Evidence map›Paper›PMID 26445615›Full record

ArticleThoracic cancer2015

Identification of novel microtubule-binding proteins by taxol-mediated microtubule stabilization and mass spectrometry analysis.

Xianfei He, Zhu Liu, Qianqian He, Juan Qin, Ningning Liu, Linlin Zhang, Dengwen Li, Jun Zhou, Wenqing Shui, Min Liu

Open access · goldAbstract read
In one paragraph

Article in Thoracic cancer, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

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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

10 authors at 2 institutions in 1 country.

Xianfei HeState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Zhu LiuDepartment of Biochemistry, School of Basic Medical Sciences, Tianjin Medical University Tianjin, China.
Qianqian HeState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Juan QinState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Ningning LiuState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Linlin ZhangState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Dengwen LiState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Jun ZhouState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China.
Wenqing ShuiState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University Tianjin, China ; Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences Tianjin, China.
Min LiuDepartment of Biochemistry, School of Basic Medical Sciences, Tianjin Medical University Tianjin, China.
Nankai University · CNTianjin Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-binding proteins (MBPs) are structurally and functionally diverse regulators of microtubule-mediated cellular processes. Alteration of MBPs has been implicated in the pathogenesis of human diseases, including cancer. MBPs can stabilize or destabilize microtubules or move along microtubules to transport various cargoes. In addition, MBPs can control microtubule dynamics through direct interaction with microtubules or coordination with other proteins. To better understand microtubule structure and function, it is necessary to identify additional MBPs. In this study, we isolated microtubules and MBPs from mammalian cells by a taxol-based method and then profiled a panel of MBPs by mass spectrometry. We discovered a number of previously uncharacterized MBPs, including several membrane-associated proteins and proteins involved in post-translational modifications, in addition to several structural components. These results support the notion that microtubules have a wide range of functions and may undergo more exquisite regulation than previously recognized.

Indexed as

Mass spectrometrymicrotubulemicrotubule-binding proteintaxoltubulin

Identifiers

PMID26445615
PMCPMC4567012
OpenAlexW1587961229

What OpenQuestion holds

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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.