On the public citation graph

Minimal lactazole scaffold for in vitro production of pseudo-natural thiopeptides

0 signed · 73 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/anie.201307288openalex-snapshot
Thiopeptide Engineering: A Multidisciplinary Effort towards Future Drugs
inferredcites →https://doi.org/10.1002/anie.201604345openalex-snapshot
Leader Peptide‐Free In Vitro Reconstitution of Microviridin Biosynthesis Enables Design of Synthetic Protease‐Targeted Libraries
inferredcites →https://doi.org/10.1002/anie.201609079openalex-snapshot
Nonribosomal Peptide Synthesis—Principles and Prospects
inferredcites →https://doi.org/10.1002/bip.21416openalex-snapshot
Ribosomal biosynthesis of the cyclic peptide toxins of Amanita mushrooms
inferredcites →https://doi.org/10.1002/cbic.201500541openalex-snapshot
Insights into the Biosynthesis of Dehydroalanines in Goadsporin
inferredcites →https://doi.org/10.1002/cbic.201900521openalex-snapshot
In Vitro Biosynthesis of Peptides Containing Exotic Azoline Analogues
inferredcites →https://doi.org/10.1016/j.cbpa.2012.01.018openalex-snapshot
Combinatorial biosynthesis of polyketides — a perspective
inferredcites →https://doi.org/10.1016/j.cbpa.2015.11.016openalex-snapshot
Combinatorial biosynthesis of RiPPs: docking with marine life
inferredcites →https://doi.org/10.1016/j.cbpa.2018.06.014openalex-snapshot
Engineering of RiPP pathways for the production of artificial peptides bearing various non-proteinogenic structures
inferredcites →https://doi.org/10.1016/j.cell.2014.08.032openalex-snapshot
A Systematic Analysis of Biosynthetic Gene Clusters in the Human Microbiome Reveals a Common Family of Antibiotics
inferredcites →https://doi.org/10.1016/j.chembiol.2009.01.007openalex-snapshot
Thiopeptide Biosynthesis Featuring Ribosomally Synthesized Precursor Peptides and Conserved Posttranslational Modifications
inferredcites →https://doi.org/10.1016/j.chembiol.2012.10.013openalex-snapshot
Codon Randomization for Rapid Exploration of Chemical Space in Thiopeptide Antibiotic Variants
inferredcites →https://doi.org/10.1016/j.chembiol.2014.03.008openalex-snapshot
Genome Mining Reveals a Minimum Gene Set for the Biosynthesis of 32-Membered Macrocyclic Thiopeptides Lactazoles
inferredcites →https://doi.org/10.1016/j.chembiol.2014.04.008openalex-snapshot
One-Pot Synthesis of Azoline-Containing Peptides in a Cell-free Translation System Integrated with a Posttranslational Cyclodehydratase
inferredcites →https://doi.org/10.1016/j.chembiol.2015.06.014openalex-snapshot
Modularity of RiPP Enzymes Enables Designed Synthesis of Decorated Peptides
inferredcites →https://doi.org/10.1016/j.chembiol.2015.11.017openalex-snapshot
Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis
inferredcites →https://doi.org/10.1016/j.mib.2018.02.010openalex-snapshot
RiPP antibiotics: biosynthesis and engineering potential
inferredcites →https://doi.org/10.1016/j.molcel.2018.11.032openalex-snapshot
Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison
inferredcites →https://doi.org/10.1021/acs.biochem.8b00835openalex-snapshot
Oxidation of the Cyanobactin Precursor Peptide Is Independent of the Leader Peptide and Operates in a Defined Order
inferredcites →https://doi.org/10.1021/acs.chemrev.6b00523openalex-snapshot
Aminoacyl-tRNA-Utilizing Enzymes in Natural Product Biosynthesis
inferredcites →https://doi.org/10.1021/acs.chemrev.6b00591openalex-snapshot
Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes
inferredcites →https://doi.org/10.1021/acs.chemrev.6b00623openalex-snapshot
YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function
inferredcites →https://doi.org/10.1021/acs.chemrev.8b00430openalex-snapshot
RNA Display Methods for the Discovery of Bioactive Macrocycles
inferredcites →https://doi.org/10.1021/acscentsci.7b00141openalex-snapshot
Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products
inferredcites →https://doi.org/10.1021/acscentsci.7b00581openalex-snapshot
Development and Application of Yeast and Phage Display of Diverse Lanthipeptides
inferredcites →https://doi.org/10.1021/acssynbio.9b00080openalex-snapshot
Assessing the Flexibility of the Prochlorosin 2.8 Scaffold for Bioengineering Applications
inferredcites →https://doi.org/10.1021/bi401529yopenalex-snapshot
Orchestration of Enzymatic Processing by Thiazole/Oxazole-Modified Microcin Dehydrogenases
inferredcites →https://doi.org/10.1021/cb5007745openalex-snapshot
Saturation Mutagenesis of TsrA Ala4 Unveils a Highly Mutable Residue of Thiostrepton A
inferredcites →https://doi.org/10.1021/cr0300441openalex-snapshot
Thiopeptide Antibiotics
inferredcites →https://doi.org/10.1021/ja102339qopenalex-snapshot
Manipulation of Thiocillin Variants by Prepeptide Gene Replacement: Structure, Conformation, and Activity of Heterocycle Substitution Mutants
inferredcites →https://doi.org/10.1021/ja302820xopenalex-snapshot
Generation of Thiocillin Ring Size Variants by Prepeptide Gene Replacement and in Vivo Processing by Bacillus cereus
inferredcites →https://doi.org/10.1021/ja807890aopenalex-snapshot
Thiostrepton Biosynthesis: Prototype for a New Family of Bacteriocins
inferredcites →https://doi.org/10.1021/ja900488aopenalex-snapshot
Ribosomally Synthesized Thiopeptide Antibiotics Targeting Elongation Factor Tu
inferredcites →https://doi.org/10.1021/ja908777topenalex-snapshot
Generation of Thiocillin Variants by Prepeptide Gene Replacement and in Vivo Processing by Bacillus cereus
inferredcites →https://doi.org/10.1021/jacs.5b00940openalex-snapshot
Chemoenzymatic Synthesis of Thiazolyl Peptide Natural Products Featuring an Enzyme-Catalyzed Formal [4 + 2] Cycloaddition
inferredcites →https://doi.org/10.1021/jacs.5b10194openalex-snapshot
In Vitro Biosynthesis of the Core Scaffold of the Thiopeptide Thiomuracin
inferredcites →https://doi.org/10.1021/jacs.6b05389openalex-snapshot
Identification of Pyridine Synthase Recognition Sequences Allows a Modular Solid-Phase Route to Thiopeptide Variants
inferredcites →https://doi.org/10.1021/jacs.6b08987openalex-snapshot
Biosynthetic Timing and Substrate Specificity for the Thiopeptide Thiomuracin
inferredcites →https://doi.org/10.1021/jacs.6b10792openalex-snapshot
Structure–Activity Relationship and Molecular Mechanics Reveal the Importance of Ring Entropy in the Biosynthesis and Activity of a Natural Product
inferredcites →https://doi.org/10.1021/jacs.7b00693openalex-snapshot
Reconstitution and Substrate Specificity of the Radical S-Adenosyl-methionine Thiazole C-Methyltransferase in Thiomuracin Biosynthesis
inferredcites →https://doi.org/10.1021/jacs.7b01497openalex-snapshot
Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK
inferredcites →https://doi.org/10.1021/jacs.7b08492openalex-snapshot
NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide
inferredcites →https://doi.org/10.1021/jacs.8b03896openalex-snapshot
Bioinformatic Expansion and Discovery of Thiopeptide Antibiotics
inferredcites →https://doi.org/10.1021/jacs.8b04238openalex-snapshot
Biosynthesis of the Thiopeptins and Identification of an F420H2-Dependent Dehydropiperidine Reductase
inferredcites →https://doi.org/10.1021/jacs.8b11521openalex-snapshot
Flexizyme-Enabled Benchtop Biosynthesis of Thiopeptides
inferredcites →https://doi.org/10.1021/jacs.8b11852openalex-snapshot
Thiopeptide Pyridine Synthase TbtD Catalyzes an Intermolecular Formal Aza-Diels–Alder Reaction
inferredcites →https://doi.org/10.1021/jm101602qopenalex-snapshot
4-Aminothiazolyl Analogues of GE2270 A: Antibacterial Lead Finding
inferredcites →https://doi.org/10.1021/jm201685hopenalex-snapshot
Discovery of LFF571: An Investigational Agent for Clostridium difficile Infection
inferredcites →https://doi.org/10.1021/jm300783copenalex-snapshot
Antibiotic Optimization and Chemical Structure Stabilization of Thiomuracin A
inferredcites →https://doi.org/10.1021/sb500267dopenalex-snapshot
Assessing the Combinatorial Potential of the RiPP Cyanobactin tru Pathway
inferredcites →https://doi.org/10.1038/nature13888openalex-snapshot
Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
inferredcites →https://doi.org/10.1038/nchem.2666openalex-snapshot
Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium
inferredcites →https://doi.org/10.1038/nchembio.1608openalex-snapshot
Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis
inferredcites →https://doi.org/10.1038/nchembio.1841openalex-snapshot
Structural analysis of leader peptide binding enables leader-free cyanobactin processing
inferredcites →https://doi.org/10.1038/nchembio.1856openalex-snapshot
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis
inferredcites →https://doi.org/10.1038/nchembio.1893openalex-snapshot
Reinvigorating natural product combinatorial biosynthesis with synthetic biology
inferredcites →https://doi.org/10.1038/nchembio.2393openalex-snapshot
Autocatalytic backbone N-methylation in a family of ribosomal peptide natural products
inferredcites →https://doi.org/10.1038/ncomms14207openalex-snapshot
Dissection of goadsporin biosynthesis by in vitro reconstitution leading to designer analogues expressed in vivo
inferredcites →https://doi.org/10.1038/nprot.2011.331openalex-snapshot
Flexizymes for genetic code reprogramming
inferredcites →https://doi.org/10.1038/s41467-017-00439-1openalex-snapshot
Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ
inferredcites →https://doi.org/10.1038/s41467-017-01413-7openalex-snapshot
Phage display and selection of lanthipeptides on the carboxy-terminus of the gene-3 minor coat protein
inferredcites →https://doi.org/10.1038/s41589-018-0008-5openalex-snapshot
A lanthipeptide library used to identify a protein–protein interaction inhibitor
inferredcites →https://doi.org/10.1038/s41589-019-0250-5openalex-snapshot
Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale
inferredcites →https://doi.org/10.1039/c2np20085fopenalex-snapshot
Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature
inferredcites →https://doi.org/10.1039/c5ob01336dopenalex-snapshot
Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming
inferredcites →https://doi.org/10.1039/c6ra20302gopenalex-snapshot
Mutagenesis of precursor peptide for the generation of nosiheptide analogues
inferredcites →https://doi.org/10.1073/pnas.0900008106openalex-snapshot
Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
inferredcites →https://doi.org/10.1073/pnas.1307111110openalex-snapshot
The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffolds
inferredcites →https://doi.org/10.1073/pnas.1602733113openalex-snapshot
Recombinant thiopeptides containing noncanonical amino acids
inferredcites →https://doi.org/10.1073/pnas.1716035114openalex-snapshot
Structural insights into enzymatic [4+2] aza -cycloaddition in thiopeptide antibiotic biosynthesis
inferredcites →https://doi.org/10.1128/aac.04251-14openalex-snapshot
Multicenter, Randomized Clinical Trial To Compare the Safety and Efficacy of LFF571 and Vancomycin for Clostridium difficile Infections
inferredcites →https://doi.org/10.1128/jb.00396-16openalex-snapshot
Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis
inferredcites →https://doi.org/10.3390/md12010317openalex-snapshot
Thiopeptide Antibiotics: Retrospective and Recent Advances
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.