Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain. - Test2 - elhamkhani - TriplyDB

Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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Legumain Regulates Differentiation Fate of Human Bone Marrow Stromal Cells and Is Altered in Postmenopausal Osteoporosis.Chemoproteomic profiling and discovery of protein electrophiles in human cells.Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells.Macrocyclization by asparaginyl endopeptidases.Protease activity of legumain is inhibited by an increase of cystatin E/M in the DJ-1-knockout mouse spleen, cerebrum and heart.Distinct Roles of Catalytic Cysteine and Histidine in the Protease and Ligase Mechanisms of Human Legumain As Revealed by DFT-Based QM/MM Simulations.Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase.Structural basis of ribosomal peptide macrocyclization in plants.Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation.Structural analyses of Arabidopsis thaliana legumain γ reveal the differential recognition and processing of proteolysis and ligation substrates.

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Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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2015 nî lūn-bûn

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Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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Angewandte Chemie International Edition

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Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

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Julia C Fegg

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P2860

ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase.

Asparagine endopeptidase controls anti-influenza virus immune responses through TLR7 activation

Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation

Structural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage

Insights into the regulatory mechanism for caspase-8 activation

Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase.

Evolution, mechanisms, and applications of intein-mediated protein splicing.

Discovery of an allosteric site in the caspases

Cystatin E/M suppresses legumain activity and invasion of human melanoma

Regulation of gamma-glutamylcysteine synthetase expression in response to oxidative stress.

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2917-2921

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