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Structure and activity of the axon guidance protein MICAL

https://doi.org/10.1073/pnas.0504838102
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What this work says

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

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Prediction of β-turns in proteins by 1-4 and 2-3 correlation model
inferredcites →https://doi.org/10.1002/pro.5560061119openalex-snapshot
Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding
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Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
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Prolonged Oxidative Stress on Actin
inferredcites →https://doi.org/10.1006/abio.2000.4757openalex-snapshot
Prediction of Tight Turns and Their Types in Proteins
inferredcites →https://doi.org/10.1016/0022-2836(79)90301-2openalex-snapshot
Crystal structure of p-hydroxybenzoate hydroxylase
inferredcites →https://doi.org/10.1016/0022-2836(90)90310-iopenalex-snapshot
Rubredoxin reductase of Pseudomonas oleovorans
inferredcites →https://doi.org/10.1016/0263-7855(96)00018-5openalex-snapshot
VMD: Visual molecular dynamics
inferredcites →https://doi.org/10.1016/j.bbrc.2004.12.182openalex-snapshot
The MICAL proteins and rab1: a possible link to the cytoskeleton?
inferredcites →https://doi.org/10.1016/j.str.2004.03.008openalex-snapshot
Rational Protein Crystallization by Mutational Surface Engineering
inferredcites →https://doi.org/10.1016/s0006-291x(03)00918-5openalex-snapshot
MICAL-1 isoforms, novel rab1 interacting proteins
inferredcites →https://doi.org/10.1016/s0006-3495(00)76713-0openalex-snapshot
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
inferredcites →https://doi.org/10.1016/s0006-3495(95)80142-6openalex-snapshot
H2O2-treated actin: assembly and polymer interactions with cross-linking proteins
inferredcites →https://doi.org/10.1016/s0006-3495(97)78684-3openalex-snapshot
An improved function for fitting sedimentation velocity data for low-molecular-weight solutes
inferredcites →https://doi.org/10.1016/s0006-3495(99)77376-5openalex-snapshot
Thiol Oxidation of Actin Produces Dimers That Enhance the Elasticity of the F-Actin Network
inferredcites →https://doi.org/10.1016/s0014-5793(01)03240-9openalex-snapshot
Functional plasticity of CH domains
inferredcites →https://doi.org/10.1016/s0076-6879(97)76066-xopenalex-snapshot
[20] Processing of X-ray diffraction data collected in oscillation mode
inferredcites →https://doi.org/10.1016/s0092-8674(00)81715-8openalex-snapshot
Plexin A Is a Neuronal Semaphorin Receptor that Controls Axon Guidance
inferredcites →https://doi.org/10.1016/s0092-8674(02)00794-8openalex-snapshot
MICALs, a Family of Conserved Flavoprotein Oxidoreductases, Function in Plexin-Mediated Axonal Repulsion
inferredcites →https://doi.org/10.1016/s0891-5849(02)00799-2openalex-snapshot
Methionine oxidation as a major cause of the functional impairment of oxidized actin
inferredcites →https://doi.org/10.1016/s0925-4773(99)00314-7openalex-snapshot
The LIM domain: regulation by association
inferredcites →https://doi.org/10.1016/s0969-2126(98)00062-8openalex-snapshot
The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
inferredcites →https://doi.org/10.1021/jm031087copenalex-snapshot
Crystal Structures of Monoamine Oxidase B in Complex with Four Inhibitors of the N -Propargylaminoindan Class
inferredcites →https://doi.org/10.1038/emm.1999.9openalex-snapshot
Redox signaling: hydrogen peroxide as intracellular messenger
inferredcites →https://doi.org/10.1038/nsb732openalex-snapshot
Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
inferredcites →https://doi.org/10.1073/pnas.022640199openalex-snapshot
Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase
inferredcites →https://doi.org/10.1074/jbc.m111842200openalex-snapshot
MICAL, a Novel CasL Interacting Molecule, Associates with Vimentin
inferredcites →https://doi.org/10.1093/bioinformatics/15.4.305openalex-snapshot
ESPript: analysis of multiple sequence alignments in PostScript.
inferredcites →https://doi.org/10.1107/s0021889803006721openalex-snapshot
POVScript+: a program for model and data visualization using persistence of vision ray-tracing
inferredcites →https://doi.org/10.1107/s0021889891004399openalex-snapshot
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
inferredcites →https://doi.org/10.1107/s0108767386099622openalex-snapshot
Improved Fourier coefficients for maps using phases from partial structures with errors
inferredcites →https://doi.org/10.1107/s0108767390010224openalex-snapshot
Improved methods for building protein models in electron density maps and the location of errors in these models
inferredcites →https://doi.org/10.1107/s0907444900014736openalex-snapshot
Use of TLS parameters to model anisotropic displacements in macromolecular refinement
inferredcites →https://doi.org/10.1107/s0907444994003112openalex-snapshot
The CCP4 suite: programs for protein crystallography
inferredcites →https://doi.org/10.1107/s0907444995014983openalex-snapshot
xdlMAPMANandxdlDATAMAN– Programs for Reformatting, Analysis and Manipulation of Biomacromolecular Electron-Density Maps and Reflection Data Sets
inferredcites →https://doi.org/10.1107/s0907444997005696openalex-snapshot
wARP: Improvement and Extension of Crystallographic Phases by Weighted Averaging of Multiple-Refined Dummy Atomic Models
inferredcites →https://doi.org/10.1107/s0909049503023938openalex-snapshot
SOLVE and RESOLVE: automated structure solution, density modification and model building
inferredcites →https://doi.org/10.1110/ps.12801openalex-snapshot
Sequence‐structure analysis of FAD‐containing proteins
inferredcites →https://doi.org/10.1110/ps.8.5.1045openalex-snapshot
Prediction of the location and type of β‐turns in proteins using neural networks
inferredcites →https://doi.org/10.1110/ps.9.9.1774openalex-snapshot
The oxidation produced by hydrogen peroxide on Ca‐ATP‐G‐actin
inferredcites →https://doi.org/10.1126/science.7939628openalex-snapshot
The Mobile Flavin of 4-OH Benzoate Hydroxylase
inferredcites →https://doi.org/10.1126/stke.2000.15.pe1openalex-snapshot
EGF Receptor Transactivation Mediated by the Proteolytic Production of EGF-like Agonists
inferredcites →https://doi.org/10.1126/stke.2000.50.pe1openalex-snapshot
Conformational Display: A Role for Switch Polymorphism in the Superfamily of Regulatory GTPases
inferredcites →https://doi.org/10.1126/stke.2000.53.pe1openalex-snapshot
Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation
inferredcites →https://doi.org/10.1126/stke.2002.155.pe44openalex-snapshot
Semaphorins: Green Light for Redox Signaling?

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4156146openalex-extracted
CHK1 Controls Zygote Pronuclear Envelope Breakdown by Regulating F-actin Through Interacting with MICAL3
inferred← citeshttps://doi.org/10.2139/ssrn.4156153openalex-extracted
CHK1 Controls Zygote Pronuclear Envelope Breakdown by Regulating F-Actin Through Interacting With MICAL3
inferred← citeshttps://doi.org/10.1002/ana.25167openalex-snapshot
Mutations in MICAL‐1cause autosomal‐dominant lateral temporal epilepsy
inferred← citeshttps://doi.org/10.1002/bies.202100152openalex-snapshot
Rho GTPases: Non‐canonical regulation by cysteine oxidation
inferred← citeshttps://doi.org/10.1002/cm.20527openalex-snapshot
Extracellular inhibitors, repellents, and semaphorin/plexin/MICAL‐mediated actin filament disassembly
inferred← citeshttps://doi.org/10.1002/cm.21315openalex-snapshot
Actin filaments—A target for redox regulation
inferred← citeshttps://doi.org/10.1002/cne.21799openalex-snapshot
ERM proteins regulate growth cone responses to Sema3A
inferred← citeshttps://doi.org/10.1002/pro.3512openalex-snapshot
Human MICAL1: Activation by the small GTPase Rab8 and small‐angle X‐ray scattering studies on the oligomerization state of MICAL1 and its complex with Rab8
inferred← citeshttps://doi.org/10.1007/164_2020_380openalex-snapshot
Oxidants in Physiological Processes
inferred← citeshttps://doi.org/10.1007/978-0-387-70956-7_4openalex-snapshot
MICAL Flavoprotein Monooxygenases: Structure, Function and Role in Semaphorin Signaling
inferred← citeshttps://doi.org/10.1007/978-4-431-54385-5_5openalex-snapshot
Structure of Semaphorins and Their Receptors
inferred← citeshttps://doi.org/10.1007/s00018-011-0787-2openalex-snapshot
MICALs in control of the cytoskeleton, exocytosis, and cell death
inferred← citeshttps://doi.org/10.1007/s00018-012-1019-0openalex-snapshot
Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions
inferred← citeshttps://doi.org/10.1007/s00404-007-0507-1openalex-snapshot
Reactive oxygen species, total antioxidant concentration of seminal plasma and their effect on sperm parameters and outcome of IVF/ICSI patients
inferred← citeshttps://doi.org/10.1007/s10555-010-9225-4openalex-snapshot
Metastasis: cancer cell’s escape from oxidative stress
inferred← citeshttps://doi.org/10.1007/s10858-006-9062-5openalex-snapshot
Solution structure of calponin homology domain of Human MICAL-1
inferred← citeshttps://doi.org/10.1007/s12013-025-01978-xopenalex-snapshot
Prevalence and Functional Roles of Intrinsic Disorder in the [F-actin]-monooxygenase MICAL Family Members and their Interactors
inferred← citeshttps://doi.org/10.1016/b978-008045382-8.00135-0openalex-snapshot
Flavin-Dependent Enzymes
inferred← citeshttps://doi.org/10.1016/j.abb.2009.11.028openalex-snapshot
Control of catalysis in flavin-dependent monooxygenases
inferred← citeshttps://doi.org/10.1016/j.abb.2011.08.004openalex-snapshot
Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1
inferred← citeshttps://doi.org/10.1016/j.abb.2013.12.005openalex-snapshot
Flavin dependent monooxygenases
inferred← citeshttps://doi.org/10.1016/j.abb.2016.01.016openalex-snapshot
Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains
inferred← citeshttps://doi.org/10.1016/j.abb.2017.06.004openalex-snapshot
Structure-function studies of MICAL, the unusual multidomain flavoenzyme involved in actin cytoskeleton dynamics
inferred← citeshttps://doi.org/10.1016/j.abb.2026.111023openalex-snapshot
NADPH gating and F-actin engagement define the structural bases of MICAL1 autoinhibition and activation
inferred← citeshttps://doi.org/10.1016/j.bbagen.2014.10.030openalex-snapshot
Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation
inferred← citeshttps://doi.org/10.1016/j.bbrc.2009.05.026openalex-snapshot
Identification of proteins interacting with GTP cyclohydrolase I
inferred← citeshttps://doi.org/10.1016/j.canlet.2020.04.019openalex-snapshot
MICAL2 is a novel nucleocytoplasmic shuttling protein promoting cancer invasion and growth of lung adenocarcinoma
inferred← citeshttps://doi.org/10.1016/j.ejcb.2022.151249openalex-snapshot
Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2017.02.010openalex-snapshot
Regulated methionine oxidation by monooxygenases
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2018.10.407openalex-snapshot
Peroxiredoxin interaction with the cytoskeletal-regulatory protein CRMP2: Investigation of a putative redox relay
inferred← citeshttps://doi.org/10.1016/j.lfs.2021.119045openalex-snapshot
MICAL2 regulates myofibroblasts differentiation in epidural fibrosis via SRF/MRTF-A signaling pathway
inferred← citeshttps://doi.org/10.1016/j.mod.2007.01.006openalex-snapshot
Drosophila MICAL regulates myofilament organization and synaptic structure
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2007.05.009openalex-snapshot
Excretory–secretory proteome of larval Schistosoma mansoni and Echinostoma caproni, two parasites of Biomphalaria glabrata
inferred← citeshttps://doi.org/10.1016/j.neuron.2008.03.017openalex-snapshot
Cyclic GMP-Gated CNG Channels Function in Sema3A-Induced Growth Cone Repulsion
inferred← citeshttps://doi.org/10.1016/j.pep.2016.05.008openalex-snapshot
A simple and efficient method for generating high-quality recombinant Mical enzyme for in vitro assays
inferred← citeshttps://doi.org/10.1016/j.pnpbp.2017.11.020openalex-snapshot
Glucocorticoids, genes and brain function
inferred← citeshttps://doi.org/10.1016/j.sbi.2006.10.003openalex-snapshot
New frontiers in structural flavoenzymology
inferred← citeshttps://doi.org/10.1016/j.semcdb.2012.10.005openalex-snapshot
Semaphorins in cancer: Biological mechanisms and therapeutic approaches
inferred← citeshttps://doi.org/10.1016/j.semcdb.2012.11.003openalex-snapshot
Structural insights into semaphorins and their receptors
inferred← citeshttps://doi.org/10.1021/acs.jproteome.2c00127openalex-snapshot
Accurate Proteomewide Measurement of Methionine Oxidation in Aging Mouse Brains
inferred← citeshttps://doi.org/10.1021/bi4008462openalex-snapshot
Actin Stimulates Reduction of the MICAL-2 Monooxygenase Domain
inferred← citeshttps://doi.org/10.1038/nature08724openalex-snapshot
Mical links semaphorins to F-actin disassembly
inferred← citeshttps://doi.org/10.1038/ncomms14528openalex-snapshot
Oxidation of F-actin controls the terminal steps of cytokinesis
inferred← citeshttps://doi.org/10.1038/s41467-024-50940-7openalex-snapshot
Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly
inferred← citeshttps://doi.org/10.1038/s41467-024-54131-2openalex-snapshot
Structural basis of MICAL autoinhibition
inferred← citeshttps://doi.org/10.1038/s41598-017-17943-5openalex-snapshot
The MICALs are a Family of F-actin Dismantling Oxidoreductases Conserved from Drosophila to Humans
inferred← citeshttps://doi.org/10.1038/s44319-024-00267-7openalex-snapshot
CHK1 controls zygote pronuclear envelope breakdown by regulating F-actin through interacting with MICAL3
inferred← citeshttps://doi.org/10.1038/srep22176openalex-snapshot
Modulation of MICAL Monooxygenase Activity by its Calponin Homology Domain: Structural and Mechanistic Insights
inferred← citeshttps://doi.org/10.1042/bst20190866openalex-snapshot
Signal-regulated oxidation of proteins via MICAL
inferred← citeshttps://doi.org/10.1073/pnas.1806851116openalex-snapshot
Semaphorin signaling via MICAL3 induces symmetric cell division to expand breast cancer stem-like cells
inferred← citeshttps://doi.org/10.1073/pnas.2403880121openalex-snapshot
Formylation facilitates the reduction of oxidized initiator methionines
inferred← citeshttps://doi.org/10.1074/jbc.m113.521443openalex-snapshot
Identification of a Dithiol-disulfide Switch in Collapsin Response Mediator Protein 2 (CRMP2) That Is Toggled in a Model of Neuronal Differentiation
inferred← citeshttps://doi.org/10.1080/15384101.2025.2485843openalex-snapshot
Leaving the mark: FMOs as an emerging class of cytokinetic regulators
inferred← citeshttps://doi.org/10.1089/ars.2013.5487openalex-snapshot
MICAL-Family Proteins: Complex Regulators of the Actin Cytoskeleton
inferred← citeshttps://doi.org/10.1096/fasebj.22.1_supplement.749.2openalex-snapshot
Identification of proteins interacting with GTP cyclohydrolase I
inferred← citeshttps://doi.org/10.1098/rsta.2013.0155openalex-snapshot
Understanding cell signalling systems: paving the way for new therapies
inferred← citeshttps://doi.org/10.1098/rstb.2006.1892openalex-snapshot
Semaphorins in axon regeneration: developmental guidance molecules gone wrong?
inferred← citeshttps://doi.org/10.1101/131755openalex-snapshot
Flavin Monooxygenases Regulate C. elegans Axon Guidance and Growth Cone Protrusion with UNC-6/Netrin signaling and Rac GTPases
inferred← citeshttps://doi.org/10.1101/2025.01.30.635440openalex-snapshot
The KRAB-Zinc Finger protein ZKSCAN3 represses enhancers via embedded retrotransposons
inferred← citeshttps://doi.org/10.1107/s2052252519015409openalex-snapshot
Structural and kinetic insights into flavin-containing monooxygenase and calponin-homology domains in human MICAL3
inferred← citeshttps://doi.org/10.1110/ps.072914007openalex-snapshot
Toward rational protein crystallization: A Web server for the design of crystallizable protein variants
inferred← citeshttps://doi.org/10.1126/scisignal.2001127openalex-snapshot
Thioredoxin Mediates Oxidation-Dependent Phosphorylation of CRMP2 and Growth Cone Collapse
inferred← citeshttps://doi.org/10.1128/mcb.01389-10openalex-snapshot
MICAL-1 Is a Negative Regulator of MST-NDR Kinase Signaling and Apoptosis
inferred← citeshttps://doi.org/10.1172/jci133181openalex-snapshot
MICAL1 constrains cardiac stress responses and protects against disease by oxidizing CaMKII
inferred← citeshttps://doi.org/10.1177/1073858409340702openalex-snapshot
From Guidance Signals to Movement: Signaling Molecules Governing Growth Cone Turning
inferred← citeshttps://doi.org/10.1242/jcs.089367openalex-snapshot
Differential regulation of actin microfilaments by human MICAL proteins
inferred← citeshttps://doi.org/10.1242/jcs.202028openalex-snapshot
Emerging roles of MICAL family proteins – from actin oxidation to membrane trafficking during cytokinesis
inferred← citeshttps://doi.org/10.1371/journal.pgen.1006998openalex-snapshot
Flavin monooxygenases regulate Caenorhabditis elegans axon guidance and growth cone protrusion with UNC-6/Netrin signaling and Rac GTPases
inferred← citeshttps://doi.org/10.1517/17460441.2.10.1329openalex-snapshot
Protein crystallization in drug design: towards a rational approach
inferred← citeshttps://doi.org/10.1523/jneurosci.5646-07.2008openalex-snapshot
Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein
inferred← citeshttps://doi.org/10.18632/oncotarget.6577openalex-snapshot
MICAL2is a novel human cancer gene controlling mesenchymal to epithelial transition involved in cancer growth and invasion
inferred← citeshttps://doi.org/10.21203/rs.3.rs-712397/v1openalex-snapshot
NADPH-dependent oxidation of CRMP2 through a MICAL1-Prx1 redox relay controls neurite outgrowth
inferred← citeshttps://doi.org/10.2147/ott.s37744openalex-snapshot
The emerging role of class-3 semaphorins and their neuropilin receptors in oncology
inferred← citeshttps://doi.org/10.32920/21985076openalex-snapshot
MICAL1 Monooxygenase in Autosomal Dominant Lateral Temporal Epilepsy: Role in Cytoskeletal Regulation and Relation to Cancer
inferred← citeshttps://doi.org/10.32920/21985076.v1openalex-snapshot
MICAL1 Monooxygenase in Autosomal Dominant Lateral Temporal Epilepsy: Role in Cytoskeletal Regulation and Relation to Cancer
inferred← citeshttps://doi.org/10.3389/fcell.2023.1124202openalex-snapshot
MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics
inferred← citeshttps://doi.org/10.3390/genes13050715openalex-snapshot
MICAL1 Monooxygenase in Autosomal Dominant Lateral Temporal Epilepsy: Role in Cytoskeletal Regulation and Relation to Cancer
inferred← citeshttps://doi.org/10.3390/ijms14046920openalex-snapshot
MICAL, the Flavoenzyme Participating in Cytoskeleton Dynamics
inferred← citeshttps://doi.org/10.3390/molecules26247519openalex-snapshot
Enriching the Arsenal of Pharmacological Tools against MICAL2
inferred← citeshttps://doi.org/10.3410/f.727333330.793538614openalex-snapshot
Faculty Opinions recommendation of Oxidation of F-actin controls the terminal steps of cytokinesis.
inferred← citeshttps://doi.org/10.4331/wjbc.v1.i8.254openalex-snapshot
Important relationships between Rab and MICAL proteins in endocytic trafficking
inferred← citeshttps://doi.org/10.70675/04897de0zb90bz4ba0za353zc413571e1916openalex-snapshot
Actin reduction by MsrB2 is a key component of the cytokinetic abscission checkpoint and prevents tetraploidy
inferred← citeshttps://doi.org/10.7150/thno.28228openalex-snapshot
MICAL2 Mediates p53 Ubiquitin Degradation through Oxidating p53 Methionine 40 and 160 and Promotes Colorectal Cancer Malignance
inferred← citeshttps://doi.org/10.7301/z0f18wzsopenalex-snapshot
Molecular Basis for Phosphate Signaling by Prokaryotic and Eukaryotic Phosphatases
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