About: Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53

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About: Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	article (en) հոդված (hy) wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 2010 (uk) im Dezember 2010 veröffentlichter wissenschaftlicher Artikel (de) 2010 ഡിസംബര്‍ 1 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
publication date	wds:Q58166236-4D4F84E4-714F-4745-A8CF-8BB6AEFE6BAF
publication date	2010-12-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q58166236-0A6C8BEE-E77C-41CE-BE01-0BBDDEB264A4 wds:Q58166236-15DB6D8D-057A-44FD-96B6-949EEF92B668 wds:Q58166236-8518DA55-F513-4689-BA1A-DF943FA727B8 wds:Q58166236-A33FC3BD-D2F5-4677-B14A-EA9B3F2361C7 wds:Q58166236-C81D9B04-1375-49C1-83DF-F13D6D28E644 wds:Q58166236-D20F4CDC-F664-42E5-BB7A-C102A928A79A
author name string	Nick Tomczyk Perdita E. Barran Christoph Q. Schmidt Ted R. Hupp Hannah V. Florance Penka V. Nikolova
rdfs:label	Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (en) Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (nl)
skos:prefLabel	Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (en) Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (nl)
name	Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (en) Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (nl)
author	wds:Q58166236-0B19866D-33B8-446A-AEF0-444EA9004E28 wds:Q58166236-74430798-DF13-4CF6-912F-6725D09EFEF0
author	Paul N. Barlow Peter Faull
title	wds:Q58166236-8CD15115-3660-4E01-9E15-81BC97978E97
title	Utilising ion mobility-mass spectrometry to interrogate macromolecules: Factor H complement control protein modules 10–15 and 19–20 and the DNA-binding core domain of tumour suppressor p53 (en)
page(s)	wds:Q58166236-224D3687-890C-42BA-87A4-C8151C9FF0DC
page(s)	99-110
instance of	wds:Q58166236-D0A4FDC4-0ED5-44AA-9311-67B488665ED8
instance of	scholarly article
main subject	wds:Q58166236-4FCC9638-F2B0-4713-AE1A-029054DA8246
main subject	macromolecule
published in	wds:Q58166236-7ECC9616-D009-4CF9-AC94-33CCFD411FFA
published in	International Journal of Mass Spectrometry
issue	wds:Q58166236-C24B4B14-E145-4326-AF64-9E88F619FDAD
volume	wds:Q58166236-C0D88742-69BD-476C-BC1E-1C649DE4E8C3
issue	1-3
volume	298
DOI	wds:Q58166236-499F2412-0E02-4E59-90F9-58CBBBD5E9C7
DOI	http://dx.doi.org/10.1016/J.IJMS.2010.01.007
DOI	10.1016/J.IJMS.2010.01.007
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58166236
is cites work of	Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery Mass spectrometry methods for intrinsically disordered proteins. Visible and ultraviolet spectroscopy of gas phase protein ions. Intrinsic disorder in proteins: a challenge for (un)structural biology met by ion mobility-mass spectrometry Adding a new separation dimension to MS and LC-MS: What is the utility of ion mobility spectrometry? Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum
is cites work of	wds:Q38044422-1010C146-7EE6-47E8-B7D9-5FC024243938 wds:Q30402767-7A38D5EF-97F3-4C22-99C6-9EA62134A7AE wds:Q39721582-33576432-DD54-421C-9E14-C0688709B23D wds:Q38056343-087C02C7-0FA6-47F4-B302-B9855EDA9232 wds:Q38005330-C7664ECD-11CE-4B52-9524-041BE8B19DFD wds:Q47662080-5C66DD9F-1798-48E5-8DC4-CC46A6DE31A4

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