Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
By Hui Zhang, Xiao-Jun Li, Daniel B. Martin, R. Aebersold. Nature Biotechnology, 2003
1,338 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/b40869949cadf490831ed85e8d94509d2c5971e1
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- R. Aebersold
- John R. Yates III
- C. Ruse
- A. Nakorchevsky
- Paola Picotti
- Alexey I. Nesvizhskii
- B. Domon
- Steven A. Carr
In Oncology
In Spectroscopy
- R. Aebersold
- John R. Yates III
- C. Ruse
- A. Nakorchevsky
- Alexey I. Nesvizhskii
- B. Domon
- Paola Picotti
- Steven A. Carr
Citations in the corpus
- Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution*S (2007, background): “For example, capture of glycosylated proteins or peptides has been shown to greatly reduce plasma complexity and thereby enable detection of some lower abundance proteins (31–35), although recovery may be an issue as peptides from only 100 plasma proteins were detected in studies of serum (32, 33).”
- Selected reaction monitoring for quantitative proteomics: a tutorial (2008, methodology): “To be able to quantify low abundance proteins in plasma, peptides with Nlinked sugars were specifically enriched by solid phase capture ( Zhang et al, 2003; Stahl-Zeng et al, 2007).”
- Proteomics by mass spectrometry: approaches, advances, and applications. (2009, background): “N-linked glycosylated peptides are selectively bound to the solid support (121) and are subsequently enzymatically released.”