Evidence map›Paper›PMID 37163105›Full record

ArticlebioRxiv : the preprint server for biology2023

The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality control.

Upneet Kaur, Kyle C Kihn, Haiping Ke, Weiwei Kuo, Lila M Gierasch, Daniel N Hebert, Patrick L Wintrode, Daniel Deredge, Anne Gershenson

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 2 institutions in 1 country.

Upneet KaurDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
Kyle C KihnDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD 21201.
Haiping KeDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
Weiwei KuoDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
Lila M GieraschDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
Daniel N HebertDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
Patrick L WintrodeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD 21201.
Daniel DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD 21201.
Anne GershensonDepartment of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003.
University of Massachusetts Amherst · USUniversity of Maryland, Baltimore · US

Funding

Protein folding in the cell: Challenges and coping mechanisms Administrative Supplement for Equipment PurchaseR35GM118161 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2016 to 2025
$5.5M
Cellular protein maturation and degradationR01GM086874 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RAUCH, JENNIFER NICOLE · 2009 to 2025
$4.5M
Development of a novel pulse-chase in-cell footprinting method for protein folding analysisR01GM128985 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI JONES, LISA M · 2018 to 2021
$1.2M
NIGMS NIH HHS R01 GM086874NIGMS NIH HHS R01 GM128985NIGMS NIH HHS R35 GM118161
6 · The paper itself

Abstract

Many multi-domain proteins including the serpin family of serine protease inhibitors contain non-sequential domains composed of regions that are far apart in sequence. Because proteins are translated vectorially from N- to C-terminus, such domains pose a particular challenge: how to balance the conformational lability necessary to form productive interactions between early and late translated regions while avoiding aggregation. This balance is mediated by the protein sequence properties and the interactions of the folding protein with the cellular quality control machinery. For serpins, particularly

Indexed as

alpha1-antitrypsin (α1-antitrypsin)endoplasmic-reticulum-associated protein degradation (ERAD)ER quality controlprotein aggregationprotein foldingprotein misfoldingproteostasisserpin

Identifiers

PMID37163105
PMCPMC10168285
OpenAlexW4367322066

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.