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Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions.

Biotechnology for biofuels

Santos CA, Zanphorlin LM, Crucello A, Tonoli CCC, Ruller R, Horta MAC, Murakami MT, de Souza AP.
PMID: 27006690
Biotechnol Biofuels. 2016 Mar 22;9:71. doi: 10.1186/s13068-016-0487-0. eCollection 2016.

BACKGROUND: The conversion of biomass-derived sugars via enzymatic hydrolysis for biofuel production is a challenge. Therefore, the search for microorganisms and key enzymes that increase the efficiency of the saccharification of cellulosic substrates remains an important and high-priority area...

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Santos CA, Zanphorlin LM, Crucello A, et al. Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions. Biotechnol Biofuels. 2016;9:71doi: 10.1186/s13068-016-0487-0.
Santos, C. A., Zanphorlin, L. M., Crucello, A., Tonoli, C. C. C., Ruller, R., Horta, M. A. C., Murakami, M. T., & de Souza, A. P. (2016). Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions. Biotechnology for biofuels, 971. https://doi.org/10.1186/s13068-016-0487-0
Santos, Clelton A, et al. "Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions." Biotechnology for biofuels vol. 9 (2016): 71. doi: https://doi.org/10.1186/s13068-016-0487-0
Santos CA, Zanphorlin LM, Crucello A, Tonoli CCC, Ruller R, Horta MAC, Murakami MT, de Souza AP. Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions. Biotechnol Biofuels. 2016 Mar 22;9:71. doi: 10.1186/s13068-016-0487-0. eCollection 2016. PMID: 27006690; PMCID: PMC4802607.
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Development of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genes.

Biotechnology for biofuels

Guo Z, Duquesne S, Bozonnet S, Cioci G, Nicaud JM, Marty A, O'Donohue MJ.
PMID: 26244054
Biotechnol Biofuels. 2015 Aug 04;8:109. doi: 10.1186/s13068-015-0289-9. eCollection 2015.

BACKGROUND: Yarrowia lipolytica, one of the most widely studied "nonconventional" oleaginous yeast species, is unable to grow on cellobiose. Engineering cellobiose-degrading ability into this yeast is a vital step towards the development of cellulolytic biocatalysts suitable for consolidated bioprocessing.RESULTS:...

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Guo Z, Duquesne S, Bozonnet S, et al. Development of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genes. Biotechnol Biofuels. 2015;8:109doi: 10.1186/s13068-015-0289-9.
Guo, Z., Duquesne, S., Bozonnet, S., Cioci, G., Nicaud, J. M., Marty, A., & O'Donohue, M. J. (2015). Development of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genes. Biotechnology for biofuels, 8109. https://doi.org/10.1186/s13068-015-0289-9
Guo, Zhongpeng, et al. "Development of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genes." Biotechnology for biofuels vol. 8 (2015): 109. doi: https://doi.org/10.1186/s13068-015-0289-9
Guo Z, Duquesne S, Bozonnet S, Cioci G, Nicaud JM, Marty A, O'Donohue MJ. Development of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genes. Biotechnol Biofuels. 2015 Aug 04;8:109. doi: 10.1186/s13068-015-0289-9. eCollection 2015. PMID: 26244054; PMCID: PMC4524412.
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Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune.

Bioscience, biotechnology, and biochemistry

Mizuno K, Awazu N, Tachiki T.
PMID: 27393352
Biosci Biotechnol Biochem. 1998;62(1):39-43. doi: 10.1271/bbb.62.39.

Hydrolyzing activities toward p-nitrophenyl (p-NP)-β-D-glucoside and laminarin in a culture filtrate of Bacillus circulans KA-304, which has been observed to form protoplasts from Schizophyllum commune mycelia, increased when the bacterium was grown on a cell-wall preparation (CWP) of S....

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Mizuno K, Awazu N, Tachiki T. Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Biosci Biotechnol Biochem. 1998;62(1):39-43doi: 10.1271/bbb.62.39.
Mizuno, K., Awazu, N., & Tachiki, T. (1998). Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Bioscience, biotechnology, and biochemistry, 62(1), 39-43. https://doi.org/10.1271/bbb.62.39
Mizuno, K, et al. "Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune." Bioscience, biotechnology, and biochemistry vol. 62,1 (1998): 39-43. doi: https://doi.org/10.1271/bbb.62.39
Mizuno K, Awazu N, Tachiki T. Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Biosci Biotechnol Biochem. 1998;62(1):39-43. doi: 10.1271/bbb.62.39. PMID: 27393352.
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Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes.

ACS central science

Jiang J, Kuo CL, Wu L, Franke C, Kallemeijn WW, Florea BI, van Meel E, van der Marel GA, Codée JD, Boot RG, Davies GJ, Overkleeft HS, Aerts JM.
PMID: 27280170
ACS Cent Sci. 2016 May 25;2(5):351-8. doi: 10.1021/acscentsci.6b00057. Epub 2016 Apr 26.

The development of small molecule activity-based probes (ABPs) is an evolving and powerful area of chemistry. There is a major need for synthetically accessible and specific ABPs to advance our understanding of enzymes in health and disease. α-Glucosidases are...

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Jiang J, Kuo CL, Wu L, et al. Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes. ACS Cent Sci. 2016;2(5):351-8doi: 10.1021/acscentsci.6b00057.
Jiang, J., Kuo, C. L., Wu, L., Franke, C., Kallemeijn, W. W., Florea, B. I., van Meel, E., van der Marel, G. A., Codée, J. D., Boot, R. G., Davies, G. J., Overkleeft, H. S., & Aerts, J. M. (2016). Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes. ACS central science, 2(5), 351-8. https://doi.org/10.1021/acscentsci.6b00057
Jiang, Jianbing, et al. "Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes." ACS central science vol. 2,5 (2016): 351-8. doi: https://doi.org/10.1021/acscentsci.6b00057
Jiang J, Kuo CL, Wu L, Franke C, Kallemeijn WW, Florea BI, van Meel E, van der Marel GA, Codée JD, Boot RG, Davies GJ, Overkleeft HS, Aerts JM. Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes. ACS Cent Sci. 2016 May 25;2(5):351-8. doi: 10.1021/acscentsci.6b00057. Epub 2016 Apr 26. PMID: 27280170; PMCID: PMC4882745.
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Lignocellulolytic enzyme profiles of edible mushroom fungi.

World journal of microbiology & biotechnology

Buswell JA, Cai YJ, Chang ST, Peberdy JF, Fu SY, Yu HS.
PMID: 24415386
World J Microbiol Biotechnol. 1996 Sep;12(5):537-42. doi: 10.1007/BF00419469.

One of the most economically-viable processes for the bioconversion of many types of lignocellulosic wastes is represented by edible mushroom cultivation. Lentinula edodes, Volvariella volvacea and Pleurotus sajor-caju are three important commercially cultivated mushrooms which exhibit varying abilities to...

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Buswell JA, Cai YJ, Chang ST, et al. Lignocellulolytic enzyme profiles of edible mushroom fungi. World J Microbiol Biotechnol. 1996;12(5):537-42doi: 10.1007/BF00419469.
Buswell, J. A., Cai, Y. J., Chang, S. T., Peberdy, J. F., Fu, S. Y., & Yu, H. S. (1996). Lignocellulolytic enzyme profiles of edible mushroom fungi. World journal of microbiology & biotechnology, 12(5), 537-42. https://doi.org/10.1007/BF00419469
Buswell, J A, et al. "Lignocellulolytic enzyme profiles of edible mushroom fungi." World journal of microbiology & biotechnology vol. 12,5 (1996): 537-42. doi: https://doi.org/10.1007/BF00419469
Buswell JA, Cai YJ, Chang ST, Peberdy JF, Fu SY, Yu HS. Lignocellulolytic enzyme profiles of edible mushroom fungi. World J Microbiol Biotechnol. 1996 Sep;12(5):537-42. doi: 10.1007/BF00419469. PMID: 24415386.
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A novel promising Trichoderma harzianum strain for the production of a cellulolytic complex using sugarcane bagasse in natura.

SpringerPlus

Benoliel B, Torres FA, de Moraes LM.
PMID: 24349958
Springerplus. 2013 Dec 06;2:656. doi: 10.1186/2193-1801-2-656. eCollection 2013.

Brazil is a major producer of agro-industrial residues, such as sugarcane bagasse, which could be used as raw material for microbial production of cellulases as an important strategy for the development of sustainable processes of second generation ethanol production....

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Benoliel B, Torres FA, de Moraes LM. A novel promising Trichoderma harzianum strain for the production of a cellulolytic complex using sugarcane bagasse in natura. Springerplus. 2013;2:656doi: 10.1186/2193-1801-2-656.
Benoliel, B., Torres, F. A., & de Moraes, L. M. (2013). A novel promising Trichoderma harzianum strain for the production of a cellulolytic complex using sugarcane bagasse in natura. SpringerPlus, 2656. https://doi.org/10.1186/2193-1801-2-656
Benoliel, Bruno, et al. "A novel promising Trichoderma harzianum strain for the production of a cellulolytic complex using sugarcane bagasse in natura." SpringerPlus vol. 2 (2013): 656. doi: https://doi.org/10.1186/2193-1801-2-656
Benoliel B, Torres FA, de Moraes LM. A novel promising Trichoderma harzianum strain for the production of a cellulolytic complex using sugarcane bagasse in natura. Springerplus. 2013 Dec 06;2:656. doi: 10.1186/2193-1801-2-656. eCollection 2013. PMID: 24349958; PMCID: PMC3862859.
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A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities.

Biotechnology for biofuels

Zhou Y, Wang X, Wei W, Xu J, Wang W, Xie Z, Zhang Z, Jiang H, Wang Q, Wei C.
PMID: 26877766
Biotechnol Biofuels. 2016 Feb 13;9:36. doi: 10.1186/s13068-016-0449-6. eCollection 2016.

BACKGROUND: Cellulose, an abundant and renewable polysaccharides, constitutes the largest resource for bioconversion of biofuels. Plant polysaccharides hydrolysis is catalyzed by cellulases, which include endoglucanases, exoglucanases, and β-glucosidases. Converting cellulose and hemicellulose to short chains of oligosaccharides by endo-/exoglucanases...

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Zhou Y, Wang X, Wei W, et al. A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities. Biotechnol Biofuels. 2016;9:36doi: 10.1186/s13068-016-0449-6.
Zhou, Y., Wang, X., Wei, W., Xu, J., Wang, W., Xie, Z., Zhang, Z., Jiang, H., Wang, Q., & Wei, C. (2016). A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities. Biotechnology for biofuels, 936. https://doi.org/10.1186/s13068-016-0449-6
Zhou, Yu, et al. "A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities." Biotechnology for biofuels vol. 9 (2016): 36. doi: https://doi.org/10.1186/s13068-016-0449-6
Zhou Y, Wang X, Wei W, Xu J, Wang W, Xie Z, Zhang Z, Jiang H, Wang Q, Wei C. A novel efficient β-glucanase from a paddy soil microbial metagenome with versatile activities. Biotechnol Biofuels. 2016 Feb 13;9:36. doi: 10.1186/s13068-016-0449-6. eCollection 2016. PMID: 26877766; PMCID: PMC4752780.
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Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves.

Planta

Kakes P.
PMID: 24241426
Planta. 1985 Oct;166(2):156-60. doi: 10.1007/BF00397342.

Linamarase (EC 3.2.1.21) is a specialized β-glucosidase that hydrolyses the cyanogenic glucoside linamarin. Two clones of Trifolium repens L. derived from natural populations, of which one clone exhibited linamarase activity, were used in a comparative study to try to...

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Kakes P. Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves. Planta. 1985;166(2):156-60doi: 10.1007/BF00397342.
Kakes, P. (1985). Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves. Planta, 166(2), 156-60. https://doi.org/10.1007/BF00397342
Kakes, P. "Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves." Planta vol. 166,2 (1985): 156-60. doi: https://doi.org/10.1007/BF00397342
Kakes P. Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves. Planta. 1985 Oct;166(2):156-60. doi: 10.1007/BF00397342. PMID: 24241426.
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Glucose-tolerant β-glucosidase retrieved from a Kusaya gravy metagenome.

Frontiers in microbiology

Uchiyama T, Yaoi K, Miyazaki K.
PMID: 26136726
Front Microbiol. 2015 Jun 16;6:548. doi: 10.3389/fmicb.2015.00548. eCollection 2015.

β-glucosidases (BGLs) hydrolyze cello-oligosaccharides to glucose and play a crucial role in the enzymatic saccharification of cellulosic biomass. Despite their significance for the production of glucose, most identified BGLs are commonly inhibited by low (∼mM) concentrations of glucose. Therefore,...

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Uchiyama T, Yaoi K, Miyazaki K. Glucose-tolerant β-glucosidase retrieved from a Kusaya gravy metagenome. Front Microbiol. 2015;6:548doi: 10.3389/fmicb.2015.00548.
Uchiyama, T., Yaoi, K., & Miyazaki, K. (2015). Glucose-tolerant β-glucosidase retrieved from a Kusaya gravy metagenome. Frontiers in microbiology, 6548. https://doi.org/10.3389/fmicb.2015.00548
Uchiyama, Taku, et al. "Glucose-tolerant β-glucosidase retrieved from a Kusaya gravy metagenome." Frontiers in microbiology vol. 6 (2015): 548. doi: https://doi.org/10.3389/fmicb.2015.00548
Uchiyama T, Yaoi K, Miyazaki K. Glucose-tolerant β-glucosidase retrieved from a Kusaya gravy metagenome. Front Microbiol. 2015 Jun 16;6:548. doi: 10.3389/fmicb.2015.00548. eCollection 2015. PMID: 26136726; PMCID: PMC4468940.
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Tissue Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds.

Plant physiology

Poulton JE, Li CP.
PMID: 12232058
Plant Physiol. 1994 Jan;104(1):29-35. doi: 10.1104/pp.104.1.29.

Plum (Prunus domestica) seeds, which contain the cyanogenic diglucoside (R)-amygdalin and lesser amounts of the corresponding monoglucoside (R)-prunasin, release the respiratory toxin HCN upon tissue disruption. Amygdalin hydrolase (AH) and prunasin hydrolase (PH), two specific [beta]-glucosidases responsible for hydrolysis...

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Poulton JE, Li CP. Tissue Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds. Plant Physiol. 1994;104(1):29-35doi: 10.1104/pp.104.1.29.
Poulton, J. E., & Li, C. P. (1994). Tissue Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds. Plant physiology, 104(1), 29-35. https://doi.org/10.1104/pp.104.1.29
Poulton, J. E., and Li, C. P.. "Tissue Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds." Plant physiology vol. 104,1 (1994): 29-35. doi: https://doi.org/10.1104/pp.104.1.29
Poulton JE, Li CP. Tissue Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds. Plant Physiol. 1994 Jan;104(1):29-35. doi: 10.1104/pp.104.1.29. PMID: 12232058; PMCID: PMC159159.
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Purification and characterisation of a beta-glucosidase abundantly expressed in ripe sweet cherry (Prunus avium L.) fruit.

Plant science : an international journal of experimental plant biology

Gerardi C, Blando F, Santino A, Zacheo G.
PMID: 11297776
Plant Sci. 2001 Apr;160(5):795-805. doi: 10.1016/s0168-9452(00)00423-4.

A beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) was purified to homogeneity from ripe fruits of sweet cherry (Prunus avium L.) by ammonium sulphate precipitation, ion exchange and size exclusion chromatography. The enzyme is a monomer with a molecular mass of...

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Gerardi C, Blando F, Santino A, et al. Purification and characterisation of a beta-glucosidase abundantly expressed in ripe sweet cherry (Prunus avium L.) fruit. Plant Sci. 2001;160(5):795-805doi: 10.1016/s0168-9452(00)00423-4.
Gerardi, C., Blando, F., Santino, A., & Zacheo, G. (2001). Purification and characterisation of a beta-glucosidase abundantly expressed in ripe sweet cherry (Prunus avium L.) fruit. Plant science : an international journal of experimental plant biology, 160(5), 795-805. https://doi.org/10.1016/s0168-9452(00)00423-4
Gerardi, C, et al. "Purification and characterisation of a beta-glucosidase abundantly expressed in ripe sweet cherry (Prunus avium L.) fruit." Plant science : an international journal of experimental plant biology vol. 160,5 (2001): 795-805. doi: https://doi.org/10.1016/s0168-9452(00)00423-4
Gerardi C, Blando F, Santino A, Zacheo G. Purification and characterisation of a beta-glucosidase abundantly expressed in ripe sweet cherry (Prunus avium L.) fruit. Plant Sci. 2001 Apr;160(5):795-805. doi: 10.1016/s0168-9452(00)00423-4. PMID: 11297776.
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Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS.

Plant physiology

Cline K, Albersheim P.
PMID: 16661872
Plant Physiol. 1981 Jul;68(1):207-20. doi: 10.1104/pp.68.1.207.

The fact that fungal glucans will stimulate soybeans to accumulate phytoalexins prompted an investigation of soybean cell beta-1,3-glucanases and beta-glucosidases, as well as the ability of these enzymes to hydrolyze the fungal glucans. Several beta-1,3-glucanases and beta-glucosidases can be...

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Cline K, Albersheim P. Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS. Plant Physiol. 1981;68(1):207-20doi: 10.1104/pp.68.1.207.
Cline, K., & Albersheim, P. (1981). Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS. Plant physiology, 68(1), 207-20. https://doi.org/10.1104/pp.68.1.207
Cline, K, and Albersheim, P. "Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS." Plant physiology vol. 68,1 (1981): 207-20. doi: https://doi.org/10.1104/pp.68.1.207
Cline K, Albersheim P. Host-Pathogen Interactions: XVI. PURIFICATION AND CHARACTERIZATION OF A beta-GLUCOSYL HYDROLASE/TRANSFERASE PRESENT IN THE WALLS OF SOYBEAN CELLS. Plant Physiol. 1981 Jul;68(1):207-20. doi: 10.1104/pp.68.1.207. PMID: 16661872; PMCID: PMC425917.
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