Detalhe da pesquisa
1.
Molecular mechanism of the chitinolytic peroxygenase reaction.
Proc Natl Acad Sci U S A;
117(3): 1504-1513, 2020 01 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-31907317
2.
Outer membrane vesicles catabolize lignin-derived aromatic compounds in Pseudomonas putida KT2440.
Proc Natl Acad Sci U S A;
117(17): 9302-9310, 2020 04 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-32245809
3.
Characterization and engineering of a two-enzyme system for plastics depolymerization.
Proc Natl Acad Sci U S A;
117(41): 25476-25485, 2020 10 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-32989159
4.
Passive membrane transport of lignin-related compounds.
Proc Natl Acad Sci U S A;
116(46): 23117-23123, 2019 11 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-31659054
5.
The dissociation mechanism of processive cellulases.
Proc Natl Acad Sci U S A;
116(46): 23061-23067, 2019 11 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-31666327
6.
Nanomechanics of cellulose deformation reveal molecular defects that facilitate natural deconstruction.
Proc Natl Acad Sci U S A;
116(20): 9825-9830, 2019 05 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-31036649
7.
Enabling microbial syringol conversion through structure-guided protein engineering.
Proc Natl Acad Sci U S A;
116(28): 13970-13976, 2019 07 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-31235604
8.
Characterization and engineering of a plastic-degrading aromatic polyesterase.
Proc Natl Acad Sci U S A;
115(19): E4350-E4357, 2018 05 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-29666242
9.
Promoting microbial utilization of phenolic substrates from bio-oil.
J Ind Microbiol Biotechnol;
46(11): 1531-1545, 2019 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-31270700
10.
Lignin valorization through integrated biological funneling and chemical catalysis.
Proc Natl Acad Sci U S A;
111(33): 12013-8, 2014 Aug 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-25092344
11.
Specificity of O-glycosylation in enhancing the stability and cellulose binding affinity of Family 1 carbohydrate-binding modules.
Proc Natl Acad Sci U S A;
111(21): 7612-7, 2014 May 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-24821760
12.
Biochemical and Structural Characterizations of Two Dictyostelium Cellobiohydrolases from the Amoebozoa Kingdom Reveal a High Level of Conservation between Distant Phylogenetic Trees of Life.
Appl Environ Microbiol;
82(11): 3395-409, 2016 06 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-27037126
13.
Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.
Proc Natl Acad Sci U S A;
110(36): 14646-51, 2013 Sep 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-23959893
14.
Aromatic catabolic pathway selection for optimal production of pyruvate and lactate from lignin.
Metab Eng;
28: 240-247, 2015 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-25617773
15.
Structural, biochemical, and computational characterization of the glycoside hydrolase family 7 cellobiohydrolase of the tree-killing fungus Heterobasidion irregulare.
J Biol Chem;
288(8): 5861-72, 2013 Feb 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-23303184
16.
The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies.
J Am Chem Soc;
136(1): 321-9, 2014 Jan 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-24341799
17.
Charge engineering of cellulases improves ionic liquid tolerance and reduces lignin inhibition.
Biotechnol Bioeng;
111(8): 1541-9, 2014 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-24522957
18.
Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity.
Biophys J;
104(4): 904-12, 2013 Feb 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-23442969
19.
Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose.
J Biol Chem;
287(24): 20603-12, 2012 Jun 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-22496371
20.
Product binding varies dramatically between processive and nonprocessive cellulase enzymes.
J Biol Chem;
287(29): 24807-13, 2012 Jul 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-22648408