Evidence map›Paper›PMID 32490208›Full record

ArticleScience advances2020

Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.

Mia Shin, Cristina Puchades, Ananya Asmita, Neha Puri, Eric Adjei, R Luke Wiseman, A Wali Karzai, Gabriel C Lander

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 86 citations in OpenAlex.

  1. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Mia ShinDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-1607-5301
Cristina PuchadesDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-3240-4176
Ananya AsmitaDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.ORCID 0000-0003-0006-279X
Neha PuriDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Eric AdjeiDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.ORCID 0000-0001-5113-7769
R Luke WisemanDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-9287-6840
A Wali KarzaiDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-4921-1135
Scripps Research Institute · USStony Brook University · US

Funding

IMPACTING MITOCHONDRIAL FUNCTION THROUGH ALTERED PROTEASE ACTIVITYR01NS095892 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2016 to 2025
$5.3M
Molecular basis of axonal transport described by high-resolution 3D imagingDP2EB020402 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2014 to 2014
$2.8M
The Role the AAA+ Lon Proteases in Bacterial PathogenesisR01AI127533 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI KARZAI, A. WALI · 2017 to 2021
$2.4M
Defining the molecular mechanisms underlying mitochondrial proteostasisR21AG061697 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2019 to 2020
$619k
COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPYS10OD021634 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2016 to 2016
$531k
NIAID NIH HHS R01 AI127533NIA NIH HHS R21 AG061697NIBIB NIH HHS DP2 EB020402NIH HHS S10 OD021634NINDS NIH HHS R01 NS095892
6 · The paper itself

Abstract

Substrate-bound structures of AAA+ protein translocases reveal a conserved asymmetric spiral staircase architecture wherein a sequential ATP hydrolysis cycle drives hand-over-hand substrate translocation. However, this configuration is unlikely to represent the full conformational landscape of these enzymes, as biochemical studies suggest distinct conformational states depending on the presence or absence of substrate. Here, we used cryo-electron microscopy to determine structures of the

Indexed as

EndopeptidasesPeptide HydrolasesAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesCatalytic DomainCryoelectron MicroscopyProteolysisAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesEndopeptidasesPeptide Hydrolases

Identifiers

PMID32490208
PMCPMC7239648
OpenAlexW3027233291

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.