Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
Journals
Microarrays
Special Issues
Peptide Microarrays
share announcement

Peptide Microarrays

A special issue of Microarrays (ISSN 2076-3905).

Deadline for manuscript submissions: closed (31 May 2015) | Viewed by 9630

Special Issue Editors

Prof. Dr. Frank Breitling

E-Mail Website
Guest Editor
Karlsruhe Institute of Technology, Institute of Microstructure Technology, Hermann-von-Helmholtz-Platz 1, 76344 Eggenstein-Leopoldshafen, Germany
Dr. Alexander Nesterov-Müller

E-Mail Website
Guest Editor
Karlsruhe Institute of Technology, Institute of Microstructure Technology, Hermann-von-Helmholtz-Platz 1, 76344 Eggenstein-Leopoldshafen, Germany

Special Issue Information

Dear Colleagues,

A quarter century since their invention by Ronald Frank, peptide arrays now move into the focus of the life sciences. Three features make them very attractive for researchers from different fields: (1) they are suitable for high throughput analysis; (2) individual peptides allow a direct linkage to the proteome level, e.g., by revealing the pathogen an antibody is targeting; and (3) peptides fold into many different unique 3D structures that might help to advance also neighboring scientific fields, e.g., chemical catalysis.

This Special Issue will collate contributions on peptide array methodology, their biophysical and bioengineering applications, peptide array based studies of posttranslational modifications, protein–protein interactions, drug discovery and drug delivery.

Prof. Dr. Frank Breitling
Dr. Alexander Nesterov-Müller
Guest Editors

Manuscript Submission 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. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Microarrays 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 350 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


Keywords

  • microarrays
  • peptide libraries
  • high throughput analysis
  • seromics
  • posttranslational modifications
  • interacteom

Published Papers (2 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

307 KiB  
Article
A Synthetic Kinome Microarray Data Generator
by Farhad Maleki and Anthony Kusalik
Microarrays 2015, 4(4), 432-453; https://doi.org/10.3390/microarrays4040432 - 16 Oct 2015
Cited by 3 | Viewed by 4310
Abstract
Cellular pathways involve the phosphorylation and dephosphorylation of proteins. Peptide microarrays called kinome arrays facilitate the measurement of the phosphorylation activity of hundreds of proteins in a single experiment. Analyzing the data from kinome microarrays is a multi-step process. Typically, various techniques are [...] Read more.
Cellular pathways involve the phosphorylation and dephosphorylation of proteins. Peptide microarrays called kinome arrays facilitate the measurement of the phosphorylation activity of hundreds of proteins in a single experiment. Analyzing the data from kinome microarrays is a multi-step process. Typically, various techniques are possible for a particular step, and it is necessary to compare and evaluate them. Such evaluations require data for which correct analysis results are known. Unfortunately, such kinome data is not readily available in the community. Further, there are no established techniques for creating artificial kinome datasets with known results and with the same characteristics as real kinome datasets. In this paper, a methodology for generating synthetic kinome array data is proposed. The methodology relies on actual intensity measurements from kinome microarray experiments and preserves their subtle characteristics. The utility of the methodology is demonstrated by evaluating methods for eliminating heterogeneous variance in kinome microarray data. Phosphorylation intensities from kinome microarrays often exhibit such heterogeneous variance and its presence can negatively impact downstream statistical techniques that rely on homogeneity of variance. It is shown that using the output from the proposed synthetic data generator, it is possible to critically compare two variance stabilization methods. Full article
(This article belongs to the Special Issue Peptide Microarrays)
►▼ Show Figures

Figure 1

1625 KiB  
Communication
SPOTing Acetyl-Lysine Dependent Interactions
by Sarah Picaud and Panagis Filippakopoulos
Microarrays 2015, 4(3), 370-388; https://doi.org/10.3390/microarrays4030370 - 17 Aug 2015
Cited by 10 | Viewed by 5042
Abstract
Post translational modifications have been recognized as chemical signals that create docking sites for evolutionary conserved effector modules, allowing for signal integration within large networks of interactions. Lysine acetylation in particular has attracted attention as a regulatory modification, affecting chromatin structure and linking [...] Read more.
Post translational modifications have been recognized as chemical signals that create docking sites for evolutionary conserved effector modules, allowing for signal integration within large networks of interactions. Lysine acetylation in particular has attracted attention as a regulatory modification, affecting chromatin structure and linking to transcriptional activation. Advances in peptide array technologies have facilitated the study of acetyl-lysine-containing linear motifs interacting with the evolutionary conserved bromodomain module, which specifically recognizes and binds to acetylated sequences in histones and other proteins. Here we summarize recent work employing SPOT peptide technology to identify acetyl-lysine dependent interactions and document the protocols adapted in our lab, as well as our efforts to characterize such bromodomain-histone interactions. Our results highlight the versatility of SPOT methods and establish an affordable tool for rapid access to potential protein/modified-peptide interactions involving lysine acetylation. Full article
(This article belongs to the Special Issue Peptide Microarrays)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-2
Back to TopTop