Krokhin O - Search Results

1

Accelerating Proteomics Using Broad Specificity Proteases.

Jiang X, Yeung D, Liu Y, Spicer V, Afshari H, Lao Y, Lin F, Krokhin O, Zahedi RP. Jiang X, et al. Among authors: krokhin o. J Proteome Res. 2024 Apr 5;23(4):1360-1369. doi: 10.1021/acs.jproteome.3c00852. Epub 2024 Mar 8. J Proteome Res. 2024. PMID: 38457694

2

Separation selectivity of anionic metal complexes of N,N'-bis(hydroxybenzyl)ethylenediamine-N,N'-diacetic acid in ion and ion electrokinetic chromatography.

Krokhin OV, Hoshino H, Shpigun OA, Yotsuyanagi T. Krokhin OV, et al. J Chromatogr A. 2000 Oct 20;895(1-2):255-61. doi: 10.1016/s0021-9673(00)00708-1. J Chromatogr A. 2000. PMID: 11105869

3

Predicting Electrophoretic Mobility of Tryptic Peptides for High-Throughput CZE-MS Analysis.

Krokhin OV, Anderson G, Spicer V, Sun L, Dovichi NJ. Krokhin OV, et al. Anal Chem. 2017 Feb 7;89(3):2000-2008. doi: 10.1021/acs.analchem.6b04544. Epub 2017 Jan 19. Anal Chem. 2017. PMID: 28208305 Free PMC article.

4

Peptide retention prediction in reversed-phase chromatography: proteomic applications.

Krokhin O. Krokhin O. Expert Rev Proteomics. 2012;9(1):1-4. doi: 10.1586/epr.11.79. Expert Rev Proteomics. 2012. PMID: 22292816 No abstract available.

5

Ion-chromatographic selectivity of polyelectrolyte sorbents based on some aliphatic and aromatic ionenes.

Pirogov AV, Krokhin OV, Platonov MM, Deryugina YI, Shpigun OA. Pirogov AV, et al. Among authors: krokhin ov. J Chromatogr A. 2000 Jul 7;884(1-2):31-9. doi: 10.1016/s0021-9673(00)00273-9. J Chromatogr A. 2000. PMID: 10917420

6

An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: its application to protein peptide mapping by off-line HPLC-MALDI MS.

Krokhin OV, Craig R, Spicer V, Ens W, Standing KG, Beavis RC, Wilkins JA. Krokhin OV, et al. Mol Cell Proteomics. 2004 Sep;3(9):908-19. doi: 10.1074/mcp.M400031-MCP200. Epub 2004 Jul 6. Mol Cell Proteomics. 2004. PMID: 15238601 Free article.

7

Use of peptide retention time prediction for protein identification by off-line reversed-phase HPLC-MALDI MS/MS.

Krokhin OV, Ying S, Cortens JP, Ghosh D, Spicer V, Ens W, Standing KG, Beavis RC, Wilkins JA. Krokhin OV, et al. Anal Chem. 2006 Sep 1;78(17):6265-9. doi: 10.1021/ac060251b. Anal Chem. 2006. PMID: 16944911

8

Formation of (bn-1 + H2O) ions by collisional activation of MALDI-formed peptide [M + H]+ ions in a QqTOF mass spectrometer.

She YM, Krokhin O, Spicer V, Loboda A, Garland G, Ens W, Standing KG, Westmore JB. She YM, et al. Among authors: krokhin o. J Am Soc Mass Spectrom. 2007 Jun;18(6):1024-37. doi: 10.1016/j.jasms.2007.02.008. Epub 2007 Apr 5. J Am Soc Mass Spectrom. 2007. PMID: 17418589 Free PMC article.

9

Assessment of the reproducibility of random hexapeptide peptide library-based protein normalization.

Dwivedi RC, Krokhin OV, Cortens JP, Wilkins JA. Dwivedi RC, et al. J Proteome Res. 2010 Feb 5;9(2):1144-9. doi: 10.1021/pr900608z. J Proteome Res. 2010. PMID: 20020779

10

Unifying expression scale for peptide hydrophobicity in proteomic reversed phase high-pressure liquid chromatography experiments.

Grigoryan M, Shamshurin D, Spicer V, Krokhin OV. Grigoryan M, et al. Anal Chem. 2013 Nov 19;85(22):10878-86. doi: 10.1021/ac402310t. Epub 2013 Nov 1. Anal Chem. 2013. PMID: 24127634

The standard peptide mixtures and tryptic digests of samples of different origins were separated under the identical chromatographic condition most commonly employed in proteomics: 100 A C18 sorbent with 0.1% formic acid as an ion-pairing modifier. Following our original approach …

The standard peptide mixtures and tryptic digests of samples of different origins were separated under the identical chromatographic conditi …

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