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231225s2019 xx |||||o 00| ||eng c |
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7 |
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|a 10.1107/S1600577519005113
|2 doi
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|a pubmed24n1474.xml
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Stachowski, Timothy
|e verfasserin
|4 aut
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|a Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 17.02.2020
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|a Date Revised 18.07.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Dissociation of transforming growth factor beta-1 (TGFβ-1) from the inhibitory protein latency-associated peptide (LAP) can occur from low doses of X-ray irradiation of the LAP-TGFβ-1 complex, resulting in the activation of TGFβ-1, and can have health-related consequences. Using the tools and knowledge developed in the study of radiation damage in the crystallographic setting, small-angle X-ray scattering (SAXS) and complementary techniques suggest an activation process that is initiated but not driven by the initial X-ray exposure. LAP is revealed to be extended when not bound to TGFβ-1 and has a different structural conformation compared to the bound state. These studies pave the way for the structural understanding of systems impacted at therapeutic X-ray doses and show the potential impact of radiation damage studies beyond their original intent
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|a Journal Article
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|a SAXS
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|a latency-associated peptide
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|a radiation damage
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|a transforming growth factor beta-1
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|a Peptides
|2 NLM
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|a Protein Precursors
|2 NLM
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|a TGFB1 protein, human
|2 NLM
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| 650 |
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|a Transforming Growth Factor beta
|2 NLM
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|a Transforming Growth Factor beta1
|2 NLM
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| 650 |
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|a latency-associated propeptide, TGF-beta
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| 700 |
1 |
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|a Grant, Thomas D
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|a Snell, Edward H
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 26(2019), Pt 4 vom: 01. Juli, Seite 967-979
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|x 1600-5775
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|g volume:26
|g year:2019
|g number:Pt 4
|g day:01
|g month:07
|g pages:967-979
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|u http://dx.doi.org/10.1107/S1600577519005113
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