ArticleAnalytical chemistry2009
Combining bottom-up and top-down mass spectrometric strategies for de novo sequencing of the crustacean hyperglycemic hormone from Cancer borealis.
Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Decoding Neuropeptide Complexity: Advancing Neurobiological Insights from Invertebrates to Vertebrates through Evolutionary Perspectives.ACS chemical neuroscience · 2025Review
- ADVANCES IN HIGH-RESOLUTION MALDI MASS SPECTROMETRY FOR NEUROBIOLOGY.Mass spectrometry reviews · 2022Review
- Targeted Top-Down Mass Spectrometry for the Characterization and Tissue-Specific Functional Discovery of Crustacean Hyperglycemic Hormones (CHH) and CHH Precursor-Related Peptides in Response to Low pH Stress.Journal of the American Society for Mass Spectrometry · 2021Article
- Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry.RSC advances · 2018Review
- Article
- An Optimized Informatics Pipeline for Mass Spectrometry-Based Peptidomics.Journal of the American Society for Mass Spectrometry · 2015Article
- Peptidomics of Neuropeptidergic Tissues of the Tsetse Fly Glossina morsitans morsitans.Journal of the American Society for Mass Spectrometry · 2015Article
- In situ identification and mapping of neuropeptides from the stomatogastric nervous system of Cancer borealis.Rapid communications in mass spectrometry : RCM · 2014Article
- A multi-scale strategy for discovery of novel endogenous neuropeptides in the crustacean nervous system.Journal of proteomics · 2013Article
- High-definition de novo sequencing of crustacean hyperglycemic hormone (CHH)-family neuropeptides.Molecular & cellular proteomics : MCP · 2012Article
- Mass Spectrometry-based Proteomics and Peptidomics for Systems Biology and Biomarker Discovery.Frontiers in biology · 2012Article
- Discovery and characterization of the Crustacean hyperglycemic hormone precursor related peptides (CPRP) and orcokinin neuropeptides in the sinus glands of the blue crab Callinectes sapidus using multiple tandem mass spectrometry techniques.Journal of proteome research · 2011Article
- Crustacean neuropeptides.Cellular and molecular life sciences : CMLS · 2010Review
- Mass spectral imaging and profiling of neuropeptides at the organ and cellular domains.Analytical and bioanalytical chemistry · 2010Review
- Combining capillary electrophoresis matrix-assisted laser desorption/ionization mass spectrometry and stable isotopic labeling techniques for comparative crustacean peptidomics.Journal of chromatography. A · 2010Article
- Expanding the Crustacean neuropeptidome using a multifaceted mass spectrometric approach.Journal of proteome research · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The crustacean hyperglycemic hormone (CHH) is a 72-amino acid residue polypeptide with multiple physiological effects. The X-organ/sinus gland is the primary source for CHH and its family members. However, the amino acid sequence of CHH in Cancer borealis , a premier model system for neuromodulation, has not been characterized. In this study, a novel hybrid strategy combining "bottom-up" and "top-down" methodologies enabled direct sequencing of CHH peptide in the sinus gland of C. borealis . Multiple mass spectrometry (MS)-based techniques were employed to characterize the CHH peptide, including direct tissue analysis by MALDI-FT-ICR-MS, de novo sequencing of tryptic digested CHH by nano-LC/ESI-Q-TOF MS and intact CHH analysis by LC/FT-ICR-MS. In-trap cleaning removed the extensive matrix adducts of CHH in the direct tissue analysis by MALDI-FT-ICR-MS. Fragmentation efficiency of the intact CHH was drastically improved after the reduction-alkylation of the disulfide bonds. The sequence coverage was further enhanced by employing multiple complementary fragmentation techniques. Overall, this example is the largest neuropeptide de novo sequenced in C. borealis by mass spectrometric methods.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.