Special Issue "Chemokines"


A special issue of Pharmaceuticals (ISSN 1424-8247).

Deadline for manuscript submissions: closed (30 April 2013)

Special Issue Editor

Guest Editor
Dr. Mark Murphy

Research Immunology, Actelion Pharmaceuticals Ltd, Gewerbestrasse 16, CH- 4123 Allschwil, Switzerland
Website: http://www.actelion.com/
Interests: immunology; targeted therapies for inflammatory and autoimmune diseases; signal transduction pathways as innovative therapeutic targets; stem cells; protein-protein interactions; targeted therapies for cancer; cytokines/chemokines

Special Issue Information


Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Pharmaceuticals is an international peer-reviewed Open Access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 800 CHF (Swiss Francs).

Published Papers (2 papers)

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p. 1145-1169
by ,  and
Pharmaceuticals 2013, 6(9), 1145-1169; doi:10.3390/ph6091145
Received: 28 June 2013 / Revised: 18 August 2013 / Accepted: 4 September 2013 / Published: 23 September 2013
Show/Hide Abstract | Cited by 8 | PDF Full-text (690 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Chemokines)
p. 929-959
by ,  and
Pharmaceuticals 2013, 6(8), 929-959; doi:10.3390/ph6080929
Received: 9 May 2013 / Revised: 3 July 2013 / Accepted: 29 July 2013 / Published: 6 August 2013
Show/Hide Abstract | Cited by 33 | PDF Full-text (611 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Chemokines)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Review
Title: Orthosteric and Allosteric Ligand Interactions within the Chemokine System-­‐Implications for Future Drug Design
Authors: Stefanie Thiele and Mette M. Rosenkilde
Affiliation: The Laboratory of Molecular Pharmacology, Department of Neuroscience and Pharmacology, University of Copenhagen, The Panum Institute, Copenhagen, DK-2200, Denmark
Abstract: Chemokine receptors are class A 7TM receptors, thereby belonging to the largest protein group in the human genome. Together with their peptide ligands they control cell migration, and have been targets for drug development resulting in numerous small molecule drug candidates. Given the large size and extracellular receptor interaction of chemokines with their receptors, small molecules often act in an allosteric mode with a site within the transmembrane domain, and studies showing their probe-­‐dependent and receptor-­‐dependent character are accumulating. This mode of action is in clear contrast to prototype class A 7TM receptors, such as the adrenergic receptors, or class C 7TM receptors in which small molecule allosteric sites are often found in the extracellular domains. Here, the structural knowledge on chemokine and small-­‐molecule ligand interaction with chemokine receptors is reviewed, providing the basis for understanding the diversity of allosteric interactions in chemokine receptors.

Last update: 25 March 2013

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