skip to main content
Idioma:
Refinado por: Base de dados/Biblioteca: Wiley-Blackwell Full Collection 2013 remover
Result Number Material Type Add to My Shelf Action Record Details and Options
1
Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
Material Type:
Artigo 		Adicionar ao Meu Espaço

Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68

Pons, Tirso ; Naumoff, Daniil G. ; Martínez-Fleites, Carlos ; Hernández, Lázaro

Proteins, structure, function, and bioinformatics, 2004-02, Vol.54 (3), p.424-432 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

Texto completo disponível

Citações Citado por
2
Investigating the binding of β-1,4-galactan to Bacillus licheniformis β-1,4-galactanase by crystallography and computational modeling
Investigating the binding of β-1,4-galactan to Bacillus licheniformis β-1,4-galactanase by crystallography and computational modeling
Material Type:
Artigo 		Adicionar ao Meu Espaço

Investigating the binding of β-1,4-galactan to Bacillus licheniformis β-1,4-galactanase by crystallography and computational modeling

Le Nours, Jérôme ; De Maria, Leonardo ; Welner, Ditte ; Jørgensen, Christel T. ; Christensen, Lars L. H. ; Borchert, Torben V. ; Larsen, Sine ; Lo Leggio, Leila

Proteins, structure, function, and bioinformatics, 2009-06, Vol.75 (4), p.977-989 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

Texto completo disponível

Citações Citado por
3
Structural characterization of the Acetobacter xylinum endo-β-1,4-glucanase CMCax required for cellulose biosynthesis
Structural characterization of the Acetobacter xylinum endo-β-1,4-glucanase CMCax required for cellulose biosynthesis
Material Type:
Artigo 		Adicionar ao Meu Espaço

Structural characterization of the Acetobacter xylinum endo-β-1,4-glucanase CMCax required for cellulose biosynthesis

Yasutake, Yoshiaki ; Kawano, Shin ; Tajima, Kenji ; Yao, Min ; Satoh, Yasuharu ; Munekata, Masanobu ; Tanaka, Isao

Proteins, structure, function, and bioinformatics, 2006-09, Vol.64 (4), p.1069-1077 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

Texto completo disponível

Citações Citado por
4
Identification and expression of GH-8 family chitosanases from several Bacillus thuringiensis subspecies
Identification and expression of GH-8 family chitosanases from several Bacillus thuringiensis subspecies
Material Type:
Artigo 		Adicionar ao Meu Espaço

Identification and expression of GH-8 family chitosanases from several Bacillus thuringiensis subspecies

Lee, Han-Seung ; Jang, Jun Sung ; Choi, Soo-Keun ; Lee, Dong-Woo ; Kim, Eui-Joong ; Jung, Heung-Chae ; Pan, Jae-Gu

FEMS microbiology letters, 2007-12, Vol.277 (2), p.133-141 [Periódico revisado por pares]

Oxford, UK: Oxford, UK : Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
5
Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus
Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus
Material Type:
Artigo 		Adicionar ao Meu Espaço

Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus

Centeno, Maria S.J ; Goyal, Arun ; Prates, José A.M ; Ferreira, Luís M.A ; Gilbert, Harry J ; Fontes, Carlos M.G.A

FEMS microbiology letters, 2006-12, Vol.265 (1), p.26-34 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
6
Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase
Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase
Material Type:
Artigo 		Adicionar ao Meu Espaço

Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase

Akeboshi, Hiromi ; Tonozuka, Takashi ; Furukawa, Takaaki ; Ichikawa, Kazuhiro ; Aoki, Hiroyoshi ; Shimonishi, Akiko ; Nishikawa, Atsushi ; Sakano, Yoshiyuki

European journal of biochemistry, 2004-11, Vol.271 (22), p.4420-4427 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
7
The unique set of putative membrane-associated anti-σ factors in Clostridium thermocellum suggests a novel extracellular carbohydrate-sensing mechanism involved in gene regulation
The unique set of putative membrane-associated anti-σ factors in Clostridium thermocellum suggests a novel extracellular carbohydrate-sensing mechanism involved in gene regulation
Material Type:
Artigo 		Adicionar ao Meu Espaço

The unique set of putative membrane-associated anti-σ factors in Clostridium thermocellum suggests a novel extracellular carbohydrate-sensing mechanism involved in gene regulation

Kahel-Raifer, Hamutal ; Jindou, Sadanari ; Bahari, Liat ; Nataf, Yakir ; Shoham, Yuval ; Bayer, Edward A ; Borovok, Ilya ; Lamed, Raphael

FEMS microbiology letters, 2010-07, Vol.308 (1), p.84-93 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
8
Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina
Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina
Material Type:
Artigo 		Adicionar ao Meu Espaço

Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina

Stals, Ingeborg ; Samyn, Bart ; Sergeant, Kjell ; White, Theresa ; Hoorelbeke, Katleen ; Coorevits, An ; Devreese, Bart ; Claeyssens, Marc ; Piens, Kathleen

FEMS microbiology letters, 2010-02, Vol.303 (1), p.9-17 [Periódico revisado por pares]

Oxford, UK: Oxford, UK : Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
9
Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)
Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)
Material Type:
Artigo 		Adicionar ao Meu Espaço

Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-β-d-glucosaminidase activity in Streptomyces coelicolor A3(2)

Saito, Akihiro ; Ebise, Hiroki ; Orihara, Yukari ; Murakami, Satoshi ; Sano, Yukari ; Kimura, Akane ; Sugiyama, Yuuta ; Ando, Akikazu ; Fujii, Takeshi ; Miyashita, Kiyotaka

FEMS microbiology letters, 2013-03, Vol.340 (1), p.33-40 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por
10
Family 6 carbohydrate-binding modules display multiple β1,3-linked glucan-specific binding interfaces
Family 6 carbohydrate-binding modules display multiple β1,3-linked glucan-specific binding interfaces
Material Type:
Artigo 		Adicionar ao Meu Espaço

Family 6 carbohydrate-binding modules display multiple β1,3-linked glucan-specific binding interfaces

Correia, Márcia A.S ; Pires, Virgínia M.R ; Gilbert, Harry J ; Bolam, David N ; Fernandes, Vânia O ; Alves, Victor D ; Prates, José A.M ; Ferreira, Luís M.A ; Fontes, Carlos M.G.A

FEMS microbiology letters, 2009-11, Vol.300 (1), p.48-57 [Periódico revisado por pares]

Oxford, UK: Oxford, UK : Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por

Personalize Seus Resultados

  1. Editar

Refine Search Results

Expandir Meus Resultados

  1.   

Data de Publicação 

De até
Refinar
  1. Antes de2004  (1)
  2. 2004Até2005  (2)
  3. 2006Até2006  (3)
  4. 2007Até2009  (3)
  5. Após 2009  (3)
  6. Mais opções open sub menu

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.