333 research outputs found
Physicochemical property distributions for accurate and rapid pairwise protein homology detection
<p>Abstract</p> <p>Background</p> <p>The challenge of remote homology detection is that many evolutionarily related sequences have very little similarity at the amino acid level. Kernel-based discriminative methods, such as support vector machines (SVMs), that use vector representations of sequences derived from sequence properties have been shown to have superior accuracy when compared to traditional approaches for the task of remote homology detection.</p> <p>Results</p> <p>We introduce a new method for feature vector representation based on the physicochemical properties of the primary protein sequence. A distribution of physicochemical property scores are assembled from 4-mers of the sequence and normalized based on the null distribution of the property over all possible 4-mers. With this approach there is little computational cost associated with the transformation of the protein into feature space, and overall performance in terms of remote homology detection is comparable with current state-of-the-art methods. We demonstrate that the features can be used for the task of pairwise remote homology detection with improved accuracy versus sequence-based methods such as BLAST and other feature-based methods of similar computational cost.</p> <p>Conclusions</p> <p>A protein feature method based on physicochemical properties is a viable approach for extracting features in a computationally inexpensive manner while retaining the sensitivity of SVM protein homology detection. Furthermore, identifying features that can be used for generic pairwise homology detection in lieu of family-based homology detection is important for applications such as large database searches and comparative genomics.</p
MPLEx: a Robust and Universal Protocol for Single-Sample Integrative Proteomic, Metabolomic, and Lipidomic Analyses
ABSTRACT Integrative multi-omics analyses can empower more effective investigation and complete understanding of complex biological systems. Despite recent advances in a range of omics analyses, multi-omic measurements of the same sample are still challenging and current methods have not been well evaluated in terms of reproducibility and broad applicability. Here we adapted a solvent-based method, widely applied for extracting lipids and metabolites, to add proteomics to mass spectrometry-based multi-omics measurements. The m etabolite, p rotein, and l ipid ex traction (MPLEx) protocol proved to be robust and applicable to a diverse set of sample types, including cell cultures, microbial communities, and tissues. To illustrate the utility of this protocol, an integrative multi-omics analysis was performed using a lung epithelial cell line infected with Middle East respiratory syndrome coronavirus, which showed the impact of this virus on the host glycolytic pathway and also suggested a role for lipids during infection. The MPLEx method is a simple, fast, and robust protocol that can be applied for integrative multi-omic measurements from diverse sample types (e.g., environmental, in vitro , and clinical). IMPORTANCE In systems biology studies, the integration of multiple omics measurements (i.e., genomics, transcriptomics, proteomics, metabolomics, and lipidomics) has been shown to provide a more complete and informative view of biological pathways. Thus, the prospect of extracting different types of molecules (e.g., DNAs, RNAs, proteins, and metabolites) and performing multiple omics measurements on single samples is very attractive, but such studies are challenging due to the fact that the extraction conditions differ according to the molecule type. Here, we adapted an organic solvent-based extraction method that demonstrated broad applicability and robustness, which enabled comprehensive proteomics, metabolomics, and lipidomics analyses from the same sample
CSF H3F3A K27M circulating tumor DNA copy number quantifies tumor growth and in vitro treatment response
https://deepblue.lib.umich.edu/bitstream/2027.42/145434/1/40478_2018_Article_580.pd
ΠΠΈΠ½Π°ΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ΅Π½Π΄Π΅Π½ΡΠΈΠΈ Π² ΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΈΠΈ ΠΏΡΠ΅Π΄ΠΌΠ΅ΡΠ° Π»ΠΈΠ½Π³Π²ΠΎΡΠΊΠΎΠ»ΠΎΠ³ΠΈΠΈ
ΠΠΊΠΎΠ»ΠΎΠ³ΠΈΠ·Π°ΡΠΈΡ Π²ΡΠ΅Ρ
ΡΡΠ΅Ρ ΠΎΠ±ΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎΠΉ ΠΆΠΈΠ·Π½ΠΈ ΠΈ ΡΠ°ΠΌΠΎΠ³ΠΎ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ° ΡΠΈΡΠΎΠΊΠΎ ΠΎΠ±ΡΡΠΆΠ΄Π°Π΅ΡΡΡ Π²ΠΎ ΠΌΠ½ΠΎΠ³ΠΈΡ
Π½Π°ΡΠΊΠ°, Π° ΡΠ°ΠΊΠΆΠ΅ ΠΈ Π² ΠΎΠ±Π»Π°ΡΡΠΈ ΡΠ·ΡΠΊΠ°. ΠΠΎ ΠΌΠ½ΠΎΠ³ΠΈΡ
ΡΠ°Π±ΠΎΡΠ°Ρ
Π»ΠΈΠ½Π³Π²ΠΈΡΡΠΎΠ² ΡΠΊΠΎΠ»ΠΎΠ³ΠΈΡ ΡΠ·ΡΠΊΠ° ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅ΡΡΡ ΠΊΠ°ΠΊ Π½Π°ΡΠΊΠ° ΠΎ
Π²Π·Π°ΠΈΠΌΠΎΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΡΡ
ΠΌΠ΅ΠΆΠ΄Ρ ΡΠ·ΡΠΊΠΎΠΌ ΠΈ Π΅Π³ΠΎ ΠΎΠΊΡΡΠΆΠ΅Π½ΠΈΠ΅ΠΌ, ΡΠ°ΠΊ ΠΊΠ°ΠΊ ΡΠ·ΡΠΊ ΡΡΡΠ΅ΡΡΠ²ΡΠ΅Ρ Π½Π΅ ΡΠΎΠ»ΡΠΊΠΎ Π² ΡΠΎΠ·Π½Π°Π½ΠΈΠΈ Π³ΠΎΠ²ΠΎΡΡΡΠΈΡ
Π½Π° Π½Π΅ΠΌ ΠΈ ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΡΠ΅Ρ ΡΠΎΠ»ΡΠΊΠΎ ΠΏΡΠΈ Π²Π·Π°ΠΈΠΌΠΎΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΡΡ
Ρ Π΄ΡΡΠ³ΠΈΠΌΠΈ ΠΊΠΎΠΌΠΌΡΠ½ΠΈΠΊΠ°Π½ΡΠ°ΠΌΠΈ ΠΈ Ρ ΠΈΡ
ΡΠΎΡΠΈΠ°Π»ΡΠ½ΡΠΌ ΠΈ ΠΏΡΠΈΡΠΎΠ΄Π½ΡΠΌ ΠΎΠΊΡΡΠΆΠ΅Π½ΠΈΠ΅ΠΌ. Π ΡΡΠΎΠΌ ΠΊΠΎΠ½ΡΠ΅ΠΊΡΡΠ΅ ΠΏΠΎΠ½ΡΡΠΈΠ΅ Β«ΡΠ·ΡΠΊΠΎΠ²ΠΎΠ΅ ΡΠΎΠ·Π½Π°Π½ΠΈΠ΅Β» ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»ΡΠ΅Ρ ΡΠΎΠ±ΠΎΠΉ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΡΡ ΠΊΠ°ΡΡΠΈΠ½Ρ Π²Π·Π°ΠΈΠΌΠΎΡΠ²ΡΠ·ΠΈ ΠΊΡΠ»ΡΡΡΡΡ ΠΈ ΠΎΠ±ΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎΠΉ ΠΆΠΈΠ·Π½ΠΈ ΡΠΎΡΠΈΡΠΌΠ°, ΠΊΠΎΡΠΎΡΠ°Ρ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅Ρ Π΅Π³ΠΎ ΠΏΡΠΈΡ
ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΎΠ΅ ΡΠ²ΠΎΠ΅ΠΎΠ±ΡΠ°Π·ΠΈΠ΅ ΠΈ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ΅ΡΡΡ Π΄Π°Π½Π½ΠΎΠ³ΠΎ ΡΠ·ΡΠΊΠ°
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