Evidence map›Paper›PMID 34471136›Full record

ArticleNature communications2021

Dynamic tracking and identification of tissue-specific secretory proteins in the circulation of live mice.

Kwang-Eun Kim, Isaac Park, Jeesoo Kim, Myeong-Gyun Kang, Won Gun Choi, Hyemi Shin, Jong-Seo Kim, Hyun-Woo Rhee, Jae Myoung Suh

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 98 citations in OpenAlex.

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  16. TiOBioprocess and biosystems engineering · 2026
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  17. Review
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  19. SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  20. Article

17 more citing papers are in PubMed but not listed here.

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 2 countries.

Kwang-Eun Kim *Graduate School of Medical Science and Engineering, KAIST, Daejeon, Republic of Korea.ORCID 0000-0002-5355-1979
Isaac Park *Department of Chemistry, Seoul National University, Seoul, Republic of Korea.
Jeesoo KimCenter for RNA Research, Institute for Basic Science, Seoul, Republic of Korea.
Myeong-Gyun KangDepartment of Chemistry, Seoul National University, Seoul, Republic of Korea.
Won Gun ChoiGraduate School of Medical Science and Engineering, KAIST, Daejeon, Republic of Korea.
Hyemi ShinGraduate School of Medical Science and Engineering, KAIST, Daejeon, Republic of Korea.ORCID 0000-0002-7445-7834
Jong-Seo KimCenter for RNA Research, Institute for Basic Science, Seoul, Republic of Korea. jongseokim@snu.ac.kr.ORCID 0000-0002-8909-8440
Hyun-Woo RheeDepartment of Chemistry, Seoul National University, Seoul, Republic of Korea. rheehw@snu.ac.kr.ORCID 0000-0002-3817-3455
Jae Myoung SuhGraduate School of Medical Science and Engineering, KAIST, Daejeon, Republic of Korea. jmsuh@kaist.ac.kr.ORCID 0000-0001-8097-4662
Seoul National University · KRKorea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretory proteins are an essential component of interorgan communication networks that regulate animal physiology. Current approaches for identifying secretory proteins from specific cell and tissue types are largely limited to in vitro or ex vivo models which often fail to recapitulate in vivo biology. As such, there is mounting interest in developing in vivo analytical tools that can provide accurate information on the origin, identity, and spatiotemporal dynamics of secretory proteins. Here, we describe iSLET (in situ Secretory protein Labeling via ER-anchored TurboID) which selectively labels proteins that transit through the classical secretory pathway via catalytic actions of Sec61b-TurboID, a proximity labeling enzyme anchored in the ER lumen. To validate iSLET in a whole-body system, we express iSLET in the mouse liver and demonstrate efficient labeling of liver secretory proteins which could be tracked and identified within circulating blood plasma. Furthermore, proteomic analysis of the labeled liver secretome enriched from liver iSLET mouse plasma is highly consistent with previous reports of liver secretory protein profiles. Taken together, iSLET is a versatile and powerful tool for studying spatiotemporal dynamics of secretory proteins, a valuable class of biomarkers and therapeutic targets.

Indexed as

AnimalsEndoplasmic ReticulumHEK293 CellsHeLa CellsHep G2 CellsHumansLiverMiceMice, Inbred C57BLNIH 3T3 CellsProteomeProteomicsSecretory PathwaySEC Translocation ChannelsProteomeSEC61B protein, humanSEC Translocation Channels

Identifiers

PMID34471136
PMCPMC8410947
OpenAlexW3198499670

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.