scholarly article | Q13442814 |
P6179 | Dimensions Publication ID | 1009620990 |
P356 | DOI | 10.1007/S00284-005-4583-9 |
P2888 | exact match | https://scigraph.springernature.com/pub.10.1007/s00284-005-4583-9 |
P698 | PubMed publication ID | 16450065 |
P2093 | author name string | Michael Smith | |
Dominic W S Wong | |||
Charles C Lee | |||
George H Robertson | |||
Tina G Williams | |||
Kurt Wagschal | |||
Rena E Kibblewhite-Accinelli | |||
P2860 | cites work | Comparison of the genomes of two Xanthomonas pathogens with differing host specificities | Q22122346 |
Updating the sequence-based classification of glycosyl hydrolases | Q24534321 | ||
Basic local alignment search tool | Q25938991 | ||
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates | Q27642761 | ||
Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites | Q27860691 | ||
Biotechnology of microbial xylanases: enzymology, molecular biology, and application | Q28215002 | ||
Xylanases: from biology to biotechnology | Q28298739 | ||
Flavobacterium frigidarium sp. nov., an aerobic, psychrophilic, xylanolytic and laminarinolytic bacterium from Antarctica | Q30657952 | ||
A novel Cellvibrio mixtus family 10 xylanase that is both intracellular and expressed under non-inducing conditions | Q30897942 | ||
Cold-adapted enzymes: from fundamentals to biotechnology. | Q33838253 | ||
Xylanases, xylanase families and extremophilic xylanases | Q36010807 | ||
Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI. | Q36122188 | ||
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A novel family 8 xylanase, functional and physicochemical characterization | Q38287632 | ||
Endo-beta-1,4-xylanase families: differences in catalytic properties | Q38342457 | ||
Enzymatic degradation of cell wall and related plant polysaccharides | Q38618120 | ||
Microbial xylanolytic enzyme system: properties and applications | Q41428392 | ||
Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans | Q42123399 | ||
Nucleotide sequences of xylan-inducible xylanase and xylosidase/arabinosidase genes from Bacteroides ovatus V975. | Q42685421 | ||
A gene encoding a novel extremely thermostable 1,4-beta-xylanase isolated directly from an environmental DNA sample | Q42694518 | ||
A novel cold-tolerant Clostridium strain PXYL1 isolated from a psychrophilic cattle manure digester that secretes thermolabile xylanase and cellulase | Q44320604 | ||
The use of forced protein evolution to investigate and improve stability of family 10 xylanases. The production of Ca2+-independent stable xylanases | Q45081444 | ||
Engineering the thermotolerance and pH optimum of family 11 xylanases by site-directed mutagenesis. | Q51637027 | ||
Glutamic acid 274 is the nucleophile in the active site of a “retaining” exoglucanase from Cellulomonas fimi | Q68312130 | ||
Identification of Flavobacterium columnare by a species-specific polymerase chain reaction and renaming of ATCC43622 strain to Flavobacterium johnsoniae | Q80870928 | ||
P433 | issue | 2 | |
P304 | page(s) | 112-116 | |
P577 | publication date | 2006-01-31 | |
P1433 | published in | Current Microbiology | Q15752443 |
P1476 | title | Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp | |
P478 | volume | 52 |
Q37898189 | Biotechnological uses of enzymes from psychrophiles |
Q90582579 | Characterization of a novel cold-active xylanase from Luteimonas species |
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Q43020756 | Cloning, expression and characterization of a novel cold-active and halophilic xylanase from Zunongwangia profunda |
Q30386304 | Kinetic and thermodynamic characterization of a novel low-temperature-active xylanase from Arthrobacter sp. GN16 isolated from the feces of Grus nigricollis. |
Q33931325 | Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis |
Q51325266 | Production of Glucaric Acid from Hemicellulose Substrate by Rosettasome Enzyme Assemblies. |
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