. Three-dimensional structure of porcine kidney D-amino acid oxidase at 3 Å resolution. of outstanding interest J. Biochem (Tokyo). 120:1996;14-17 The structure of recombinant porcine D-amino acid oxidase is described. The authors emphasise the absence of a residue that could function as the catalytic base postulated in the carboanion mechanism. Although the crystals employed for the crystallographic analysis have different symmetry and are grown under different conditions, the structures of the pig kidney and recombinant enzymes are identical.
-
(1996)
J. Biochem (Tokyo)
, vol.120
, pp. 14-17
-
-
Mizutani, H.1
Miyahara, I.2
Hirotsu, K.3
Nishima, Y.4
Shiga, K.5
Setoyama, C.6
Miura, R.7
-
7
-
-
0028988978
-
D-serine, an endogenous synaptic modulator: Localization to astrocytes and giutamate-stimulate release
-
Schell MJ, Molliver ME, Snyder SH. D-serine, an endogenous synaptic modulator: localization to astrocytes and giutamate-stimulate release. Proc Natl Acad Sci USA. 92:1995;3948-3952.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 3948-3952
-
-
Schell, M.J.1
Molliver, M.E.2
Snyder, S.H.3
-
8
-
-
0030925616
-
Active site plasticity in D-amino acid oxidase: A crystallographic analysis
-
of special interest. The structure of the complex between reduced DAAO and amino tryptophan and of the covalent adduct with 3-methyl-2-oxobutyric acid show that no substantial conformational changes occur upon enzyme reduction and highlight the role of loop 216-228 in substrate binding.
-
Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. of special interest Biochemistry. 36:1997;5853-5860 The structure of the complex between reduced DAAO and amino tryptophan and of the covalent adduct with 3-methyl-2-oxobutyric acid show that no substantial conformational changes occur upon enzyme reduction and highlight the role of loop 216-228 in substrate binding.
-
(1997)
Biochemistry
, vol.36
, pp. 5853-5860
-
-
Todone, F.1
Vanoni, M.A.2
Mozzarelli, A.3
Bolognesi, M.4
Coda, A.5
Curti, B.6
Mattevi, A.7
-
9
-
-
0024601564
-
Mechanisms of flavoprotein-catalyzed reactions
-
Ghisla S, Massey V. Mechanisms of flavoprotein-catalyzed reactions. Eur J Biochem. 181:1989;1-17.
-
(1989)
Eur J Biochem
, vol.181
, pp. 1-17
-
-
Ghisla, S.1
Massey, V.2
-
10
-
-
45549117277
-
The reaction mechanism of D-amino acid oxidase: Concerted or not concerted?
-
Miura R, Miyake L. The reaction mechanism of D-amino acid oxidase: concerted or not concerted? Bioorgan Chem. 16:1988;97-110.
-
(1988)
Bioorgan Chem
, vol.16
, pp. 97-110
-
-
Miura, R.1
Miyake, L.2
-
11
-
-
0016715866
-
Use of 5-deaza FAD to study hydrogen transfer in the D-amino acid oxidase reaction
-
Hersh LB, Schuman Jorns M. Use of 5-deaza FAD to study hydrogen transfer in the D-amino acid oxidase reaction. J Biol Chem. 250:1975;8728-8732.
-
(1975)
J Biol Chem
, vol.250
, pp. 8728-8732
-
-
Hersh, L.B.1
Schuman Jorns, M.2
-
12
-
-
0028113910
-
Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228
-
Pollegioni L, Fukui K, Massey V. Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228. J Biol Chem. 269:1994;31666-31673.
-
(1994)
J Biol Chem
, vol.269
, pp. 31666-31673
-
-
Pollegioni, L.1
Fukui, K.2
Massey, V.3
-
13
-
-
0031054686
-
On the mechanism of D-amino acid oxidase
-
of special interest. The kinetic mechanism of the reaction of yeast D-amino acid oxidase with substituted phenylglycines is discussed in detail. The new data are consistent with a hydride transfer mechanism, in agreement with the structural data.
-
Pollegioni L, Blodig W, Ghisla S. On the mechanism of D-amino acid oxidase. of special interest J Biol Chem. 272:1997;4924-4934 The kinetic mechanism of the reaction of yeast D-amino acid oxidase with substituted phenylglycines is discussed in detail. The new data are consistent with a hydride transfer mechanism, in agreement with the structural data.
-
(1997)
J Biol Chem
, vol.272
, pp. 4924-4934
-
-
Pollegioni, L.1
Blodig, W.2
Ghisla, S.3
-
14
-
-
0024421234
-
Substrate binding and catalysis by gluthathione reductase as derived from refined enzyme: Substrate crystal structures at 2 Å resolution
-
Karplus PA, Schulz GE. Substrate binding and catalysis by gluthathione reductase as derived from refined enzyme: substrate crystal structures at 2 Å resolution. J Mol Biol. 210:1989;163-180.
-
(1989)
J Mol Biol
, vol.210
, pp. 163-180
-
-
Karplus, P.A.1
Schulz, G.E.2
-
15
-
-
0029068515
-
The three-dimensional structure of NAD(P)H: Quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
-
Li R, Bianchet MA, Talalay P, Amzel LM. The three-dimensional structure of NAD(P)H: quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA. 92:1995;8846-8850.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 8846-8850
-
-
Li, R.1
Bianchet, M.A.2
Talalay, P.3
Amzel, L.M.4
-
16
-
-
0027304244
-
Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
-
Kim J, Wang M, Paschke R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc Natl Acad Sci USA. 90:1993;7523-7527.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 7523-7527
-
-
Kim, J.1
Wang, M.2
Paschke, R.3
-
17
-
-
0029822206
-
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: Influence of the location of the catalytic base on substrate specificity
-
of outstanding interest. The crystal structures of the human acyl-CoA dehydrogenase in the wild-type and mutant forms beautifully reveal that the enzyme substrate specificity is determined by the position of the active-site base within the catalytic centre.
-
Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJP. Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. of outstanding interest Biochemistry. 35:1996;12412-12420 The crystal structures of the human acyl-CoA dehydrogenase in the wild-type and mutant forms beautifully reveal that the enzyme substrate specificity is determined by the position of the active-site base within the catalytic centre.
-
(1996)
Biochemistry
, vol.35
, pp. 12412-12420
-
-
Lee, H.J.1
Wang, M.2
Paschke, R.3
Nandy, A.4
Ghisla, S.5
Kim, J.J.P.6
-
18
-
-
0029040665
-
Structure and mechanism of action of the acyl-CoA dehydrogenases
-
Thorpe C, Kim JJP. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9:1995;718-725.
-
(1995)
FASEB J
, vol.9
, pp. 718-725
-
-
Thorpe, C.1
Kim, J.J.P.2
-
19
-
-
0029056202
-
An enzyme-substrate complex involved in bacterial cell wall biosynthesis
-
Benson TE, Filman DJ, Walsh CT, Hogle JM. An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat Struct Biol. 2:1995;644-653.
-
(1995)
Nat Struct Biol
, vol.2
, pp. 644-653
-
-
Benson, T.E.1
Filman, D.J.2
Walsh, C.T.3
Hogle, J.M.4
-
20
-
-
0031047397
-
Kinetic characterisation of wild-type and S229A mutant MurB: Role of Ser229 as a general acid
-
of outstanding interest. The outcomes of protein engineering experiments are discussed on the basis of the known 3D structure of MurB, thus providing a comprehensive picture of the mechanism of the MurB-catalysed reaction.
-
Benson TE, Walsh CT, Massey V. Kinetic characterisation of wild-type and S229A mutant MurB: role of Ser229 as a general acid. of outstanding interest Biochemistry. 36:1997;796-805 The outcomes of protein engineering experiments are discussed on the basis of the known 3D structure of MurB, thus providing a comprehensive picture of the mechanism of the MurB-catalysed reaction.
-
(1997)
Biochemistry
, vol.36
, pp. 796-805
-
-
Benson, T.E.1
Walsh, C.T.2
Massey, V.3
-
21
-
-
0030739371
-
Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase
-
Fraaije MW, van Berkel WJH. Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. J Biol Chem. 272:1997;18111-18116.
-
(1997)
J Biol Chem
, vol.272
, pp. 18111-18116
-
-
Fraaije, M.W.1
Van Berkel, W.J.H.2
-
22
-
-
0031571090
-
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: The shape of the active-site cavity controls substrate specificity
-
a value. This feature facilitates substrate oxidation by a hydride transfer mechanism.
-
a value. This feature facilitates substrate oxidation by a hydride transfer mechanism.
-
(1997)
Structure
, vol.5
, pp. 907-920
-
-
Mattevi, A.1
Fraaije, M.W.2
Mozzarelli, A.3
Olivi, L.4
Coda, A.5
Van Berkel, W.J.H.6
-
23
-
-
0030032041
-
The chemical mechanism of flavoprotein-catalysed α-hydroxy acid dehydrogenation: A mutational analysis
-
2 and related enzymes, analysed within the framework of the carboanion mechanism hypothesis.
-
2 and related enzymes, analysed within the framework of the carboanion mechanism hypothesis.
-
(1996)
Biochem Soc Trans
, vol.24
, pp. 77-83
-
-
Lederer, F.1
Belmouden, A.2
Gondry, M.3
-
24
-
-
0013038907
-
Structure of glycolate oxidase from spinach
-
Lindqvist Y, Brändén CI. Structure of glycolate oxidase from spinach. Proc Natl Acad Sci USA. 82:1985;6855-6859.
-
(1985)
Proc Natl Acad Sci USA
, vol.82
, pp. 6855-6859
-
-
Lindqvist, Y.1
Brändén, C.I.2
-
27
-
-
0025853478
-
2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding
-
2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding. J Biol Chem. 266:1991;3198-3207.
-
(1991)
J Biol Chem
, vol.266
, pp. 3198-3207
-
-
Lindqvist, Y.1
Branden, C.I.2
Mathews, F.S.3
Lederer, F.4
-
28
-
-
0030940522
-
Three-dimensional structures of glycolate oxidase with bound active-site inhibitors
-
of special interest. The structure of glycolate oxidase in complex with two competitive inhibitors reveals that a flexible loop enables the enzyme active site to accommodate ligands bulkier than the physiological substrate.
-
Stenberg K, Lindqvist Y. Three-dimensional structures of glycolate oxidase with bound active-site inhibitors. of special interest Protein Sci. 6:1997;1009-1015 The structure of glycolate oxidase in complex with two competitive inhibitors reveals that a flexible loop enables the enzyme active site to accommodate ligands bulkier than the physiological substrate.
-
(1997)
Protein Sci
, vol.6
, pp. 1009-1015
-
-
Stenberg, K.1
Lindqvist, Y.2
-
29
-
-
0028954322
-
Involvement of Tyr24 and Trp 108 in substrate binding and substrate specificity of glycolate oxidase
-
Stenberg K, Clausen T, Lindqvist Y, Macheroux P. Involvement of Tyr24 and Trp 108 in substrate binding and substrate specificity of glycolate oxidase. Eur J Biochem. 228:1995;408-416.
-
(1995)
Eur J Biochem
, vol.228
, pp. 408-416
-
-
Stenberg, K.1
Clausen, T.2
Lindqvist, Y.3
MacHeroux, P.4
-
30
-
-
0025763437
-
Enzyme catalysis: Not different just better
-
Knowles JR. Enzyme catalysis: not different just better. Nature. 350:1991;121-124.
-
(1991)
Nature
, vol.350
, pp. 121-124
-
-
Knowles, J.R.1
-
31
-
-
50549204004
-
D-amino acid oxidase II. Specificity, competitive inhibition and reaction sequence
-
Dixon M, Kleppe K. D-amino acid oxidase II. Specificity, competitive inhibition and reaction sequence. Biochim Biophys Acta. 96:1965;368-382.
-
(1965)
Biochim Biophys Acta
, vol.96
, pp. 368-382
-
-
Dixon, M.1
Kleppe, K.2
-
32
-
-
0031010615
-
Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase
-
of special interest. In excellent agreement with the crystallographic data, limited-proteolysis studies indicate that loop 216-228 of D-amino acid oxidase functions as an active-site gate, determining the rate of the overall reaction. Furthermore, the loop controls the substrate specificity to the point that, when proteolytically cleaved, the activity of the enzyme towards various substrates is dramatically altered.
-
Vanoni MA, Cosma A, Mazzeo D, Mattevi A, Todone F, Curti B. Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase. of special interest Biochemistry. 36:1997;5624-5632 In excellent agreement with the crystallographic data, limited-proteolysis studies indicate that loop 216-228 of D-amino acid oxidase functions as an active-site gate, determining the rate of the overall reaction. Furthermore, the loop controls the substrate specificity to the point that, when proteolytically cleaved, the activity of the enzyme towards various substrates is dramatically altered.
-
(1997)
Biochemistry
, vol.36
, pp. 5624-5632
-
-
Vanoni, M.A.1
Cosma, A.2
Mazzeo, D.3
Mattevi, A.4
Todone, F.5
Curti, B.6
-
33
-
-
0030018859
-
The role of α/β barrel loop 4 extension in modulating the physical and functional properties of long-chain 2-hydroxy-acid oxidase isozymes
-
8 barrel plays a key role in determining the enzyme's substrate specificity.
-
8 barrel plays a key role in determining the enzyme's substrate specificity.
-
(1996)
Eur J Biochem
, vol.238
, pp. 790-798
-
-
Belmouden, A.1
Lederer, F.2
-
34
-
-
0027432601
-
Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases.
-
Li J, Vrielink A, Brick P, Blow D. Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases. Biochemistry. 32:1993;11507-11515.
-
(1993)
Biochemistry
, vol.32
, pp. 11507-11515
-
-
Li, J.1
Vrielink, A.2
Brick, P.3
Blow, D.4
-
36
-
-
0029001789
-
Structure and mechanism of parahydroxybenzoate hydroxylase
-
Entsch B, van Berkel WJH. Structure and mechanism of parahydroxybenzoate hydroxylase. FASEB J. 9:1995;476-483.
-
(1995)
FASEB J
, vol.9
, pp. 476-483
-
-
Entsch, B.1
Van Berkel, W.J.H.2
-
37
-
-
0029936955
-
Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys
-
Moran GR, Entsch B, Palfey BA, Ballou DP. Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys. Biochemistry. 35:1996;9278-9285.
-
(1996)
Biochemistry
, vol.35
, pp. 9278-9285
-
-
Moran, G.R.1
Entsch, B.2
Palfey, B.A.3
Ballou, D.P.4
-
38
-
-
0028145298
-
Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of flavin ring
-
Schreuder HA, Mattevi A, Oblomova G, Kalk KH, Hol J, van der Bolt FJT, van der Berkel WJH. Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of flavin ring. Biochemistry. 33:1994;10161-10170.
-
(1994)
Biochemistry
, vol.33
, pp. 10161-10170
-
-
Schreuder, H.A.1
Mattevi, A.2
Oblomova, G.3
Kalk, K.H.4
Hol, J.5
Van Der Bolt, F.J.T.6
Van Der Berkel, W.J.H.7
-
39
-
-
0000425730
-
Dehydrogenation mechanism in flavoprotein catalysis
-
V. Massey, Williams C.H. Jr. Amsterdam: Elsevier
-
Ghisla S. Dehydrogenation mechanism in flavoprotein catalysis. Massey V, Williams CH Jr. In Flavins and Flavoproteins. 1982;133-142 Elsevier, Amsterdam.
-
(1982)
In Flavins and Flavoproteins
, pp. 133-142
-
-
Ghisla, S.1
-
40
-
-
0030879888
-
Orbital steering in the catalytic power of enzymes: Small structural changes with large catalytic consequences
-
of special interest. An insightful analysis of the stereochemistry of hydride transfer in a pyridine nucleotide dependent dehydrogenase.
-
Mesecar AD, Stoddard BL, Koshland DE Jr. Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences. of special interest Science. 77:1997;202-206 An insightful analysis of the stereochemistry of hydride transfer in a pyridine nucleotide dependent dehydrogenase.
-
(1997)
Science
, vol.77
, pp. 202-206
-
-
Mesecar, A.D.1
Stoddard, B.L.2
Koshland D.E., Jr.3
-
41
-
-
0030584680
-
Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase
-
Stoll VS, Kimber MS, Pai EF. Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase. Structure. 4:1996;437-447.
-
(1996)
Structure
, vol.4
, pp. 437-447
-
-
Stoll, V.S.1
Kimber, M.S.2
Pai, E.F.3
-
42
-
-
0028108347
-
Activation of molecular oxygen by flavins and flavoproteins
-
Massey V. Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem. 269:1995;22459-22462.
-
(1995)
J Biol Chem
, vol.269
, pp. 22459-22462
-
-
Massey, V.1
-
43
-
-
0029115180
-
Structure of charge-transfer complexes of flavoenzyme D-amino acid oxidase: A study by resonance Raman spectroscopy and extended Hückel molecular orbital method
-
Nishina Y, Sato K, Shiga K. Structure of charge-transfer complexes of flavoenzyme D-amino acid oxidase: a study by resonance Raman spectroscopy and extended Hückel molecular orbital method. J Biochem. 118:1995;614-620.
-
(1995)
J Biochem
, vol.118
, pp. 614-620
-
-
Nishina, Y.1
Sato, K.2
Shiga, K.3
-
44
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
-
(1991)
J Appl Crystallogr
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
45
-
-
0030886160
-
On the reaction mechanism of L-lactate oxidase: Quantitative structure-activity analysis of the reaction with para-substituted L-mandelates
-
of special interest. This paper addresses the problem of solving the reaction mechanism of α-hydroxy acid dehydrogenases by investigating the reactivity of L-lactate oxidase towards p-substituted mandelates. The new data are compatible with a mechanism in which there is little development of charge in the transition state. This could be through either hydride transfer or a mechanism based on α-proton abstraction occurring simultaneously with neutralisation of the resulting charge by another event.
-
Yorita K, Janko K, Aki K, Ghisla S, Palfey BA, Massey V. On the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates. of special interest Proc Natl Acad Sci USA. 94:1997;9590-9595 This paper addresses the problem of solving the reaction mechanism of α-hydroxy acid dehydrogenases by investigating the reactivity of L-lactate oxidase towards p-substituted mandelates. The new data are compatible with a mechanism in which there is little development of charge in the transition state. This could be through either hydride transfer or a mechanism based on α-proton abstraction occurring simultaneously with neutralisation of the resulting charge by another event.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9590-9595
-
-
Yorita, K.1
Janko, K.2
Aki, K.3
Ghisla, S.4
Palfey, B.A.5
Massey, V.6
|