(Q62392169)

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A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I

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A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I (English)

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1

Jerry Ståhlberg

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Gunnar Johansson

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2

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Göran Pettersson

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3

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publication date

March 1991

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published in

Nature Biotechnology

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volume

9

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issue

3

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page(s)

286-290

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https://scigraph.springernature.com/pub.10.1038/nbt0391-286

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Cellulase families revealed by hydrophobic cluster analysis

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7 January 2021

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EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme

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7 January 2021

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Isolated fungal cellulose terminal domains and a synthetic minimum analogue bind to cellulose

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7 January 2021

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Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.

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A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei

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7 January 2021

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Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing

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https://api.crossref.org/works/10.1038%2FNBT0391-286

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7 January 2021

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Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei

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https://api.crossref.org/works/10.1038%2FNBT0391-286

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7 January 2021

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An Algorithm for Least-Squares Estimation of Nonlinear Parameters

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10.1038/NBT0391-286

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1030378855

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(Q62392169)

A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I

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