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Peptidomics

Overview of attention for book
Cover of 'Peptidomics'

Table of Contents

  1. Altmetric Badge
    Book Overview
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    Chapter 1 Origins, Technological Development, and Applications of Peptidomics
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    Chapter 2 Brain Tissue Sample Stabilization and Extraction Strategies for Neuropeptidomics
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    Chapter 3 Isolation of Endogenous Peptides from Cultured Cell Conditioned Media for Mass Spectrometry
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    Chapter 4 Mass Spectrometric Identification of Endogenous Peptides
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    Chapter 5 Bioinformatics for Prohormone and Neuropeptide Discovery
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    Chapter 6 Substrate Capture Assay Using Inactive Oligopeptidases to Identify Novel Peptides
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    Chapter 7 Non-targeted Identification of d-Amino Acid-Containing Peptides Through Enzymatic Screening, Chiral Amino Acid Analysis, and LC-MS
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    Chapter 8 Quantitative Peptidomics: General Considerations
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    Chapter 9 Quantitative Peptidomics with Isotopic and Isobaric Tags
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    Chapter 10 Quantitative Peptidomics Using Reductive Methylation of Amines
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    Chapter 11 Metabolic Labeling to Quantify Drosophila Neuropeptides and Peptide Hormones
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    Chapter 12 Data Preprocessing, Visualization, and Statistical Analyses of Nontargeted Peptidomics Data from MALDI-MS
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    Chapter 13 Affinity Purification of Neuropeptide Precursors from Mice Lacking Carboxypeptidase E Activity
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    Chapter 14 Mass Spectrometry Based Immunopeptidomics for the Discovery of Cancer Neoantigens
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    Chapter 15 Milk Peptidomics to Identify Functional Peptides and for Quality Control of Dairy Products
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    Chapter 16 Neuropeptidomic Analysis of Zebrafish Brain
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    Chapter 17 Identification, Quantitation, and Imaging of the Crustacean Peptidome
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    Chapter 18 Identification of Endogenous Neuropeptides in the Nematode C. elegans Using Mass Spectrometry
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    Chapter 19 EndoProteoFASP as a Tool to Unveil the Peptidome-Protease Profile: Application to Salivary Diagnostics
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    Chapter 20 Methodology for Urine Peptidome Analysis Based on Nano-HPLC Coupled to Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
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    Chapter 21 Identification of Components in Frog Skin Secretions with Therapeutic Potential as Antidiabetic Agents
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    Chapter 22 High-Accuracy Mass Spectrometry Based Screening Method for the Discovery of Cysteine Containing Peptides in Animal Venoms and Toxins
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    Chapter 23 Analysis of the Snake Venom Peptidome
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    Chapter 24 Identification of Peptides in Spider Venom Using Mass Spectrometry
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    Chapter 25 Single Cell Peptidomics: Approach for Peptide Identification by N-Terminal Peptide Derivatization
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    Chapter 26 Peptidomic Identification of Cysteine-Rich Peptides from Plants
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    Chapter 27 Analysis of Endogenous Peptide Pools of Physcomitrella patens Moss
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    Chapter 28 The Bright Future of Peptidomics
Attention for Chapter 24: Identification of Peptides in Spider Venom Using Mass Spectrometry
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Chapter title
Identification of Peptides in Spider Venom Using Mass Spectrometry
Chapter number 24
Book title
Peptidomics
Published in
Methods in molecular biology, February 2018
DOI 10.1007/978-1-4939-7537-2_24
Pubmed ID
29476524
Book ISBNs
978-1-4939-7536-5, 978-1-4939-7537-2
Authors

Rafael L. Lomazi, Erika S. Nishiduka, Pedro I. SilvaJr, Alexandre K. Tashima, Pedro I. Silva, Lomazi, Rafael L., Nishiduka, Erika S., Silva, Pedro I., Tashima, Alexandre K.

Abstract

Spider venoms are composed of hundreds of proteins and peptides. Several of these venom toxins are cysteine-rich peptides in the mass range of 3-9 kDa. Small peptides (<3 kDa) can be fully characterized by mass spectrometry analysis, while proteins are generally identified by the bottom-up approach in which proteins are first digested with trypsin to generate shorter peptides for MS/MS characterization. In general, it is sufficient for protein identification to sequence two or more peptides, but for venom peptidomics it is desirable to completely elucidate peptide sequences and the number of disulfide bonds in the molecules. In this chapter we describe a methodology to completely sequence and determine the number of disulfide bonds of spider venom peptides in the mass range of 3-9 kDa by multiple enzyme digestion, mass spectrometry of native and digested peptides, de novo analysis, and sequence overlap alignment.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 22 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 4 18%
Student > Ph. D. Student 3 14%
Student > Master 3 14%
Other 2 9%
Researcher 2 9%
Other 3 14%
Unknown 5 23%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 41%
Agricultural and Biological Sciences 2 9%
Chemistry 2 9%
Medicine and Dentistry 1 5%
Engineering 1 5%
Other 0 0%
Unknown 7 32%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 17 January 2019.
All research outputs
#18,589,103
of 23,025,074 outputs
Outputs from Methods in molecular biology
#7,969
of 13,170 outputs
Outputs of similar age
#256,997
of 330,613 outputs
Outputs of similar age from Methods in molecular biology
#39
of 58 outputs
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So far Altmetric has tracked 13,170 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 24th percentile – i.e., 24% of its peers scored the same or lower than it.
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