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Distinct Structural Features of the Lon Protease Drive Conserved Hand-over-Hand Substrate Translocation

https://doi.org/10.1101/617159
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1 of the 55 references listed on this page is in the Retraction Watch database as retracted (export 2026-11-04): 10.7554/elife.18129 (notice 2019-04-03).

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What this work says

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

inferredcites →https://doi.org/10.1002/jcc.20084openalex-snapshot
UCSF Chimera—A visualization system for exploratory research and analysis
inferredcites →https://doi.org/10.1002/pro.3235openalex-snapshot
UCSF ChimeraX: Meeting modern challenges in visualization and analysis
inferredcites →https://doi.org/10.1002/pro.3293openalex-snapshot
Guidelines for using Bsoft for high resolution reconstruction and validation of biomolecular structures from electron micrographs
inferredcites →https://doi.org/10.1002/pro.376openalex-snapshot
Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity
inferredcites →https://doi.org/10.1016/j.bbabio.2016.03.025openalex-snapshot
Emerging role of Lon protease as a master regulator of mitochondrial functions
inferredcites →https://doi.org/10.1016/j.bbapap.2008.02.010openalex-snapshot
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
inferredcites →https://doi.org/10.1016/j.jmb.2010.06.030openalex-snapshot
Crystal Structures of Bacillus subtilis Lon Protease
inferredcites →https://doi.org/10.1016/j.jmb.2012.02.039openalex-snapshot
Identification of a Region in the N-Terminus of Escherichia coli Lon That Affects ATPase, Substrate Translocation and Proteolytic Activity
inferredcites →https://doi.org/10.1016/j.jsb.2003.10.010openalex-snapshot
Evolutionary history and higher order classification of AAA+ ATPases
inferredcites →https://doi.org/10.1016/j.jsb.2003.11.007openalex-snapshot
FindEM—a fast, efficient program for automatic selection of particles from electron micrographs
inferredcites →https://doi.org/10.1016/j.jsb.2005.03.010openalex-snapshot
Automated molecular microscopy: The new Leginon system
inferredcites →https://doi.org/10.1016/j.jsb.2009.01.002openalex-snapshot
Appion: An integrated, database-driven pipeline to facilitate EM image processing
inferredcites →https://doi.org/10.1016/j.jsb.2009.01.004openalex-snapshot
DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
inferredcites →https://doi.org/10.1016/j.jsb.2012.09.006openalex-snapshot
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
inferredcites →https://doi.org/10.1016/j.jsb.2015.08.008openalex-snapshot
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
inferredcites →https://doi.org/10.1016/j.molcel.2017.05.016openalex-snapshot
HspQ Functions as a Unique Specificity-Enhancing Factor for the AAA+ Lon Protease
inferredcites →https://doi.org/10.1016/j.str.2016.03.001openalex-snapshot
Structural Insights into the Allosteric Operation of the Lon AAA+ Protease
inferredcites →https://doi.org/10.1016/j.str.2018.10.003openalex-snapshot
A Multi-model Approach to Assessing Local and Global Cryo-EM Map Quality
inferredcites →https://doi.org/10.1016/s1016-8478(23)25247-4openalex-snapshot
Oligomeric Structure of the ATP-dependent Protease La (Lon) of Escherichia coli
inferredcites →https://doi.org/10.1021/bi980945hopenalex-snapshot
Functional Role of the N-Terminal Region of the Lon Protease from Mycobacterium smegmatis
inferredcites →https://doi.org/10.1038/nature04943openalex-snapshot
Mechanism of DNA translocation in a replicative hexameric helicase
inferredcites →https://doi.org/10.1038/nmeth.3541openalex-snapshot
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nmeth.4169openalex-snapshot
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
inferredcites →https://doi.org/10.1038/nmeth.4193openalex-snapshot
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nmeth.4461openalex-snapshot
Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV
inferredcites →https://doi.org/10.1038/nrm1684openalex-snapshot
AAA+ proteins: have engine, will work
inferredcites →https://doi.org/10.1038/nrm3984openalex-snapshot
New roles for mitochondrial proteases in health, ageing and disease
inferredcites →https://doi.org/10.1038/s41586-018-0469-4openalex-snapshot
Malaria parasite translocon structure and mechanism of effector export
inferredcites →https://doi.org/10.1038/srep33631openalex-snapshot
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease
inferredcites →https://doi.org/10.1039/b609936jopenalex-snapshot
Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli : highlights from kinetic studies
inferredcites →https://doi.org/10.1073/pnas.0910392106openalex-snapshot
Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine
inferredcites →https://doi.org/10.1073/pnas.0910708106openalex-snapshot
The crystal structure of apo -FtsH reveals domain movements necessary for substrate unfolding and translocation
inferredcites →https://doi.org/10.1073/pnas.1307066110openalex-snapshot
Distinct quaternary structures of the AAA+ Lon protease control substrate degradation
inferredcites →https://doi.org/10.1073/pnas.1810648115openalex-snapshot
ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB
inferredcites →https://doi.org/10.1074/jbc.m312243200openalex-snapshot
The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site
inferredcites →https://doi.org/10.1093/nar/gky427openalex-snapshot
SWISS-MODEL: homology modelling of protein structures and complexes
inferredcites →https://doi.org/10.1101/cshperspect.a007559openalex-snapshot
Quality Control of Mitochondrial Proteostasis
inferredcites →https://doi.org/10.1101/gad.1670908openalex-snapshot
Recognition of misfolded proteins by Lon, a AAA + protease
inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot
PHENIX : a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot
Features and development of Coot
inferredcites →https://doi.org/10.1107/s0907444910019554openalex-snapshot
Structure of the N-terminal fragment ofEscherichia coliLon protease
inferredcites →https://doi.org/10.1110/ps.052069306openalex-snapshot
Slicing a protease: Structural features of the ATP‐dependent Lon proteases gleaned from investigations of isolated domains
inferredcites →https://doi.org/10.1126/science.aan1052openalex-snapshot
Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104
inferredcites →https://doi.org/10.1126/science.aao0464openalex-snapshot
Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing
inferredcites →https://doi.org/10.1126/science.aav0725openalex-snapshot
Substrate-engaged 26 S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation
inferredcites →https://doi.org/10.1146/annurev-biochem-060408-172623openalex-snapshot
AAA+ Proteases: ATP-Fueled Machines of Protein Destruction
inferredcites →https://doi.org/10.1146/annurev.biophys.35.040405.101933openalex-snapshot
EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS
inferredcites →https://doi.org/10.3389/fmolb.2017.00027openalex-snapshot
Structural Elements Regulating AAA+ Protein Quality Control Machines
inferredcites →https://doi.org/10.7554/elife.18129openalex-snapshot
RETRACTED: The structure of SV40 large T hexameric helicase in complex with AT-rich origin DNA
inferredcites →https://doi.org/10.7554/elife.18722openalex-snapshot
Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
inferredcites →https://doi.org/10.7554/elife.24487openalex-snapshot
Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase
inferredcites →https://doi.org/10.7554/elife.25754openalex-snapshot
Structure of a AAA+ unfoldase in the process of unfolding substrate
inferredcites →https://doi.org/10.7554/elife.31324openalex-snapshot
The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets
inferredcites →https://doi.org/10.7554/elife.38888openalex-snapshot
Structural principles of SNARE complex recognition by the AAA+ protein NSF
inferredcites →https://doi.org/10.7554/elife.42166openalex-snapshot
New tools for automated high-resolution cryo-EM structure determination in RELION-3

What points at this work

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

inferred← citeshttps://doi.org/10.1016/j.bpj.2021.05.027openalex-snapshot
Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines
inferred← citeshttps://doi.org/10.1016/j.crstbi.2019.10.001openalex-snapshot
Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery
inferred← citeshttps://doi.org/10.1038/s41580-019-0183-6openalex-snapshot
The molecular principles governing the activity and functional diversity of AAA+ proteins
inferred← citeshttps://doi.org/10.1038/s42003-020-0772-0openalex-snapshot
Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex
inferred← citeshttps://doi.org/10.1093/nar/gkac668openalex-snapshot
Molecular dynamics of DNA translocation by FtsK
inferred← citeshttps://doi.org/10.70675/af121c56zb1cdz4294zaa09z4897adf84b0bopenalex-snapshot
Cryo-EM characterisation of an enterobacterial stress response system
inferred← citeshttps://doi.org/10.7554/elife.52158openalex-snapshot
A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery
inferred← citeshttps://doi.org/10.7554/elife.52774openalex-snapshot
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
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