skip to main content
Mostrar Somente
Refinado por: data de publicação: 2009Até2012 remover
Result Number Material Type Add to My Shelf Action Record Details and Options
1
Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications
Material Type:
Artigo
Adicionar ao Meu Espaço

Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications

Lammens, Willem ; Le Roy, Katrien ; Schroeven, Lindsey ; Van Laere, André ; Rabijns, Anja ; Van den Ende, Wim

Journal of Experimental Botany, 2009-03, Vol.60 (3), p.727-740 [Periódico revisado por pares]

Oxford: Oxford University Press

Texto completo disponível

2
Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity
Material Type:
Artigo
Adicionar ao Meu Espaço

Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity

Burstein, Tal ; Shulman, Michal ; Jindou, Sadanari ; Petkun, Svetlana ; Frolow, Felix ; Shoham, Yuval ; Bayer, Edward A. ; Lamed, Raphael

FEBS letters, 2009-03, Vol.583 (5), p.879-884 [Periódico revisado por pares]

England: Elsevier B.V

Texto completo disponível

3
Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellum
Material Type:
Artigo
Adicionar ao Meu Espaço

Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellum

Bahari, Liat ; Gilad, Yuval ; Borovok, Ilya ; Kahel-Raifer, Hamutal ; Dassa, Bareket ; Nataf, Yakir ; Shoham, Yuval ; Lamed, Raphael ; Bayer, Edward A

Journal of industrial microbiology & biotechnology, 2011-07, Vol.38 (7), p.825-832 [Periódico revisado por pares]

Berlin/Heidelberg: Springer-Verlag

Texto completo disponível

4
An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure
Material Type:
Artigo
Adicionar ao Meu Espaço

An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure

Ling, Naomi X.-Y. ; Lee, Joanne ; Ellis, Miriam ; Liao, Ming-Long ; Mau, Shaio-Lim ; Guest, David ; Janssen, Peter H. ; Kováč, Pavol ; Bacic, Antony ; Pettolino, Filomena A.

Carbohydrate research, 2012-05, Vol.352, p.70-81 [Periódico revisado por pares]

Netherlands: Elsevier Ltd

Texto completo disponível

5
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

6
Heterologous expression of glycoside hydrolase family 2 and 42 β-galactosidases of lactic acid bacteria in Lactococcus lactis
Material Type:
Artigo
Adicionar ao Meu Espaço

Heterologous expression of glycoside hydrolase family 2 and 42 β-galactosidases of lactic acid bacteria in Lactococcus lactis

Schwab, Clarissa ; Sørensen, Kim I. ; Gänzle, Michael G.

Systematic and applied microbiology, 2010-10, Vol.33 (6), p.300-307 [Periódico revisado por pares]

München: Elsevier GmbH

Texto completo disponível

7
Characterization of a GH family 3 β-glycoside hydrolase from Chrysosporium lucknowense and its application to the hydrolysis of β-glucan and xylan
Material Type:
Artigo
Adicionar ao Meu Espaço

Characterization of a GH family 3 β-glycoside hydrolase from Chrysosporium lucknowense and its application to the hydrolysis of β-glucan and xylan

Dotsenko, G.S. ; Sinitsyna, O.A. ; Hinz, S.W.A. ; Wery, J. ; Sinitsyn, A.P.

Bioresource technology, 2012-05, Vol.112, p.345-349 [Periódico revisado por pares]

England: Elsevier Ltd

Texto completo disponível

8
Characterization of endo-1,3-1,4-β-glucanases in GH family 12 from Magnaporthe oryzae
Material Type:
Artigo
Adicionar ao Meu Espaço

Characterization of endo-1,3-1,4-β-glucanases in GH family 12 from Magnaporthe oryzae

Takeda, Takumi ; Takahashi, Machiko ; Nakanishi-Masuno, Tsugumi ; Nakano, Yuki ; Saitoh, Hiromasa ; Hirabuchi, Akiko ; Fujisawa, Shizuko ; Terauchi, Ryohei

Applied microbiology and biotechnology, 2010-11, Vol.88 (5), p.1113-1123 [Periódico revisado por pares]

Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag

Texto completo disponível

9
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

10
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

Personalize Seus Resultados

  1. Editar

Refine Search Results

Expandir Meus Resultados

  1.   

Mostrar Somente

  1. Revistas revisadas por pares (16)

Data de Publicação 

De até

Buscando em bases de dados remotas. Favor aguardar.