Novel octavalent cross-linker displays efficient trapping of protein protein interactions

S R Foster; A Pearce; A J Blake; M J Welham; J Dowden

doi:10.1039/b701542a

Novel octavalent cross-linker displays efficient trapping of protein protein interactions

S R Foster, A Pearce, A J Blake, M J Welham, J Dowden

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

1 Citation (SciVal)

Abstract

A novel octavalent, resorcin[4] arene derived, cross-linker designed to overcome some of the limitations of commercially available reagents is significantly more efficient for covalent stabilisation of protein-protein interactions.

Original language	English
Pages (from-to)	2512-2514
Number of pages	3
Journal	Chemical Communications
Issue number	24
DOIs	https://doi.org/10.1039/b701542a
Publication status	Published - 2007

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ID number: ISI:000247187900024

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10.1039/b701542a

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title = "Novel octavalent cross-linker displays efficient trapping of protein protein interactions",

abstract = "A novel octavalent, resorcin[4] arene derived, cross-linker designed to overcome some of the limitations of commercially available reagents is significantly more efficient for covalent stabilisation of protein-protein interactions.",

author = "Foster, {S R} and A Pearce and Blake, {A J} and Welham, {M J} and J Dowden",

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language = "English",

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journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

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AU - Foster, S R

AU - Pearce, A

AU - Blake, A J

AU - Welham, M J

AU - Dowden, J

N1 - ID number: ISI:000247187900024

PY - 2007

Y1 - 2007

N2 - A novel octavalent, resorcin[4] arene derived, cross-linker designed to overcome some of the limitations of commercially available reagents is significantly more efficient for covalent stabilisation of protein-protein interactions.

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U2 - 10.1039/b701542a

DO - 10.1039/b701542a

M3 - Article

SN - 1359-7345

SP - 2512

EP - 2514

JO - Chemical Communications

JF - Chemical Communications

IS - 24

ER -

Novel octavalent cross-linker displays efficient trapping of protein protein interactions

Abstract

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