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Monocyclic β-Lactams Are Selective, Mechanism-Based Inhibitors of Rhomboid Intramembrane Proteases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels
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Normal Mitochondrial Dynamics Requires Rhomboid-7 and Affects Drosophila Lifespan and Neuronal Function
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Sequence-Specific Intramembrane Proteolysis: Identification of a Recognition Motif in Rhomboid Substrates
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Esters of Methanesulfonic Acid as Irreversible Inhibitors of Acetylcholinesterase
inferredcites →https://doi.org/10.1016/s0092-8674(01)00525-6openalex-snapshot
Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine Proteases
inferredcites →https://doi.org/10.1016/s0092-8674(01)00526-8openalex-snapshot
Regulated Intracellular Ligand Transport and Proteolysis Control EGF Signal Activation in Drosophila
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Conservation of Intramembrane Proteolytic Activity and Substrate Specificity in Prokaryotic and Eukaryotic Rhomboids
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Complementation Cloning of , a Gene Encoding a Putative Metalloprotease Required for Intramembrane Cleavage of SREBPs
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Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor
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Reaction of serine proteases with substituted 3-alkoxy-4-chloroisocoumarins and 3-alkoxy-7-amino-4-chloroisocoumarins: new reactive mechanism-based inhibitors
inferredcites →https://doi.org/10.1021/bi051363kopenalex-snapshot
Proteolytic Action of GlpG, a Rhomboid Protease in the Escherichia coli Cytoplasmic Membrane
inferredcites →https://doi.org/10.1021/cr010182vopenalex-snapshot
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
inferredcites →https://doi.org/10.1038/34910openalex-snapshot
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
inferredcites →https://doi.org/10.1038/emboj.2010.243openalex-snapshot
The structural basis for catalysis and substrate specificity of a rhomboid protease
inferredcites →https://doi.org/10.1038/nature01633openalex-snapshot
Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
inferredcites →https://doi.org/10.1038/nature05255openalex-snapshot
Crystal structure of a rhomboid family intramembrane protease
inferredcites →https://doi.org/10.1038/nrmicro2130openalex-snapshot
Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms
inferredcites →https://doi.org/10.1038/sj.emboj.7600537openalex-snapshot
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
inferredcites →https://doi.org/10.1073/pnas.0408306102openalex-snapshot
Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
inferredcites →https://doi.org/10.1073/pnas.0608140104openalex-snapshot
Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase
inferredcites →https://doi.org/10.1074/jbc.m211311200openalex-snapshot
Processing of Mgm1 by the Rhomboid-type Protease Pcp1 Is Required for Maintenance of Mitochondrial Morphology and of Mitochondrial DNA
inferredcites →https://doi.org/10.1083/jcb.200604136openalex-snapshot
Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite
inferredcites →https://doi.org/10.1093/emboj/cdf434openalex-snapshot
A family of Rhomboid intramembrane proteases activates all Drosophila membrane‐tethered EGF ligands
inferredcites →https://doi.org/10.1124/pr.55.4.4openalex-snapshot
International Union of Pharmacology Committee on Receptor Nomenclature and Drug Classification. XXXVIII. Update on Terms and Symbols in Quantitative Pharmacology
inferredcites →https://doi.org/10.1126/science.1070925openalex-snapshot
Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease
inferredcites →https://doi.org/10.1128/ec.00015-10openalex-snapshot
Downregulation of an Entamoeba histolytica Rhomboid Protease Reveals Roles in Regulating Parasite Adhesion and Phagocytosis
inferredcites →https://doi.org/10.1146/annurev.genet.42.110807.091628openalex-snapshot
Rhomboid Proteases and their Biological Functions
inferredcites →https://doi.org/10.1177/108705719900400206openalex-snapshot
A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
inferredcites →https://doi.org/10.1371/journal.ppat.0020113openalex-snapshot
Two Plasmodium Rhomboid Proteases Preferentially Cleave Different Adhesins Implicated in All Invasive Stages of Malaria
inferredcites →https://doi.org/10.1371/journal.ppat.1000262openalex-snapshot
Distinct Roles of Plasmodium Rhomboid 1 in Parasite Development and Malaria Pathogenesis
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Extensive Targeting of Chemical Space at the Prime Side of Ketoamide Inhibitors of Rhomboid Proteases by Branched Substituents Empowers Their Selectivity and Potency
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Stepwise Versus Concerted Mechanisms in General‐Base Catalysis by Serine Proteases
inferred← citeshttps://doi.org/10.1002/ange.202207354openalex-snapshot
Ligand‐Enabled β‐C(sp3)−H Lactamization of Tosyl‐Protected Aliphatic Amides Using a Practical Oxidant
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Targeting the Membrane‐Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight
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Stepwise Versus Concerted Mechanisms in General‐Base Catalysis by Serine Proteases
inferred← citeshttps://doi.org/10.1002/anie.202207354openalex-snapshot
Ligand‐Enabled β‐C(sp3)−H Lactamization of Tosyl‐Protected Aliphatic Amides Using a Practical Oxidant
inferred← citeshttps://doi.org/10.1002/anie.202514067openalex-snapshot
Targeting the Membrane‐Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight
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Activity‐Based Protein Profiling of Rhomboid Proteases in Liposomes
inferred← citeshttps://doi.org/10.1002/cbic.202300418openalex-snapshot
4‐Oxo‐β‐Lactams as Novel Inhibitors for Rhomboid Proteases
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Towards a General Synthesis of 3‐Metal‐Substituted β‐Lactams
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A New Oxopiperazin‐Based Peptidomimetic Molecule Inhibits Prostatic Acid Phosphatase Secretion and Induces Prostate Cancer Cell Apoptosis
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Embedded in the Membrane: How Lipids Confer Activity and Specificity to Intramembrane Proteases
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Drosophila Rhomboid-1
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Mammalian Rhomboid Proteases
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Bacterial and Protozoan Rhomboid Proteases
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Mechanism and Inhibition of Rhomboid Proteases
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.11.002openalex-snapshot
Activity Assays for Rhomboid Proteases
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Rhomboid proteases in human disease: Mechanisms and future prospects
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Emerging role of rhomboid family proteins in mammalian biology and disease
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Untangling structure–function relationships in the rhomboid family of intramembrane proteases
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Isolation of intramembrane proteases in membrane-like environments
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Inhibitors of rhomboid proteases
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Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases
inferred← citeshttps://doi.org/10.1016/j.bmcl.2018.02.017openalex-snapshot
Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2021.128290openalex-snapshot
Development of succinimide-based inhibitors for the mitochondrial rhomboid protease PARL
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Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity
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General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases
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Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases
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Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency
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An in vitro platform for the enzymatic characterization of the rhomboid protease RHBDL4
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New insights into parasite rhomboid proteases
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Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis
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Rhomboid protease inhibitors: Emerging tools and future therapeutics
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Structure of Rhomboid Protease in Complex with β-Lactam Inhibitors Defines the S2′ Cavity
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Stereoselective synthesis of sugar-based β-lactam derivatives: docking studies and its biological evaluation
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The Rhomboid Superfamily: Structural Mechanisms and Chemical Biology Opportunities
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Discovery and Biological Evaluation of Potent and Selective N-Methylene Saccharin-Derived Inhibitors for Rhomboid Intramembrane Proteases
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Gold as Catalyst for the Hydroarylation and Domino Hydroarylation/N1–C4 Cleavage of β-Lactam-Tethered Allenyl Indoles
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Inhibitor Fingerprinting of Rhomboid Proteases by Activity-Based Protein Profiling Reveals Inhibitor Selectivity and Rhomboid Autoprocessing
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Chemical Tools for the Study of Intramembrane Proteases
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Discovery of Cellular Roles of Intramembrane Proteases
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4-Oxo-β-lactams as Covalent Inhibitors of the Mitochondrial Intramembrane Protease PARL
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Activity-Based Protein Profiling of the Escherichia coli GlpG Rhomboid Protein Delineates the Catalytic Core
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The Catalytic Machinery of Rhomboid Proteases: Combined MD and QM Simulations
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Synthesis of chiral carbocycles via enantioselective β,γ-dehydrogenation
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The enzymes of β-lactam biosynthesis
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Enantioselective cis-β-lactam synthesis by intramolecular C–H functionalization from enoldiazoacetamides and derivative donor–acceptor cyclopropenes
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Rapid synthesis of internal peptidyl α-ketoamides by on resin oxidation for the construction of rhomboid protease inhibitors
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Correction: Rapid synthesis of internal peptidyl α-ketoamides by on resin oxidation for the construction of rhomboid protease inhibitors
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Activity-based probes for rhomboid proteases discovered in a mass spectrometry-based assay
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Sensitive Versatile Fluorogenic Transmembrane Peptide Substrates for Rhomboid Intramembrane Proteases
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Structure and Mechanism of Rhomboid Protease
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Structural and mechanistic principles of intramembrane proteolysis – lessons from rhomboids
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Intramembrane proteases as drug targets
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Regulated Intramembrane Cleavage of the EGF Receptor
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Therapeutic Potential of Targeting Regulated Intramembrane Proteolysis Mechanisms of Voltage-Gated Ion Channel Subunits and Cell Adhesion Molecules
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The Rhomboid-Like Superfamily: Molecular Mechanisms and Biological Roles
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The rhomboid protease family: a decade of progress on function and mechanism
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Rhomboids of Mycobacteria: Characterization Using an aarA Mutant of Providencia stuartii and Gene Deletion in Mycobacterium smegmatis
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A New Class of Rhomboid Protease Inhibitors Discovered by Activity-Based Fluorescence Polarization
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Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures
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p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition
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Characterization of PARL-Mediated Intramembrane Proteolysis
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