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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.6b01020
|2 doi
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|a pubmed25n0867.xml
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|a (DE-627)NLM260233366
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|a (NLM)27166821
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Forato, Florian
|e verfasserin
|4 aut
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| 245 |
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|a Comparison of Zirconium Phosphonate-Modified Surfaces for Immobilizing Phosphopeptides and Phosphate-Tagged Proteins
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|c 2016
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 05.06.2018
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|a Date Revised 05.06.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Different routes for preparing zirconium phosphonate-modified surfaces for immobilizing biomolecular probes are compared. Two chemical-modification approaches were explored to form self-assembled monolayers on commercially available primary amine-functionalized slides, and the resulting surfaces were compared to well-characterized zirconium phosphonate monolayer-modified supports prepared using Langmuir-Blodgett methods. When using POCl3 as the amine phosphorylating agent followed by treatment with zirconyl chloride, the result was not a zirconium-phosphonate monolayer, as commonly assumed in the literature, but rather the process gives adsorbed zirconium oxide/hydroxide species and to a lower extent adsorbed zirconium phosphate and/or phosphonate. Reactions giving rise to these products were modeled in homogeneous-phase studies. Nevertheless, each of the three modified surfaces effectively immobilized phosphopeptides and phosphopeptide tags fused to an affinity protein. Unexpectedly, the zirconium oxide/hydroxide modified surface, formed by treating the amine-coated slides with POCl3/Zr(4+), afforded better immobilization of the peptides and proteins and efficient capture of their targets
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|a Comparative Study
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Archaeal Proteins
|2 NLM
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|a DNA-Binding Proteins
|2 NLM
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|a Organophosphonates
|2 NLM
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|a Phosphopeptides
|2 NLM
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|a Phosphoproteins
|2 NLM
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|a Sac7 protein, Sulfolobus
|2 NLM
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|a 169149-38-6
|2 NLM
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|a Zirconium
|2 NLM
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|a C6V6S92N3C
|2 NLM
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| 700 |
1 |
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|a Liu, Hao
|e verfasserin
|4 aut
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1 |
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|a Benoit, Roland
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Fayon, Franck
|e verfasserin
|4 aut
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1 |
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|a Charlier, Cathy
|e verfasserin
|4 aut
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1 |
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|a Fateh, Amina
|e verfasserin
|4 aut
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1 |
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|a Defontaine, Alain
|e verfasserin
|4 aut
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1 |
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|a Tellier, Charles
|e verfasserin
|4 aut
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1 |
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|a Talham, Daniel R
|e verfasserin
|4 aut
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|a Queffélec, Clémence
|e verfasserin
|4 aut
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|a Bujoli, Bruno
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 32(2016), 22 vom: 07. Juni, Seite 5480-90
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:32
|g year:2016
|g number:22
|g day:07
|g month:06
|g pages:5480-90
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|u http://dx.doi.org/10.1021/acs.langmuir.6b01020
|3 Volltext
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|d 32
|j 2016
|e 22
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|c 06
|h 5480-90
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