Creating functional engineered variants of the single-module non-ribosomal peptide synthetase IndC by T domain exchange.
about
L1 regularization facilitates detection of cell type-specific parameters in dynamical systems.Analysis of the linker region joining the adenylation and carrier protein domains of the modular nonribosomal peptide synthetases.Portability of the thiolation domain in recombinant pyoverdine non-ribosomal peptide synthetases.Synthetic Biology of Natural Products.Genetic manipulation of non-ribosomal peptide synthetases to generate novel bioactive peptide products.Synthetic biology advances for pharmaceutical production.Performance of objective functions and optimisation procedures for parameter estimation in system biology models.Recent advances in engineering nonribosomal peptide assembly lines.A sensitive single-enzyme assay system using the non-ribosomal peptide synthetase BpsA for measurement of L-glutamine in biological samples
P2860
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P2860
Creating functional engineered variants of the single-module non-ribosomal peptide synthetase IndC by T domain exchange.
description
2014 nî lūn-bûn
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name
Creating functional engineered ...... ase IndC by T domain exchange.
@en
Creating functional engineered ...... ase IndC by T domain exchange.
@nl
type
label
Creating functional engineered ...... ase IndC by T domain exchange.
@en
Creating functional engineered ...... ase IndC by T domain exchange.
@nl
prefLabel
Creating functional engineered ...... ase IndC by T domain exchange.
@en
Creating functional engineered ...... ase IndC by T domain exchange.
@nl
P2093
P2860
P50
P356
P1433
P1476
Creating functional engineered ...... tase IndC by T domain exchange
@en
P2093
Anja Riedel
Barbara Di Ventura
Dominik Niopek
Florian Schmidt
Hannah Meyer
Johanna Meichsner
Joshua Sachs
Julia Schessner
Katharina Niopek
Nikolaos Ignatiadis
P2860
P304
P356
10.1039/C3MB70594C
P577
2014-07-01T00:00:00Z