J
Jean-Pierre Belaich
Researcher at Centre national de la recherche scientifique
Publications - 77
Citations - 5331
Jean-Pierre Belaich is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Clostridium cellulolyticum & Cellulosome. The author has an hindex of 43, co-authored 77 publications receiving 5142 citations. Previous affiliations of Jean-Pierre Belaich include University of Provence.
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Journal ArticleDOI
The Cellulosomes: Multienzyme Machines for Degradation of Plant Cell Wall Polysaccharides
TL;DR: The recently described three-dimensional crystal structure of the cohesin-dockerin heterodimer sheds light on the critical amino acids that contribute to this high-affinity protein-protein interaction.
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Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin.
Henri-Pierre Fierobe,Florence Mingardon,Adva Mechaly,Anne Belaich,Marco T. Rincon,Sandrine Pagès,Sandrine Pagès,Raphael Lamed,Chantal Tardif,Chantal Tardif,Jean-Pierre Belaich,Jean-Pierre Belaich,Edward A. Bayer +12 more
TL;DR: The results indicate that the synergy between two prominent cellulosomal enzymes plays a crucial role during the degradation of cellulose by cellulosomes and that one dominant family-48 processive endoglucanase per complex is sufficient to achieve optimal levels of synergistic activity.
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Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain.
Sandrine Pagès,Anne Belaich,Jean-Pierre Belaich,Jean-Pierre Belaich,Ely Morag,Raphael Lamed,Yuval Shoham,Edward A. Bayer +7 more
TL;DR: Based on intra‐ and cross‐species sequence comparisons among the different dockerins together with their known specificities, a prediction as to the amino‐acid residues critical to recognition of the cohesins is tender.
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Design and Production of Active Cellulosome Chimeras SELECTIVE INCORPORATION OF DOCKERIN-CONTAINING ENZYMES INTO DEFINED FUNCTIONAL COMPLEXES
Henri-Pierre Fierobe,Adva Mechaly,Chantal Tardif,Chantal Tardif,Anne Belaich,Raphael Lamed,Yuval Shoham,Jean-Pierre Belaich,Jean-Pierre Belaich,Edward A. Bayer +9 more
TL;DR: Defined chimeric cellulosomes were produced in which selected enzymes were incorporated in specific locations within a multicomponent complex, and the resultant cellulosome chimeras exhibited enhanced synergistic action on crystalline cellulose.
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The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: purification and characterization of the recombinant form.
TL;DR: The recombinant form of the cellulase CelF of Clostridium cellulolyticum, tagged by a C-terminal histine tail, was overproduced in Escherichia coli and was identified as one of the three major components of cellulosomes.