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Cited by 386

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Monolignol Ferulate Transferase Introduces Chemically Labile Linkages into the Lignin Backbone

Wilkerson, C. G., Mansfield, S. D., Lu, F., Withers, S., Park, J.-Y., Karlen, S. D., Gonzales-Vigil, E., Padmakshan, D., Unda, F., Rencoret, J., Ralph, J.·2014·Science

Abstract

Constructed for Deconstruction: Lignin provides strength to wood but also impedes efficient degradation when wood is used as biofuel. Wilkerson et al. (p. 90 ) engineered poplar to produce lignin that is more amenable to degradation. From a handful of plants that contain more digestible lignin monomers, Angelica sinensis was selected and its monolignol transferase activities analyzed. The enzyme involved, coniferyl ferulate feruloyl-CoA monolignol transferase, was then expressed in poplar. The resulting poplar trees showed no difference in growth habit under greenhouse conditions, but their lignin showed improved digestibility.

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Metadata

Authors
Wilkerson, C. G., Mansfield, S. D., Lu, F., Withers, S., Park, J.-Y., Karlen, S. D., Gonzales-Vigil, E., Padmakshan, D., Unda, F., Rencoret, J., & Ralph, J.
Venue
Science
Published
2014-04-04
Volume
344
Issue
6179
Pages
90-93
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2015677629
Cited by
386
References
0
FWCI
21.02
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Monolignol Ferulate Transferase Introduces Chemically Labile Linkages into the Lignin Backbone. https://app.cochat.ai/papers/10.1126/science.1250161
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Wilkerson, C. G., Mansfield, S. D., Lu, F., Withers, S., Park, J.-Y., Karlen, S. D., Gonzales-Vigil, E., Padmakshan, D., Unda, F., Rencoret, J., & Ralph, J. (2014). Monolignol Ferulate Transferase Introduces Chemically Labile Linkages into the Lignin Backbone. Science. https://doi.org/10.1126/science.1250161

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.