All subdomains of the talin rod are mechanically vulnerable and may contribute to cellular mechanosensing
- Submitting institution
-
Imperial College of Science, Technology and Medicine
- Unit of assessment
- 12 - Engineering
- Output identifier
- 384
- Type
- D - Journal article
- DOI
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10.1021/acsnano.6b01658
- Title of journal
- ACS Nano
- Article number
- -
- First page
- 6648
- Volume
- 10
- Issue
- 7
- ISSN
- 1936-0851
- Open access status
- Compliant
- Month of publication
- July
- Year of publication
- 2016
- URL
-
-
- Supplementary information
-
10.1021/acsnano.6b01658
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- No
- Number of additional authors
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4
- Research group(s)
-
-
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- The discoveries were highlighted in an editorial article in Advances in Engineering (https://advanceseng.com/all-subdomains-talin-rod-mechanically-vulnerable-contribute-cellular-mechanosensing/). Led to the follow-up discovery of a cellular mechanism by which protein unfolding controls the activation of the tumour suppressor DLC1 and cell mechanics (https://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.2005599). This work underpinned a collaboration with Professor Hytonen (Tampere University) and enabled follow-up discoveries on the unfolding patterns of alpha helical proteins (https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1006126). The work also led to an invitation to the last author to present at the European Research Council Summit London 2017. An ERC Proof-of-Concept grant was awarded for follow-up research (MechanoGPER, £150k).
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -