Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2. / Jensen, P.C.; Thiele, S; Steen, A; Elder, A; Kolbeck, R; Ghosh, Sudip; Frimurer, T M; Rosenkilde, Mette Marie.

In: British Journal of Pharmacology, Vol. 166, No. 1, 05.2012, p. 258-75.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jensen, PC, Thiele, S, Steen, A, Elder, A, Kolbeck, R, Ghosh, S, Frimurer, TM & Rosenkilde, MM 2012, 'Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2', British Journal of Pharmacology, vol. 166, no. 1, pp. 258-75. https://doi.org/10.1111/j.1476-5381.2011.01771.x

APA

Jensen, P. C., Thiele, S., Steen, A., Elder, A., Kolbeck, R., Ghosh, S., Frimurer, T. M., & Rosenkilde, M. M. (2012). Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2. British Journal of Pharmacology, 166(1), 258-75. https://doi.org/10.1111/j.1476-5381.2011.01771.x

Vancouver

Jensen PC, Thiele S, Steen A, Elder A, Kolbeck R, Ghosh S et al. Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2. British Journal of Pharmacology. 2012 May;166(1):258-75. https://doi.org/10.1111/j.1476-5381.2011.01771.x

Author

Jensen, P.C. ; Thiele, S ; Steen, A ; Elder, A ; Kolbeck, R ; Ghosh, Sudip ; Frimurer, T M ; Rosenkilde, Mette Marie. / Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2. In: British Journal of Pharmacology. 2012 ; Vol. 166, No. 1. pp. 258-75.

Bibtex

@article{d6d4853200304557b704106bbdcdb25d,
title = "Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2",
abstract = "The majority of small molecule compounds targeting chemokine receptors share a similar pharmacophore with a centrally located aliphatic positive charge and flanking aromatic moieties. Here we describe a novel piperidine-based compound with structural similarity to previously described CCR8-specific agonists, but containing a unique phenyl-tetrazol moiety which, in addition to activity at CCR8 was also active at CCR1.",
keywords = "Animals, Binding Sites, COS Cells, Cercopithecus aethiops, Glutamic Acid, Humans, Inositol 1,4,5-Trisphosphate, Ligands, Models, Molecular, Piperidines, Point Mutation, Receptors, CCR1, Receptors, CCR8, Tetrazoles",
author = "P.C. Jensen and S Thiele and A Steen and A Elder and R Kolbeck and Sudip Ghosh and Frimurer, {T M} and Rosenkilde, {Mette Marie}",
note = "{\textcopyright} 2011 The Authors. British Journal of Pharmacology {\textcopyright} 2011 The British Pharmacological Society.",
year = "2012",
month = may,
doi = "10.1111/j.1476-5381.2011.01771.x",
language = "English",
volume = "166",
pages = "258--75",
journal = "British Journal of Pharmacology",
issn = "0007-1188",
publisher = "Wiley",
number = "1",

}

RIS

TY - JOUR

T1 - Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2

AU - Jensen, P.C.

AU - Thiele, S

AU - Steen, A

AU - Elder, A

AU - Kolbeck, R

AU - Ghosh, Sudip

AU - Frimurer, T M

AU - Rosenkilde, Mette Marie

N1 - © 2011 The Authors. British Journal of Pharmacology © 2011 The British Pharmacological Society.

PY - 2012/5

Y1 - 2012/5

N2 - The majority of small molecule compounds targeting chemokine receptors share a similar pharmacophore with a centrally located aliphatic positive charge and flanking aromatic moieties. Here we describe a novel piperidine-based compound with structural similarity to previously described CCR8-specific agonists, but containing a unique phenyl-tetrazol moiety which, in addition to activity at CCR8 was also active at CCR1.

AB - The majority of small molecule compounds targeting chemokine receptors share a similar pharmacophore with a centrally located aliphatic positive charge and flanking aromatic moieties. Here we describe a novel piperidine-based compound with structural similarity to previously described CCR8-specific agonists, but containing a unique phenyl-tetrazol moiety which, in addition to activity at CCR8 was also active at CCR1.

KW - Animals

KW - Binding Sites

KW - COS Cells

KW - Cercopithecus aethiops

KW - Glutamic Acid

KW - Humans

KW - Inositol 1,4,5-Trisphosphate

KW - Ligands

KW - Models, Molecular

KW - Piperidines

KW - Point Mutation

KW - Receptors, CCR1

KW - Receptors, CCR8

KW - Tetrazoles

U2 - 10.1111/j.1476-5381.2011.01771.x

DO - 10.1111/j.1476-5381.2011.01771.x

M3 - Journal article

C2 - 22050085

VL - 166

SP - 258

EP - 275

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 1

ER -

ID: 48972161