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Refinado por: Base de dados/Biblioteca: METADEX remover Base de dados/Biblioteca: Wiley-Blackwell Full Collection 2013 remover
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1
Structure and function of the thermostable l‐asparaginase from Thermococcus kodakarensis
Structure and function of the thermostable l‐asparaginase from Thermococcus kodakarensis
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Structure and function of the thermostable l‐asparaginase from Thermococcus kodakarensis

Guo, Jingxu ; Coker, Alun R. ; Wood, Steve P. ; Cooper, Jonathan B. ; Chohan, Shahid Mahmood ; Rashid, Naeem ; Akhtar, Muhummad

Acta crystallographica. Section D, Biological crystallography., 2017-11, Vol.73 (11), p.889-895 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

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2
Rhizobium etli has two l‐asparaginases with low sequence identity but similar structure and catalytic center
Rhizobium etli has two l‐asparaginases with low sequence identity but similar structure and catalytic center
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Rhizobium etli has two l‐asparaginases with low sequence identity but similar structure and catalytic center

Loch, Joanna I. ; Worsztynowicz, Paulina ; Sliwiak, Joanna ; Grzechowiak, Marta ; Imiolczyk, Barbara ; Pokrywka, Kinga ; Chwastyk, Mateusz ; Gilski, Miroslaw ; Jaskolski, Mariusz

Acta crystallographica. Section D, Biological crystallography., 2023-08, Vol.79 (8), p.775-791 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

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3
Improving the analytical toolbox to investigate copurifying host cell proteins presence: N‐(4)‐(β‐acetylglucosaminyl)‐ l‐asparaginase case study
Improving the analytical toolbox to investigate copurifying host cell proteins presence: N‐(4)‐(β‐acetylglucosaminyl)‐ l‐asparaginase case study
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Improving the analytical toolbox to investigate copurifying host cell proteins presence: N‐(4)‐(β‐acetylglucosaminyl)‐ l‐asparaginase case study

Clavier, Séverine ; Fougeron, Delphine ; Petrovic, Suzana ; Elmaleh, Hagit ; Fourneaux, Céline ; Bugnazet, Dawid ; Duffieux, Francis ; Masiero, Alessandro ; Mitra‐Kaushik, Shibani ; Genet, Bruno ; Fromentin, Yann ; Kreiss, Patrick ; Laborderie, Bénédicte ; Brault, Dominique ; Menet, Jean‐Michel

Biotechnology and bioengineering, 2020-11, Vol.117 (11), p.3368-3378 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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4
Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics
Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics
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Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics

Cerofolini, Linda ; Giuntini, Stefano ; Carlon, Azzurra ; Ravera, Enrico ; Calderone, Vito ; Fragai, Marco ; Parigi, Giacomo ; Luchinat, Claudio

Chemistry : a European journal, 2019-02, Vol.25 (8), p.1984-1991 [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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5
Engineered asparaginase from Erwinia chrysanthemi enhances asparagine hydrolase activity and diminishes enzyme immunoreactivity ‐ a new promise to treat acute lymphoblastic leukemia
Engineered asparaginase from Erwinia chrysanthemi enhances asparagine hydrolase activity and diminishes enzyme immunoreactivity ‐ a new promise to treat acute lymphoblastic leukemia
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Engineered asparaginase from Erwinia chrysanthemi enhances asparagine hydrolase activity and diminishes enzyme immunoreactivity ‐ a new promise to treat acute lymphoblastic leukemia

Munhoz Costa, Iris ; Custódio Moura, Débora ; Meira Lima, Guilherme ; Pessoa, Adalberto ; Oresco dos Santos, Camila ; Oliveira, Marcos A ; Monteiro, Gisele

Journal of chemical technology and biotechnology (1986), 2022-01, Vol.97 (1), p.228-239 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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6
Recombinant l‐asparaginase production using Pichia pastoris (MUTs strain): establishment of conditions for growth and induction phases
Recombinant l‐asparaginase production using Pichia pastoris (MUTs strain): establishment of conditions for growth and induction phases
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Recombinant l‐asparaginase production using Pichia pastoris (MUTs strain): establishment of conditions for growth and induction phases

Pillaca‐Pullo, Omar ; Rodrigues, David ; Sánchez‐Moguel, Ignacio ; Lopes, André ; Pimenta, Marcela ; Basi, Tajindar ; Feitosa, Valker ; Zavaleta, Amparo ; Monteiro, Gisele ; Pessoa Jr, Adalberto ; Vitolo, Michele

Journal of chemical technology and biotechnology (1986), 2021-01, Vol.96 (1), p.283-292 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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7
Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains
Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains
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Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains

Tomar, Rachana ; Sharma, Pankaj ; Srivastava, Ankit ; Bansal, Saurabh ; Kundu, Bishwajit

Acta crystallographica. Section D, Biological crystallography., 2014-12, Vol.70 (12), p.3187-3197 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

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8
An improved method for simple and accurate colorimetric determination of l‐asparaginase enzyme activity using Nessler's reagent
An improved method for simple and accurate colorimetric determination of l‐asparaginase enzyme activity using Nessler's reagent
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An improved method for simple and accurate colorimetric determination of l‐asparaginase enzyme activity using Nessler's reagent

Simas, Rodrigo G ; Krebs Kleingesinds, Eduardo ; Pessoa Junior, Adalberto ; Long, Paul F

Journal of chemical technology and biotechnology (1986), 2021-05, Vol.96 (5), p.1326-1332 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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9
In situ purification of periplasmatic L‐asparaginase by aqueous two phase systems with ionic liquids (ILs) as adjuvants
In situ purification of periplasmatic L‐asparaginase by aqueous two phase systems with ionic liquids (ILs) as adjuvants
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In situ purification of periplasmatic L‐asparaginase by aqueous two phase systems with ionic liquids (ILs) as adjuvants

Santos, João HPM ; Flores‐Santos, Juan C ; Meneguetti, Giovanna P ; Rangel‐Yagui, Carlota O ; Coutinho, João AP ; Vitolo, Michele ; Ventura, Sónia PM ; Pessoa, Adalberto

Journal of chemical technology and biotechnology (1986), 2018-07, Vol.93 (7), p.1871-1880 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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10
Synthesis of biologically active proteins as L6KD‐SUMO fusions forming inclusion bodies in Escherichia coli
Synthesis of biologically active proteins as L6KD‐SUMO fusions forming inclusion bodies in Escherichia coli
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Synthesis of biologically active proteins as L6KD‐SUMO fusions forming inclusion bodies in Escherichia coli

Komolov, Aleksandr S. ; Sannikova, Evgeniia P. ; Gorbunov, Aleksandr A. ; Gubaidullin, Irek I. ; Plokhikh, Konstantin S. ; Konstantinova, Galina E. ; Bulushova, Natalia V. ; Kuchin, Sergei V. ; Kozlov, Dmitriy G.

Biotechnology and bioengineering, 2024-02, Vol.121 (2), p.535-550 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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