Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.

The Journal of biological chemistry - 16 Jun 2017

Goodrich Andrew C, Meyers David J, Frueh Dominique P

Abstract excerpt

Nonribosomal peptide synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various processes will deepen our understanding of domain-domain communication in nonribosomal peptide synthetases (NRPSs) and lay the groundwork for the rational reengineering of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apoenzymes
Share to Apoproteins
Share to Carbon Isotopes

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Coenzyme A Ligases

Share to Fluorescence Polarization

Share to Holoenzymes

Share to Nitrogen Isotopes

Share to Titrimetry

Source

Open in PubMed Open full text

Identifiers

PMID: 28455448
DOI: 10.1074/jbc.M116.766220
PMCID: PMC5473208

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.PMID 28455448Read ↗

Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains.Semantic proximity Read ↗

Delineating the reaction mechanism of reductase domains of Nonribosomal Peptide Synthetases from mycobacteria.Semantic proximity Read ↗

Engineering the substrate specificity of the DhbE adenylation domain by yeast cell surface display.Semantic proximity Read ↗

The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases.Semantic proximity Read ↗

Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.Semantic proximity Read ↗

Proximity-Triggered Covalent Stabilization of Low-Affinity Protein Complexes In Vitro and In Vivo.Semantic proximity Read ↗

Precise Probing of Residue Roles by NRPS Code Swapping: Mutation, Enzymatic Characterization, Modeling, and Substrate Promiscuity of Aryl Acid Adenylation Domains.Semantic proximity Read ↗

High-throughput engineering and modification of non-ribosomal peptide synthetases based on Golden Gate assemblySemantic proximity Read ↗

Protein–Protein Interactions in Multienzyme MegasynthetasesSemantic proximity Read ↗

Noncanonical amino acids in the interrogation of cellular protein synthesis.Semantic proximity Read ↗

Engineered interfaces of an AAA+ ATPase reveal a new nucleotide-dependent coordination mechanism.Semantic proximity Read ↗

Urea-Dependent Adenylate Kinase Activation following Redistribution of Structural States.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.