Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase.
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Natural structural diversity within a conserved cyclic peptide scaffoldEnzymatic Macrocyclization of 1,2,3-Triazole Peptide MimeticsQ28828613Immunolocalization of cyclotides in plant cells, tissues and organ supports their role in host defense.Oral activity of a nature-derived cyclic peptide for the treatment of multiple sclerosis.Unveiling the diversity of cyclotides by combining peptidome and transcriptome analysis.Cyclic peptide oral bioavailability: Lessons from the past.Discovery, structure, function, and applications of cyclotides: circular proteins from plants.Discovery and optimization of peptide macrocycles.Macrocyclization by asparaginyl endopeptidases.Cyclotides: Overview and Biotechnological Applications.Distinct Roles of Catalytic Cysteine and Histidine in the Protease and Ligase Mechanisms of Human Legumain As Revealed by DFT-Based QM/MM Simulations.Kinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase.Cyclotides, a versatile ultrastable micro-protein scaffold for biotechnological applications.Co-expression of a cyclizing asparaginyl endopeptidase enables efficient production of cyclic peptides in planta.Structural basis of ribosomal peptide macrocyclization in plants.Two proteins for the price of one: Structural studies of the dual-destiny protein preproalbumin with sunflower trypsin inhibitor-1.Enzymatic N- and C-Protection in Cyanobactin RiPP Natural Products.Cyclotide Evolution: Insights from the Analyses of Their Precursor Sequences, Structures and Distribution in Violets (Viola).Overexpression of asparaginyl endopeptidase is significant for esophageal carcinoma metastasis and predicts poor patient prognosis.Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation.Segmental isotopic labeling of a single-domain globular protein without any refolding step by an asparaginyl endopeptidase.Pinpointing disulfide connectivities in cysteine-rich proteins.Butelase-mediated cyclization and ligation of peptides and proteins.The N-terminal pro-domain of the kalata B1 cyclotide precursor is intrinsically unstructured.Structural analyses of Arabidopsis thaliana legumain γ reveal the differential recognition and processing of proteolysis and ligation substrates.Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases.
P2860
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P2860
Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@en
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@nl
type
label
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@en
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@nl
prefLabel
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@en
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@nl
P2093
P2860
P50
P356
P1476
Efficient backbone cyclization ...... ant asparaginyl endopeptidase.
@en
P2093
Ivana Saska
Karen S Harris
Nicole L van der Weerden
P2860
P2888
P356
10.1038/NCOMMS10199
P407
P50
P577
2015-12-18T00:00:00Z