The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Discovering new invertebrate neuropeptides using mass spectrometry
Abstract
Neuropeptides are a complex set of messenger molecules controlling a wide array of regulatory functions and behaviors within an organism. These neuromodulators are cleaved from longer protein molecules and often experience numerous post‐translational modifications to achieve their bioactive form. As a result of this complexity, sensitive and versatile analysis schemes are needed to characterize neuropeptides. Mass spectrometry (MS) through a variety of approaches has fueled the discovery of hundreds of neuropeptides in invertebrate species in the last decade. Particularly successful are direct tissue and single neuron analyses by matrix‐assisted laser desorption/ionization (MALDI) MS, which has been used to elucidate approximately 440 neuropeptides, and examination of neuronal homogenates by electrospray ionization techniques (ESI), also leading to the characterization of over 450 peptides. Additional MS methods with great promise for the discovery of neuropeptides are MS imaging and large‐scale peptidomics studies in combination with a sequenced genome. © 2005 Wiley Periodicals, Inc.
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Cites
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
Caprioli, R. M., Farmer, T. B., & Gile, J. (1997) · Analytical Chemistry · doi:10.1021/ac970888i · Cited by 2,234
Cited by
The neuropeptide complement of the marine annelid Platynereis dumerilii
Conzelmann, M., Williams, E. A., Krug, K., Franz-Wachtel, M., Macek, B., & Jékely, G. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-906 · Cited by 165
Metadata
- Authors
- Hummon, A. B., Amare, A., & Sweedler, J. V.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2005-06-03
- Volume
- 25
- Issue
- 1
- Pages
- 77-98
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W2033340247
- Cited by
- 158
- References
- 1
- FWCI
- 7.37
- Type
- journal article
- Language
- en
- Open access
- closed
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