4.7 Article

Enhancing the catalytic activity of a novel GH5 cellulase GtCel5 from Gloeophyllum trabeum CBS 900.73 by site-directed mutagenesis on loop 6

相关参考文献

注意:仅列出部分参考文献,下载原文获取全部文献信息。
Article Biochemistry & Molecular Biology

Multiple Conformations of the Loop Region Confers Heat-Resistance on SsArd1, a Thermophilic NatA

Yu-Yung Chang et al.

CHEMBIOCHEM (2016)

Article Biochemistry & Molecular Biology

Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-β-endoglucanase

Junjie Yan et al.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2016)

Article Biotechnology & Applied Microbiology

Functional and structural analyses of a 1,4-β-endoglucanase from Ganoderma lucidum

Guizhi Liu et al.

ENZYME AND MICROBIAL TECHNOLOGY (2016)

Article Biochemistry & Molecular Biology

Biochemical Characterization and Structural Analysis of a Bifunctional Cellulase/Xylanase from Clostridium thermocellum

Shuo-Fu Yuan et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2015)

Article Chemistry, Multidisciplinary

Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase

Xiang Zhai et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2015)

Article Biotechnology & Applied Microbiology

A thermophilic endo-1,4-β-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials

Kun Wang et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2014)

Article Biochemistry & Molecular Biology

The carbohydrate-active enzymes database (CAZy) in 2013

Vincent Lombard et al.

NUCLEIC ACIDS RESEARCH (2014)

Review Biotechnology & Applied Microbiology

Bioconversion of lignocellulose: inhibitors and detoxification

Leif J. Jonsson et al.

BIOTECHNOLOGY FOR BIOFUELS (2013)

Article Biotechnology & Applied Microbiology

Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop

Ya-Shan Cheng et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2012)

Article Evolutionary Biology

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

Henrik Aspeborg et al.

BMC EVOLUTIONARY BIOLOGY (2012)

Article Biochemistry & Molecular Biology

A salt-bridge controlled by ligand binding modulates the hydrolysis reaction in a GH5 endoglucanase

Somayesadat Badieyan et al.

PROTEIN ENGINEERING DESIGN & SELECTION (2012)

Article Biochemical Research Methods

Substrate binding of a GH5 endoglucanase from the ruminal fungus Piromyces rhizinflata

Chih-Wen Tseng et al.

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS (2011)

Article Biotechnology & Applied Microbiology

Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile

Chaoning Liang et al.

JOURNAL OF BIOTECHNOLOGY (2011)

Article Biochemistry & Molecular Biology

A structural study of Hypocrea jecorina Cel5A

Toni M. Lee et al.

PROTEIN SCIENCE (2011)

Review Chemistry, Multidisciplinary

GLYCAM06: A generalizable Biomolecular force field. Carbohydrates

Karl N. Kirschner et al.

JOURNAL OF COMPUTATIONAL CHEMISTRY (2008)

Article Biochemistry & Molecular Biology

MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0

Koichiro Tamura et al.

MOLECULAR BIOLOGY AND EVOLUTION (2007)

Review Biochemical Research Methods

High-throughput screening for enhanced protein stability

Andreas S. Bommarius et al.

CURRENT OPINION IN BIOTECHNOLOGY (2006)

Article Biochemistry & Molecular Biology

Identification and molecular modeling of a family 5 endocellulase from Thermus caldophilus GK24, a cellulolytic strain of Thermus thermophilus

Dooil Kim et al.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2006)

Article Biochemistry & Molecular Biology

Comparison of multiple amber force fields and development of improved protein backbone parameters

Viktor Hornak et al.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2006)

Review Biochemistry & Molecular Biology

The TIM-barrel fold: a versatile framework for efficient enzymes

RK Wierenga

FEBS LETTERS (2001)