Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes
Lyu Q, Zhang K, Zhu Q, Li Z, Liu Y, Fitzek E, Yohe T, Zhao L, Li W, Liu T, Yin Y, et al. (2018)
Biochimica et Biophysica Acta (BBA) - General Subjects 1862(9): 1862-1869.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Lyu, Qianqian;
Zhang, Keke;
Zhu, Qiaoyun;
Li, Zhijian;
Liu, Yujie;
Fitzek, ElisabethUniBi;
Yohe, Tanner;
Zhao, Liming;
Li, Weihua;
Liu, Tao;
Yin, Yanbin;
Liu, Weizhi
Einrichtung
Erscheinungsjahr
2018
Zeitschriftentitel
Biochimica et Biophysica Acta (BBA) - General Subjects
Band
1862
Ausgabe
9
Seite(n)
1862-1869
ISSN
0304-4165
Page URI
https://pub.uni-bielefeld.de/record/2920893
Zitieren
Lyu Q, Zhang K, Zhu Q, et al. Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes. Biochimica et Biophysica Acta (BBA) - General Subjects. 2018;1862(9):1862-1869.
Lyu, Q., Zhang, K., Zhu, Q., Li, Z., Liu, Y., Fitzek, E., Yohe, T., et al. (2018). Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes. Biochimica et Biophysica Acta (BBA) - General Subjects, 1862(9), 1862-1869. doi:10.1016/j.bbagen.2018.05.024
Lyu, Qianqian, Zhang, Keke, Zhu, Qiaoyun, Li, Zhijian, Liu, Yujie, Fitzek, Elisabeth, Yohe, Tanner, et al. 2018. “Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes”. Biochimica et Biophysica Acta (BBA) - General Subjects 1862 (9): 1862-1869.
Lyu, Q., Zhang, K., Zhu, Q., Li, Z., Liu, Y., Fitzek, E., Yohe, T., Zhao, L., Li, W., Liu, T., et al. (2018). Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes. Biochimica et Biophysica Acta (BBA) - General Subjects 1862, 1862-1869.
Lyu, Q., et al., 2018. Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes. Biochimica et Biophysica Acta (BBA) - General Subjects, 1862(9), p 1862-1869.
Q. Lyu, et al., “Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes”, Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1862, 2018, pp. 1862-1869.
Lyu, Q., Zhang, K., Zhu, Q., Li, Z., Liu, Y., Fitzek, E., Yohe, T., Zhao, L., Li, W., Liu, T., Yin, Y., Liu, W.: Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862, 1862-1869 (2018).
Lyu, Qianqian, Zhang, Keke, Zhu, Qiaoyun, Li, Zhijian, Liu, Yujie, Fitzek, Elisabeth, Yohe, Tanner, Zhao, Liming, Li, Weihua, Liu, Tao, Yin, Yanbin, and Liu, Weizhi. “Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes”. Biochimica et Biophysica Acta (BBA) - General Subjects 1862.9 (2018): 1862-1869.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
3 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
Adaptations of Alteromonas sp. 76-1 to Polysaccharide Degradation: A CAZyme Plasmid for Ulvan Degradation and Two Alginolytic Systems.
Koch H, Freese HM, Hahnke RL, Simon M, Wietz M., Front Microbiol 10(), 2019
PMID: 30936857
Koch H, Freese HM, Hahnke RL, Simon M, Wietz M., Front Microbiol 10(), 2019
PMID: 30936857
Diverse Bacteria Utilize Alginate Within the Microbiome of the Giant Kelp Macrocystis pyrifera.
Lin JD, Lemay MA, Parfrey LW., Front Microbiol 9(), 2018
PMID: 30177919
Lin JD, Lemay MA, Parfrey LW., Front Microbiol 9(), 2018
PMID: 30177919
Characterization of a Novel PolyM-Preferred Alginate Lyase from Marine Vibrio splendidus OU02.
Zhuang J, Zhang K, Liu X, Liu W, Lyu Q, Ji A., Mar Drugs 16(9), 2018
PMID: 30135412
Zhuang J, Zhang K, Liu X, Liu W, Lyu Q, Ji A., Mar Drugs 16(9), 2018
PMID: 30135412
References
Daten bereitgestellt von Europe PubMed Central.
Export
Markieren/ Markierung löschen
Markierte Publikationen
Web of Science
Dieser Datensatz im Web of Science®Quellen
PMID: 29864445
PubMed | Europe PMC
Suchen in