Special Issue "Protein-Protein Interactions"

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A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: closed (30 November 2014)

Special Issue Editor

Guest Editor
Prof. Dr. Thorsten Berg
University of Leipzig, Institute for Organic Chemistry, Johannisallee 29, 04103 Leipzig, Germany
Website: http://www.uni-leipzig.de/~tberg

Special Issue Information

Submission

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. Biology 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 600 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.

Published Papers (9 papers)

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Displaying article 1-9
p. 424-442
by  and
Biology 2015, 4(2), 424-442; doi:10.3390/biology4020424
Received: 10 March 2015 / Revised: 25 May 2015 / Accepted: 29 May 2015 / Published: 12 June 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
p. 344-366
by ,  and
Biology 2015, 4(2), 344-366; doi:10.3390/biology4020344
Received: 24 February 2015 / Revised: 27 March 2015 / Accepted: 11 April 2015 / Published: 21 April 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
p. 327-343
by , , ,  and
Biology 2015, 4(2), 327-343; doi:10.3390/biology4020327
Received: 16 January 2015 / Revised: 24 March 2015 / Accepted: 31 March 2015 / Published: 9 April 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
p. 282-297
by  and
Biology 2015, 4(2), 282-297; doi:10.3390/biology4020282
Received: 27 November 2014 / Accepted: 16 March 2015 / Published: 24 March 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
p. 237-250
by , , , ,  and
Biology 2015, 4(1), 237-250; doi:10.3390/biology4010237
Received: 1 December 2014 / Revised: 8 February 2015 / Accepted: 16 February 2015 / Published: 6 March 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
p. 161-172
by , ,  and
Biology 2015, 4(1), 161-172; doi:10.3390/biology4010161
Received: 20 December 2014 / Revised: 11 February 2015 / Accepted: 17 February 2015 / Published: 2 March 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
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p. 133-150
by
Biology 2015, 4(1), 133-150; doi:10.3390/biology4010133
Received: 12 December 2014 / Accepted: 4 February 2015 / Published: 12 February 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
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p. 88-103
by ,  and
Biology 2015, 4(1), 88-103; doi:10.3390/biology4010088
Received: 25 November 2014 / Revised: 22 January 2015 / Accepted: 23 January 2015 / Published: 5 February 2015
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(This article belongs to the Special Issue Protein-Protein Interactions)
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p. 41-49
by , , ,  and
Biology 2015, 4(1), 41-49; doi:10.3390/biology4010041
Received: 28 November 2014 / Accepted: 4 January 2015 / Published: 9 January 2015
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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: Article
Title: A pull-down method for an intra-cross linked peptide with a cell-free translation system
Authors: Yutaro Tanemura, Yuki Mochizuki, Shigeyuki Kumachi, Naoto Nemoto
Affiliations: Graduate School of Science and Engineering, Saitama University, Saitama, Japan; E-Mail: nemoto@fms.saitama-u.ac.jp
Abstract: Constrained peptides are an attractive class as affinity regents or drug leads owing to their exhibit excellent binding properties. Many kinds of constrained peptides, such as cyclic peptides, have been found in nature or designed artificially by directed evolution. However, confirming binding properties of the constrained peptides can generally be troublesome because the synthesis of constrained peptides is more complicated in comparison with linear peptides. In this paper, we showed that biotinylated constrained peptides containing a disulfide bridge or a chemical cross-linking could be synthesized using a cell-free translation system and analyzed with a puromycin-linker in the manner of pull-down assay method.

Type of paper: Review
Title: Eukaryotic LYR proteins interact with ancient mitochondrial protein complexes
Author: Heike Angerer
Affiliation: Goethe University Frankfurt, Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Frankfurt am Main, Germany; E-Mail: Angerer@em.uni-frankfurt.de
Abstract: In eukaryotic cells mitochondria host ancient essential bioenergetic and biosynthetic pathways that are under nuclear control. LYR (leucine/tyrosine/arginine) motif proteins (LYRMs) of the Complex1_LYR-like superfamily interact with protein complexes of alpha-proteobacteria origin. Many LYR proteins function as extra subunits or novel assembly factors of the oxidative phosphorylation (OXPHOS) core complexes. Structural insights about complex I accessory subunits LYRM6 and LYRM3 have been provided by structural analyses of EM and X-ray structures of complex I from bovine and the yeast Yarrowia lipolytica, respectively. Both LYRMs anchor independently an acyl carrier protein (ACPM) to complex I. The function of this duplicated protein interaction of ACPM with respiratory complex I is still unknown. Analysis of protein-protein interaction screens, genetic analyses and predicted multi-domain LYRMs offer further clues on an interaction network of LYR proteins in mitochondria.


Title: KAP1 is a novel substrate for the arginine methyltransferase PRMT5
Authors: Roberta di Caprio, Michela Ciano, Giorgia Montano, Paola Costanzo and Elena Cesaro
Affiliations: Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy; E-Mail: paola.costanzo@unina.it
Abstract: KAP1, the transcriptional corepressor of Kruppel-associated box zinc finger proteins (KRAB-ZFPs), is subjected to multiple post-translational modifications that are involved in fine-tuning of its multiple biological functions.
We previously identified the protein arginine methyltransferase PRMT5 as a component of repression complex mediated by the KRAB-ZFP ZNF224. In this study, we show that KAP1 interacts with PRMT5 and is a novel substrate for PRMT5 methylation. Also, we present evidence that the methylation of KAP1 arginine residues regulate the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-transcriptional modification could actively contribute to the regulation of ZNF224-mediated repression.

Last update: 20 November 2014

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