Evidence map›Paper›PMID 37906694›Full record

ArticleProtein science : a publication of the Protein Society2023

Site-specific photo-crosslinking/cleavage for protein-protein interface identification reveals oligomeric assembly of lysosomal-associated membrane protein type 2A in mammalian cells.

Kazue Terasawa, Tatsuro Seike, Kensaku Sakamoto, Kazumasa Ohtake, Tohru Terada, Takanori Iwata, Tetsuro Watabe, Shigeyuki Yokoyama, Miki Hara-Yokoyama

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. 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

9 authors at 4 institutions in 3 countries.

Kazue TerasawaDepartment of Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Tatsuro SeikeDepartment of Periodontology, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Kensaku SakamotoLaboratory for Nonnatural Amino Acid Technology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Kazumasa OhtakeLaboratory for Nonnatural Amino Acid Technology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Tohru TeradaDepartment of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Takanori IwataDepartment of Periodontology, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Tetsuro WatabeDepartment of Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Shigeyuki YokoyamaDepartment of Drug Target Protein Research, Shinshu University School of Medicine, Nagano, Japan.
Miki Hara-YokoyamaDepartment of Biochemistry, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.ORCID 0000-0002-5621-3625
Tokyo Medical and Dental University · JPShinshu University · JPThe University of Tokyo · JPWaseda University · JP

Funding

Establishment of University Fellowships towards the Creation of Science Technology Innovation JPMJFS2109Grants-in-Aid for Scientific Research JP17K12005Grants-in-Aid for Scientific Research JP21K10063Grants-in-Aids for ScientificJapan Agency for Medical Research and DevelopmentMEXT programResearch Support Project for Life Science and Drug Discovery (Basis for Supporting Innovative Drug Discovery and Life Science Research [(BINDS]) JP23ama121027
6 · The paper itself

Abstract

Genetic code expansion enables site-specific photo-crosslinking by introducing photo-reactive non-canonical amino acids into proteins at defined positions during translation. This technology is widely used for analyzing protein-protein interactions and is applicable in mammalian cells. However, the identification of the crosslinked region still remains challenging. Here, we developed a new method to identify the crosslinked region by pre-installing a site-specific cleavage site, an α-hydroxy acid (N

Indexed as

Hydroxy AcidsMammalsAnimalsLysosomal Membrane ProteinsHydroxy AcidsLysosomal Membrane Proteinschaperone-mediated autophagygenetic code expansionLAMP2Aprotein-protein interfacesite-specific cleavagesite-specific crosslinking

Identifiers

PMID37906694
PMCPMC10659947
OpenAlexW4388040303

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.