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Literature DB >> 12603129

A modular cross-linking approach for exploring protein interactions.

Michelle Trester-Zedlitz¹, Katsuhiko Kamada, Stephen K Burley, David Fenyö, Brian T Chait, Tom W Muir.

Abstract

A method is described for the elucidation of protein-protein interactions using novel cross-linking reagents and mass spectrometry. The method incorporates (1) a modular solid-phase synthetic strategy for generating the cross-linking reagents, (2) enrichment and digestion of cross-linked proteins using microconcentrators, (3) mass spectrometric analysis of cross-linked peptides, and (4) comprehensive computational analysis of the cross-linking data. This integrated approach has been applied to the study of cross-linking between the components of the heterodimeric protein complex negative cofactor 2.

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Year: 2003 PMID： 12603129 DOI： 10.1021/ja026917a

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

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Cited

57 in total

1. Mass spectrometric detection of affinity purified crosslinked peptides.

Authors: Gregory B Hurst; Trish K Lankford; Stephen J Kennel
Journal: J Am Soc Mass Spectrom Date: 2004-06 Impact factor: 3.109

2. Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

Authors: Feixia Chu; Shu-ou Shan; Demetri T Moustakas; Frank Alber; Pascal F Egea; Robert M Stroud; Peter Walter; Alma L Burlingame
Journal: Proc Natl Acad Sci U S A Date: 2004-11-16 Impact factor: 11.205

3. Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions.

Authors: Billy Clifford-Nunn; H D Hollis Showalter; Philip C Andrews
Journal: J Am Soc Mass Spectrom Date: 2011-12-01 Impact factor: 3.109

4. A negative ion mass spectrometry approach to identify cross-linked peptides utilizing characteristic disulfide fragmentations.

Authors: Antonio N Calabrese; Nikki J Good; Tianfang Wang; Jingjia He; John H Bowie; Tara L Pukala
Journal: J Am Soc Mass Spectrom Date: 2012-05-30 Impact factor: 3.109

10. Bifunctional cross-linking approaches for mass spectrometry-based investigation of nucleic acids and protein-nucleic acid assemblies.

Authors: M Scalabrin; S M Dixit; M M Makshood; C E Krzemien; Daniele Fabris
Journal: Methods Date: 2018-05-10 Impact factor: 3.608

A modular cross-linking approach for exploring protein interactions.

1. Mass spectrometric detection of affinity purified crosslinked peptides.

2. Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

3. Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions.

4. A negative ion mass spectrometry approach to identify cross-linked peptides utilizing characteristic disulfide fragmentations.

5. Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D.

6. Integrative structure modeling of macromolecular assemblies from proteomics data.

7. Photocleavable peptide-oligonucleotide conjugates for protein kinase assays by MALDI-TOF MS.

8. Chemistry of periodate-mediated cross-linking of 3,4-dihydroxylphenylalanine-containing molecules to proteins.

9. Probabilistic cross-link analysis and experiment planning for high-throughput elucidation of protein structure.

10. Bifunctional cross-linking approaches for mass spectrometry-based investigation of nucleic acids and protein-nucleic acid assemblies.