Mark S. Bolgar

1.3k total citations
47 papers, 1.1k citations indexed

About

Mark S. Bolgar is a scholar working on Molecular Biology, Spectroscopy and Pharmacology. According to data from OpenAlex, Mark S. Bolgar has authored 47 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 20 papers in Spectroscopy and 5 papers in Pharmacology. Recurrent topics in Mark S. Bolgar's work include Analytical Chemistry and Chromatography (19 papers), Mass Spectrometry Techniques and Applications (15 papers) and Protein purification and stability (13 papers). Mark S. Bolgar is often cited by papers focused on Analytical Chemistry and Chromatography (19 papers), Mass Spectrometry Techniques and Applications (15 papers) and Protein purification and stability (13 papers). Mark S. Bolgar collaborates with scholars based in United States, Germany and United Kingdom. Mark S. Bolgar's co-authors include Simon J. Gaskell, Jon Norman, Adrienne A. Tymiak, Scott Summerfield, Athula B. Attygalle, Gerald C. DiDonato, Lee‐Chiang Lo, E Haber, Nina Berova and W. Parker and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Analytical Chemistry.

In The Last Decade

Mark S. Bolgar

46 papers receiving 1.0k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Mark S. Bolgar United States	17	503	283	107	102	100	47	1.1k
Natália Romero Spain	17	607 1.2×	188 0.7×	86 0.8×	77 0.8×	97 1.0×	40	1.5k
Anja Pfenninger Germany	21	938 1.9×	489 1.7×	129 1.2×	181 1.8×	94 0.9×	30	1.7k
Nadezhda A. Galeva United States	22	812 1.6×	176 0.6×	149 1.4×	57 0.6×	55 0.6×	42	1.4k
Catalin E. Doneanu United States	24	945 1.9×	312 1.1×	95 0.9×	27 0.3×	104 1.0×	46	1.5k
Sergey Reverdatto United States	19	885 1.8×	97 0.3×	75 0.7×	60 0.6×	47 0.5×	31	1.6k
Rodolfo M. Rasia Argentina	21	758 1.5×	147 0.5×	45 0.4×	96 0.9×	46 0.5×	56	1.8k
Oh‐Seung Kwon South Korea	21	590 1.2×	169 0.6×	44 0.4×	75 0.7×	73 0.7×	105	1.5k
Katsutoshi Takahashi Japan	26	1.0k 2.0×	314 1.1×	258 2.4×	78 0.8×	80 0.8×	77	2.2k
Harri Koskela Finland	17	334 0.7×	187 0.7×	93 0.9×	50 0.5×	84 0.8×	36	930
Eleonora Corradini Netherlands	13	589 1.2×	294 1.0×	41 0.4×	29 0.3×	56 0.6×	18	964

Countries citing papers authored by Mark S. Bolgar

Since Specialization

Citations

This map shows the geographic impact of Mark S. Bolgar's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Mark S. Bolgar with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Mark S. Bolgar more than expected).

Fields of papers citing papers by Mark S. Bolgar

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mark S. Bolgar. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Mark S. Bolgar. The network helps show where Mark S. Bolgar may publish in the future.

Co-authorship network of co-authors of Mark S. Bolgar

This figure shows the co-authorship network connecting the top 25 collaborators of Mark S. Bolgar. A scholar is included among the top collaborators of Mark S. Bolgar based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Mark S. Bolgar. Mark S. Bolgar is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Bolgar, Mark S., et al.. (2020). Hybrid mode of hydrophobic interaction chromatography of monoclonal antibodies and related biomolecules: Influence of elution conditions on chromatographic performance using poly (alkyl aspartamide) silica columns. Journal of Chromatography B. 1140. 121984–121984.

Whitaker, Neal, Duohai Pan, Zhihua Liu, et al.. (2020). Impact of Polysorbate 80 Grade on the Interfacial Properties and Interfacial Stress Induced Subvisible Particle Formation in Monoclonal Antibodies. Journal of Pharmaceutical Sciences. 110(2). 746–759. 25 indexed citations

Qiu, Difei, et al.. (2018). Comparison of imaged capillary isoelectric focusing and cation exchange chromatography for monitoring dextrose-mediated glycation of monoclonal antibodies in infusion solutions. Journal of Chromatography B. 1105. 156–163. 12 indexed citations

Xu, Meng, et al.. (2018). Pulse Proteolysis: An Orthogonal Tool for Protein Formulation Screening. Journal of Pharmaceutical Sciences. 108(2). 842–850. 2 indexed citations

Rinaldi, Frank, et al.. (2017). Identification of leachables observed in the size exclusion chromatograms of a low concentration product stored in prefilled syringes. Journal of Pharmaceutical and Biomedical Analysis. 139. 133–142. 15 indexed citations

Lin, Shujie, et al.. (2017). Enablement of the direct analysis of excipients in monoclonal antibody formulations through the incorporation of a wide pore C18 protein trap with hydrophilic interaction liquid chromatography. Journal of Chromatography B. 1068-1069. 131–135. 5 indexed citations

Huang, Yande, et al.. (2015). Trace level liquid chromatography tandem mass spectrometry quantification of the mutagenic impurity 2-hydroxypyridine N-oxide as its dansyl derivative. Journal of Chromatography A. 1386. 47–52. 9 indexed citations

Huang, Yande, Bao‐Ning Su, Qingmei Ye, et al.. (2013). Improving the efficiency of quantitative 1H NMR: An innovative external standard–internal reference approach. Journal of Pharmaceutical and Biomedical Analysis. 88. 1–6. 17 indexed citations

Bolgar, Mark S., et al.. (2012). Separation and detection of bis-maleimide-polyethylene glycol and mono-maleimide-polyethylene glycol by reversed-phase high pressure liquid chromatography. Journal of Chromatography A. 1246. 117–122. 10 indexed citations

10.

Pathirana, Charles, Yande Huang, Mark S. Bolgar, et al.. (2012). Identification of amino acid derivatives as condensation products between glyceraldehyde and guanine nucleoside. Tetrahedron Letters. 54(2). 132–133. 1 indexed citations

11.

Lu, Xujin, et al.. (2011). Development of a two-step tier-2 dissolution method for blinded overencapsulated erlotinib tablets using UV fiber optic detection. Journal of Pharmaceutical and Biomedical Analysis. 56(1). 23–29. 5 indexed citations

12.

Axe, Frank U., et al.. (2010). Reactivity of gaseous sodiated ions derived from benzene dicarboxylate salts toward residual water in the collision gas. Journal of Mass Spectrometry. 45(10). 1130–1138. 16 indexed citations

13.

Bolgar, Mark S., et al.. (2010). Evading metal adduct formation during desorption‐ionization mass spectrometry. Rapid Communications in Mass Spectrometry. 24(19). 2838–2842. 7 indexed citations

14.

Wang, Jian, Mark S. Bolgar, Huidong Gu, et al.. (2010). Effect of mobile phase pH, aqueous‐organic ratio, and buffer concentration on electrospray ionization tandem mass spectrometric fragmentation patterns: implications in liquid chromatography/tandem mass spectrometric bioanalysis. Rapid Communications in Mass Spectrometry. 24(22). 3221–3229. 33 indexed citations

15.

Hunt, John T., et al.. (2009). Control of peptide disulfide regioisomer formation by mixed cysteine-penicillamine bridges. International journal of peptide & protein research. 42(3). 249–258. 8 indexed citations

16.

Desai, D., et al.. (2007). Stability of low concentrations of guanine-based antivirals in sucrose or maltitol solutions. International Journal of Pharmaceutics. 342(1-2). 87–94. 10 indexed citations

17.

Robertson, Duncan H. L., Jane L. Hurst, Mark S. Bolgar, Simon J. Gaskell, & Robert J. Beynon. (1997). Molecular Heterogeneity of Urinary Proteins in Wild House Mouse Populations. Rapid Communications in Mass Spectrometry. 11(7). 786–790. 45 indexed citations

18.

Zein, Nada, Paul D. Reiss, Michael S. Bernatowicz, & Mark S. Bolgar. (1995). The proteolytic specificity of the natural enediyne-containing chromoproteins is unique to each chromoprotein. Chemistry & Biology. 2(7). 451–455. 34 indexed citations

19.

Tymiak, Adrienne A., et al.. (1992). Dactylocyclines, novel tetracycline derivatives produced by a Dactylosporangium sp. II. Structure elucidation.. The Journal of Antibiotics. 45(12). 1899–1906. 12 indexed citations

20.

Norman, Jon, et al.. (1991). Degradation of brain natriuretic peptide by neutral endopeptidase: Species specific sites of proteolysis determined by mass spectrometry. Biochemical and Biophysical Research Communications. 175(1). 22–30. 63 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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