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Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants

https://doi.org/10.1371/journal.pone.0161526
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What this work says

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

inferredcites →https://doi.org/10.1007/bf01589116openalex-snapshot
On the limited memory BFGS method for large scale optimization
inferredcites →https://doi.org/10.1007/s00018-012-1076-4openalex-snapshot
Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response
inferredcites →https://doi.org/10.1007/s10863-009-9255-1openalex-snapshot
Mitochondrial quality control: insights on how Parkinson’s disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis
inferredcites →https://doi.org/10.1007/s12035-010-8150-4openalex-snapshot
Mitochondrial Quality Control and Parkinson’s Disease: A Pathway Unfolds
inferredcites →https://doi.org/10.1007/s12192-012-0355-1openalex-snapshot
Temperature-induced changes of HtrA2(Omi) protease activity and structure
inferredcites →https://doi.org/10.1016/0010-4655(95)00041-dopenalex-snapshot
AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
inferredcites →https://doi.org/10.1016/0021-9991(77)90098-5openalex-snapshot
Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
inferredcites →https://doi.org/10.1016/j.abb.2011.10.007openalex-snapshot
The structural basis of mode of activation and functional diversity: A case study with HtrA family of serine proteases
inferredcites →https://doi.org/10.1016/j.bbapap.2015.12.002openalex-snapshot
Intra- and intersubunit changes accompanying thermal activation of the HtrA2(Omi) protease homotrimer
inferredcites →https://doi.org/10.1016/j.cell.2007.08.044openalex-snapshot
Allosteric Activation of DegS, a Stress Sensor PDZ Protease
inferredcites →https://doi.org/10.1016/j.cell.2011.02.024openalex-snapshot
Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages
inferredcites →https://doi.org/10.1016/j.molcel.2009.12.023openalex-snapshot
The Wilms' Tumor Suppressor Protein WT1 Is Processed by the Serine Protease HtrA2/Omi
inferredcites →https://doi.org/10.1016/j.neuint.2010.08.004openalex-snapshot
Association of Omi/HtrA2 with γ-secretase in mitochondria
inferredcites →https://doi.org/10.1016/j.neulet.2003.11.068openalex-snapshot
Alzheimer's disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi
inferredcites →https://doi.org/10.1016/j.str.2015.01.012openalex-snapshot
A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases
inferredcites →https://doi.org/10.1016/s0092-8674(04)00454-4openalex-snapshot
Crystal Structure of the DegS Stress Sensor
inferredcites →https://doi.org/10.1021/bi100907mopenalex-snapshot
Distance Mapping in Proteins Using Fluorescence Spectroscopy: The Tryptophan-Induced Quenching (TrIQ) Method
inferredcites →https://doi.org/10.1021/bi701929mopenalex-snapshot
Structure and Function of the Virulence-Associated High-Temperature Requirement A of Mycobacterium tuberculosis
inferredcites →https://doi.org/10.1021/ct200909jopenalex-snapshot
Routine Microsecond Molecular Dynamics Simulations with AMBER on GPUs. 1. Generalized Born
inferredcites →https://doi.org/10.1021/ct300284copenalex-snapshot
Routine Access to Millisecond Time Scale Events with Accelerated Molecular Dynamics
inferredcites →https://doi.org/10.1038/355472a0openalex-snapshot
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
inferredcites →https://doi.org/10.1038/416455aopenalex-snapshot
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
inferredcites →https://doi.org/10.1038/cdd.2008.166openalex-snapshot
Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
inferredcites →https://doi.org/10.1038/nature07004openalex-snapshot
Structural basis for the regulated protease and chaperone function of DegP
inferredcites →https://doi.org/10.1038/nrm3065openalex-snapshot
HTRA proteases: regulated proteolysis in protein quality control
inferredcites →https://doi.org/10.1038/nsb795openalex-snapshot
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
inferredcites →https://doi.org/10.1038/nsmb.1840openalex-snapshot
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
inferredcites →https://doi.org/10.1038/nsmb.2013openalex-snapshot
Substrate-induced remodeling of the active site regulates human HTRA1 activity
inferredcites →https://doi.org/10.1038/nsmb.2055openalex-snapshot
Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure
inferredcites →https://doi.org/10.1038/sj.cdd.4402291openalex-snapshot
The mitochondrial serine protease HtrA2/Omi: an overview
inferredcites →https://doi.org/10.1046/j.1432-1327.2000.01589.xopenalex-snapshot
Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response
inferredcites →https://doi.org/10.1063/1.445869openalex-snapshot
Comparison of simple potential functions for simulating liquid water
inferredcites →https://doi.org/10.1063/1.470117openalex-snapshot
A smooth particle mesh Ewald method
inferredcites →https://doi.org/10.1073/pnas.0801146105openalex-snapshot
Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease
inferredcites →https://doi.org/10.1073/pnas.0805464105openalex-snapshot
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
inferredcites →https://doi.org/10.1073/pnas.1101084108openalex-snapshot
The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies
inferredcites →https://doi.org/10.1074/jbc.272.48.29987openalex-snapshot
Evolutionary Divergence of Substrate Specificity within the Chymotrypsin-like Serine Protease Fold
inferredcites →https://doi.org/10.1074/jbc.m110.135541openalex-snapshot
Allostery Is an Intrinsic Property of the Protease Domain of DegS
inferredcites →https://doi.org/10.1074/jbc.m111.243832openalex-snapshot
Molecular Adaptation of the DegQ Protease to Exert Protein Quality Control in the Bacterial Cell Envelope
inferredcites →https://doi.org/10.1074/jbc.m208148200openalex-snapshot
Crystal Structure of the Protease Domain of a Heat-shock Protein HtrA from Thermotoga maritima
inferredcites →https://doi.org/10.1074/jbc.m308659200openalex-snapshot
Binding Specificity and Regulation of the Serine Protease and PDZ Domains of HtrA2/Omi
inferredcites →https://doi.org/10.1074/jbc.m404940200openalex-snapshot
The C-terminal Tail of Presenilin Regulates Omi/HtrA2 Protease Activity
inferredcites →https://doi.org/10.1074/jbc.m603443200openalex-snapshot
β-Amyloid Precursor Protein Is a Direct Cleavage Target of HtrA2 Serine Protease
inferredcites →https://doi.org/10.1096/fj.13-227256openalex-snapshot
Intricate structural coordination and domain plasticity regulate activity of serine protease HtrA2
inferredcites →https://doi.org/10.1107/s0021889807021206openalex-snapshot
Phaser crystallographic software
inferredcites →https://doi.org/10.1107/s0907444904019158openalex-snapshot
Coot : model-building tools for molecular graphics
inferredcites →https://doi.org/10.1107/s0907444905036693openalex-snapshot
Scaling and assessment of data quality
inferredcites →https://doi.org/10.1107/s0907444910048675openalex-snapshot
iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM
inferredcites →https://doi.org/10.1107/s0907444913000061openalex-snapshot
How good are my data and what is the resolution?
inferredcites →https://doi.org/10.1107/s0907444994003112openalex-snapshot
The CCP4 suite: programs for protein crystallography
inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
inferredcites →https://doi.org/10.1110/ps.072833207openalex-snapshot
Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain
inferredcites →https://doi.org/10.1111/febs.12799openalex-snapshot
Dual regulatory switch confers tighter control on HtrA2 proteolytic activity
inferredcites →https://doi.org/10.1128/jb.172.4.1791-1797.1990openalex-snapshot
The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
inferredcites →https://doi.org/10.1145/1365490.1365500openalex-snapshot
Scalable Parallel Programming with CUDA
inferredcites →https://doi.org/10.1145/1401132.1401152openalex-snapshot
Scalable parallel programming with CUDA
inferredcites →https://doi.org/10.1186/1478-811x-8-8openalex-snapshot
PDZ domains and their binding partners: structure, specificity, and modification
inferredcites →https://doi.org/10.1371/journal.pone.0055416openalex-snapshot
Allosteric Regulation of Serine Protease HtrA2 through Novel Non-Canonical Substrate Binding Pocket
inferredcites →https://doi.org/10.1371/journal.pone.0131142openalex-snapshot
Structural and Functional Analysis of Human HtrA3 Protease and Its Subdomains
inferredcites →https://doi.org/10.1517/14728222.2010.487867openalex-snapshot
HtrA proteins as targets in therapy of cancer and other diseases
inferredcites →https://doi.org/10.2174/138945009787846399openalex-snapshot
Mitochondrial Serine Protease HtrA2/Omi as a Potential Therapeutic Target
inferredcites →https://doi.org/10.2174/156800909788486704openalex-snapshot
HtrA Serine Proteases as Potential Therapeutic Targets in Cancer
inferredcites →https://doi.org/10.3233/jad-2009-1037openalex-snapshot
A New Function of Human HtrA2 as an Amyloid-β Oligomerization Inhibitor

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.3979180openalex-extracted
Inter-Subunit Crosstalk via PDZ Synergistically Governs Allosteric Activation of Proapoptotic HtrA2
inferred← citeshttps://doi.org/10.1002/med.21929openalex-snapshot
Mitochondrial quality control proteases and their modulation for cancer therapy
inferred← citeshttps://doi.org/10.1016/j.abb.2017.04.004openalex-snapshot
Structural insights into the activation mechanisms of human HtrA serine proteases
inferred← citeshttps://doi.org/10.1016/j.bbrc.2022.01.042openalex-snapshot
Role of conserved regulatory loop residues in allosteric propagation of serine protease HtrA2
inferred← citeshttps://doi.org/10.1016/j.str.2022.06.001openalex-snapshot
Inter-subunit crosstalk via PDZ synergistically governs allosteric activation of proapoptotic HtrA2
inferred← citeshttps://doi.org/10.1038/cddis.2017.487openalex-snapshot
Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2
inferred← citeshttps://doi.org/10.1073/pnas.2025022118openalex-snapshot
Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR
inferred← citeshttps://doi.org/10.1107/s205979831800952xopenalex-snapshot
The crystal structure of an essential high-temperature requirement protein HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique features
inferred← citeshttps://doi.org/10.1371/journal.ppat.1010932openalex-snapshot
Dual role of an essential HtrA2/Omi protease in the human malaria parasite: Maintenance of mitochondrial homeostasis and induction of apoptosis-like cell death under cellular stress
inferred← citeshttps://doi.org/10.1515/revneuro-2018-0004openalex-snapshot
Progress in research on the role of Omi/HtrA2 in neurological diseases
inferred← citeshttps://doi.org/10.3390/books978-3-0365-0442-1openalex-snapshot
Asymmetry in Biological Homochirality
inferred← citeshttps://doi.org/10.3390/ijms241310904openalex-snapshot
Identification and Characterization of an HtrA Sheddase Produced by Coxiella burnetii
inferred← citeshttps://doi.org/10.3390/sym12040585openalex-snapshot
Chiral Interface of Amyloid Beta (Aβ): Relevance to Protein Aging, Aggregation and Neurodegeneration
inferred← citeshttps://doi.org/10.70675/924f03a2zc226z4ba7zbbaazcf7059e331a3openalex-snapshot
E-cadherin involvement in host-pathogen interaction and cell signaling
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