Evidence map›Paper›PMID 38362424›Full record

ArticleChemical science2024

Probing the functional hotspots inside protein hydrophobic pockets by

Can Lai, Zhiyao Tang, Zheyi Liu, Pan Luo, Wenxiang Zhang, Tingting Zhang, Wenhao Zhang, Zhe Dong, Xinyuan Liu, Xueming Yang and 1 more

Abstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Analytical chemistry · 2026
    Article
  3. Article
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

11 authors.

Can LaiCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Zhiyao TangDepartment of Chemistry, College of Science, Southern University of Science and Technology Shenzhen 518055 China dongz@sustech.edu.cn.
Zheyi LiuCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Pan LuoCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Wenxiang ZhangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Tingting ZhangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Wenhao ZhangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.
Zhe DongDepartment of Chemistry, College of Science, Southern University of Science and Technology Shenzhen 518055 China dongz@sustech.edu.cn.
Xinyuan LiuDepartment of Chemistry, College of Science, Southern University of Science and Technology Shenzhen 518055 China dongz@sustech.edu.cn.ORCID https://orcid.org/0000-0002-6978-6465
Xueming YangDepartment of Chemistry, College of Science, Southern University of Science and Technology Shenzhen 518055 China dongz@sustech.edu.cn.ORCID https://orcid.org/0000-0001-6684-9187
Fangjun WangCAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian 116023 China wangfj@dicp.ac.cn.ORCID https://orcid.org/0000-0002-8118-7019

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to the complex high-order structures and interactions of proteins within an aqueous solution, a majority of chemical functionalizations happen on the hydrophilic sites of protein external surfaces which are naturally exposed to the solution. However, the hydrophobic pockets inside proteins are crucial for ligand binding and function as catalytic centers and transporting tunnels. Herein, we describe a reagent pre-organization and

Identifiers

PMID38362424
PMCPMC10866368

What OpenQuestion holds

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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.