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1
Expression of industrially relevant laccases: prokaryotic style
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Expression of industrially relevant laccases: prokaryotic style

Trends in biotechnology (Regular ed.), 2011-10, Vol.29 (10), p.480-489 [Peer Reviewed Journal]

Elsevier Ltd ;2011 Elsevier Ltd ;2015 INIST-CNRS ;Copyright © 2011 Elsevier Ltd. All rights reserved. ;Copyright Elsevier Limited Oct 2011 ;ISSN: 0167-7799 ;EISSN: 1879-3096 ;DOI: 10.1016/j.tibtech.2011.04.005 ;PMID: 21640417 ;CODEN: TRBIDM

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2
Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp
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Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp

Applied microbiology and biotechnology, 2015-12, Vol.99 (23), p.9987-9999 [Peer Reviewed Journal]

Springer-Verlag Berlin Heidelberg 2015 ;COPYRIGHT 2015 Springer ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-015-6843-3 ;PMID: 26227413

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3
Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
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Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

Microbial biotechnology, 2017-11, Vol.10 (6), p.1457-1467 [Peer Reviewed Journal]

2016 The Authors. published by John Wiley & Sons Ltd and Society for Applied Microbiology. ;2016 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology. ;2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 1751-7915 ;EISSN: 1751-7915 ;DOI: 10.1111/1751-7915.12422 ;PMID: 27696775

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4
Optimization, purification and characterization of laccase from Ganoderma leucocontextum along with its phylogenetic relationship
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Optimization, purification and characterization of laccase from Ganoderma leucocontextum along with its phylogenetic relationship

Scientific reports, 2022-02, Vol.12 (1), p.2416-2416, Article 2416 [Peer Reviewed Journal]

2022. The Author(s). ;The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2022 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-022-06111-z ;PMID: 35165332

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5
Oxidoreductases on their way to industrial biotransformations
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Oxidoreductases on their way to industrial biotransformations

Attribution-NonCommercial-NoDerivs 4.0 Spain info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/4.0/es/ ;ISSN: 0734-9750 ;EISSN: 1873-1899 ;DOI: 10.1016/j.biotechadv.2017.06.003

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6
Transcriptional analysis of Pleurotus ostreatus laccase genes
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Transcriptional analysis of Pleurotus ostreatus laccase genes

Applied microbiology and biotechnology, 2013-01, Vol.97 (2), p.705-717 [Peer Reviewed Journal]

Springer-Verlag 2012 ;Springer-Verlag 2013 ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-012-3980-9 ;PMID: 22395908

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7
Laccases: structure, function, and potential application in water bioremediation
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Laccases: structure, function, and potential application in water bioremediation

Microbial cell factories, 2019-11, Vol.18 (1), p.200-33, Article 200 [Peer Reviewed Journal]

COPYRIGHT 2019 BioMed Central Ltd. ;COPYRIGHT 2019 BioMed Central Ltd. ;The Author(s) 2019 ;ISSN: 1475-2859 ;EISSN: 1475-2859 ;DOI: 10.1186/s12934-019-1248-0 ;PMID: 31727078

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8
Distribution, mobility, and anchoring of lignin-related oxidative enzymes in Arabidopsis secondary cell walls
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Distribution, mobility, and anchoring of lignin-related oxidative enzymes in Arabidopsis secondary cell walls

Journal of experimental botany, 2018-04, Vol.69 (8), p.1849-1859 [Peer Reviewed Journal]

The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Experimental Biology. 2018 ;Attribution ;ISSN: 0022-0957 ;EISSN: 1460-2431 ;DOI: 10.1093/jxb/ery067 ;PMID: 29481639

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9
Fungal laccases – occurrence and properties
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Fungal laccases – occurrence and properties

FEMS microbiology reviews, 2006-03, Vol.30 (2), p.215-242 [Peer Reviewed Journal]

2005 Federation of European Microbiological Societies. 2005 ;2006 INIST-CNRS ;2005 Federation of European Microbiological Societies. ;ISSN: 0168-6445 ;ISSN: 1574-6976 ;EISSN: 1574-6976 ;DOI: 10.1111/j.1574-4976.2005.00010.x ;PMID: 16472305

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10
Disruption of LACCASE4 and 17 Results in Tissue-Specific Alterations to Lignification of Arabidopsis thaliana Stems
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Disruption of LACCASE4 and 17 Results in Tissue-Specific Alterations to Lignification of Arabidopsis thaliana Stems

The Plant cell, 2011-03, Vol.23 (3), p.1124-1137 [Peer Reviewed Journal]

2011 American Society of Plant Biologists ;Copyright American Society of Plant Biologists Mar 2011 ;Distributed under a Creative Commons Attribution 4.0 International License ;2011 American Society of Plant Biologists 2011 ;ISSN: 1040-4651 ;EISSN: 1532-298X ;DOI: 10.1105/tpc.110.082792 ;PMID: 21447792

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11
Laccase Affects the Rate of Cryptococcus neoformans Nonlytic Exocytosis from Macrophages
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Laccase Affects the Rate of Cryptococcus neoformans Nonlytic Exocytosis from Macrophages

mBio, 2020-09, Vol.11 (5) [Peer Reviewed Journal]

Copyright © 2020 Frazão et al. ;Copyright © 2020 Frazão et al. 2020 Frazão et al. ;ISSN: 2161-2129 ;EISSN: 2150-7511 ;DOI: 10.1128/mBio.02085-20 ;PMID: 32900810

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12
A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases
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A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases

Molecules (Basel, Switzerland), 2021-06, Vol.26 (13), p.3813 [Peer Reviewed Journal]

2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2021 by the authors. 2021 ;ISSN: 1420-3049 ;EISSN: 1420-3049 ;DOI: 10.3390/molecules26133813 ;PMID: 34206669

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13
Application of eukaryotic and prokaryotic laccases in biosensor and biofuel cells: recent advances and electrochemical aspects
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Application of eukaryotic and prokaryotic laccases in biosensor and biofuel cells: recent advances and electrochemical aspects

Applied microbiology and biotechnology, 2018-12, Vol.102 (24), p.10409-10423 [Peer Reviewed Journal]

Springer-Verlag GmbH Germany, part of Springer Nature 2018 ;COPYRIGHT 2018 Springer ;Applied Microbiology and Biotechnology is a copyright of Springer, (2018). All Rights Reserved. ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-018-9421-7 ;PMID: 30327832

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14
Electron transfer and reaction mechanism of laccases
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Article
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Electron transfer and reaction mechanism of laccases

Cellular and molecular life sciences : CMLS, 2015-03, Vol.72 (5), p.869-883 [Peer Reviewed Journal]

Springer Basel 2015 ;ISSN: 1420-682X ;EISSN: 1420-9071 ;DOI: 10.1007/s00018-014-1826-6 ;PMID: 25572295

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15
Laccases: blue enzymes for green chemistry
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Laccases: blue enzymes for green chemistry

Trends in biotechnology (Regular ed.), 2006-05, Vol.24 (5), p.219-226 [Peer Reviewed Journal]

2006 Elsevier Ltd ;2006 INIST-CNRS ;Copyright Elsevier Limited May 2006 ;ISSN: 0167-7799 ;EISSN: 1879-3096 ;DOI: 10.1016/j.tibtech.2006.03.006 ;PMID: 16574262 ;CODEN: TRBIDM

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16
Isolation and Characterization of a Novel Laccase for Lignin Degradation, LacZ1
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Isolation and Characterization of a Novel Laccase for Lignin Degradation, LacZ1

Applied and environmental microbiology, 2021-11, Vol.87 (23), p.e0135521-e0135521 [Peer Reviewed Journal]

Copyright American Society for Microbiology Nov 2021 ;Copyright © 2021 American Society for Microbiology. 2021 American Society for Microbiology ;ISSN: 0099-2240 ;EISSN: 1098-5336 ;DOI: 10.1128/AEM.01355-21 ;PMID: 34524901

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17
Laccase versus laccase-like multi-copper oxidase: a comparative study of similar enzymes with diverse substrate spectra
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Laccase versus laccase-like multi-copper oxidase: a comparative study of similar enzymes with diverse substrate spectra

PloS one, 2013-06, Vol.8 (6), p.e65633-e65633 [Peer Reviewed Journal]

COPYRIGHT 2013 Public Library of Science ;COPYRIGHT 2013 Public Library of Science ;2013 Reiss et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2013 Reiss et al 2013 Reiss et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0065633 ;PMID: 23755261

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18
Biochemical properties and yields of diverse bacterial laccase-like multicopper oxidases expressed in Escherichia coli
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Biochemical properties and yields of diverse bacterial laccase-like multicopper oxidases expressed in Escherichia coli

Scientific reports, 2015-06, Vol.5 (1), p.10465-10465, Article 10465 [Peer Reviewed Journal]

Copyright Nature Publishing Group Jun 2015 ;Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/srep10465 ;PMID: 26068013

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19
Enhanced extracellular production of laccase in Coprinopsis cinerea by silencing chitinase gene
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Enhanced extracellular production of laccase in Coprinopsis cinerea by silencing chitinase gene

Applied microbiology and biotechnology, 2024-12, Vol.108 (1) [Peer Reviewed Journal]

The Author(s) 2024 ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-024-13164-9

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20
An acid-stable bacterial laccase identified from the endophyte Pantoea ananatis Sd-1 genome exhibiting lignin degradation and dye decolorization abilities
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An acid-stable bacterial laccase identified from the endophyte Pantoea ananatis Sd-1 genome exhibiting lignin degradation and dye decolorization abilities

Biotechnology letters, 2015-11, Vol.37 (11), p.2279-2288 [Peer Reviewed Journal]

Springer Science+Business Media Dordrecht 2015 ;ISSN: 0141-5492 ;EISSN: 1573-6776 ;DOI: 10.1007/s10529-015-1914-1 ;PMID: 26209031

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