Michael J. Treuheit

3.2k total citations
58 papers, 2.6k citations indexed

About

Michael J. Treuheit is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Spectroscopy. According to data from OpenAlex, Michael J. Treuheit has authored 58 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Molecular Biology, 25 papers in Radiology, Nuclear Medicine and Imaging and 15 papers in Spectroscopy. Recurrent topics in Michael J. Treuheit's work include Protein purification and stability (29 papers), Monoclonal and Polyclonal Antibodies Research (25 papers) and Glycosylation and Glycoproteins Research (17 papers). Michael J. Treuheit is often cited by papers focused on Protein purification and stability (29 papers), Monoclonal and Polyclonal Antibodies Research (25 papers) and Glycosylation and Glycoproteins Research (17 papers). Michael J. Treuheit collaborates with scholars based in United States and France. Michael J. Treuheit's co-authors include David N. Brems, Pavel V. Bondarenko, Gary D. Pipes, Himanshu S. Gadgil, Olaf Kinstler, Andrew A. Kosky, Catherine E. Costello, H.B. Halsall, Da Ren and Graham Molineux and has published in prestigious journals such as Journal of Biological Chemistry, Analytical Chemistry and The Journal of Physical Chemistry B.

In The Last Decade

Michael J. Treuheit

57 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Michael J. Treuheit United States	27	1.9k	1.0k	457	304	265	58	2.6k
Yasuro Shinohara Japan	33	2.8k 1.4×	540 0.5×	443 1.0×	563 1.9×	135 0.5×	87	3.4k
Giorgio Fassina Italy	30	1.6k 0.8×	933 0.9×	103 0.2×	418 1.4×	258 1.0×	117	2.7k
Jun‐ichi Furukawa Japan	28	2.4k 1.2×	347 0.3×	365 0.8×	419 1.4×	124 0.5×	115	2.9k
Robert Bayer United States	20	1.8k 0.9×	894 0.9×	106 0.2×	447 1.5×	150 0.6×	25	2.5k
Hiroaki Nakagawa Japan	31	1.9k 1.0×	432 0.4×	579 1.3×	390 1.3×	106 0.4×	98	2.5k
Pavel V. Bondarenko United States	34	3.5k 1.8×	2.2k 2.2×	1.4k 3.0×	504 1.7×	248 0.9×	74	4.2k
Mark Castanares United States	17	1.0k 0.5×	421 0.4×	139 0.3×	228 0.8×	291 1.1×	31	1.7k
Sampathkumar Krishnan United States	17	2.0k 1.0×	879 0.9×	135 0.3×	154 0.5×	59 0.2×	18	2.5k
Quentin Baca United States	10	1.2k 0.6×	325 0.3×	92 0.2×	225 0.7×	140 0.5×	12	2.0k
Zahra Shahrokh United States	15	2.6k 1.4×	492 0.5×	123 0.3×	730 2.4×	565 2.1×	26	3.2k

Countries citing papers authored by Michael J. Treuheit

Since Specialization

Citations

This map shows the geographic impact of Michael J. Treuheit'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 Michael J. Treuheit with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Michael J. Treuheit more than expected).

Fields of papers citing papers by Michael J. Treuheit

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michael J. Treuheit. 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 Michael J. Treuheit. The network helps show where Michael J. Treuheit may publish in the future.

Co-authorship network of co-authors of Michael J. Treuheit

This figure shows the co-authorship network connecting the top 25 collaborators of Michael J. Treuheit. A scholar is included among the top collaborators of Michael J. Treuheit 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 Michael J. Treuheit. Michael J. Treuheit 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

Xu, Amy Y., Nicholas Clark, Hyojin Kim, et al.. (2022). Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations. Antibodies. 11(2). 24–24. 11 indexed citations

Razinkov, Vladimir I., Michael J. Treuheit, & Gerald W. Becker. (2015). Accelerated Formulation Development of Monoclonal Antibodies (mAbs) and mAb-Based Modalities: Review of Methods and Tools. SLAS DISCOVERY. 20(4). 468–483. 56 indexed citations

Zhang, Jun, Douglas D. Banks, Feng He, Michael J. Treuheit, & Gerald W. Becker. (2015). Effects of Sucrose and Benzyl Alcohol on GCSF Conformational Dynamics Revealed by Hydrogen Deuterium Exchange Mass Spectrometry. Journal of Pharmaceutical Sciences. 104(5). 1592–1600. 17 indexed citations

Su, Cheng, et al.. (2014). High-Throughput Screening and Stability Optimization of Anti-Streptavidin IgG1 and IgG2 Formulations. SLAS DISCOVERY. 19(9). 1290–1301. 17 indexed citations

Treuheit, Michael J., et al.. (2014). Optimized UV Detection of High-Concentration Antibody Formulations using High-Throughput SE-HPLC. Journal of Pharmaceutical Sciences. 104(2). 508–514. 6 indexed citations

Miller, Amanda, David M. Hambly, Bruce A. Kerwin, Michael J. Treuheit, & Himanshu S. Gadgil. (2011). Characterization of Site-Specific Glycation During Process Development of a Human Therapeutic Monoclonal Antibody. Journal of Pharmaceutical Sciences. 100(7). 2543–2550. 66 indexed citations

Valliere‐Douglass, John, Catherine M. Eakin, Mirna Mujacic, et al.. (2010). Asparagine Linked Oligosaccharides Present on a Non‐Consensus Amino Acid Sequence in the CH1 Domain of Human Antibodies. The FASEB Journal. 24(S1).

Valliere‐Douglass, John, Catherine M. Eakin, Alison Wallace, et al.. (2010). Glutamine-linked and Non-consensus Asparagine-linked Oligosaccharides Present in Human Recombinant Antibodies Define Novel Protein Glycosylation Motifs. Journal of Biological Chemistry. 285(21). 16012–16022. 71 indexed citations

Ren, Da, Gary D. Pipes, Dingjiang Liu, et al.. (2009). An improved trypsin digestion method minimizes digestion-induced modifications on proteins. Analytical Biochemistry. 392(1). 12–21. 154 indexed citations

10.

Ren, Da, Gayathri Ratnaswamy, Jill Beierle, et al.. (2008). Degradation products analysis of an Fc fusion protein using LC/MS methods. International Journal of Biological Macromolecules. 44(1). 81–85. 11 indexed citations

11.

Gadgil, Himanshu S., Gary D. Pipes, Thomas M. Dillon, Michael J. Treuheit, & Pavel V. Bondarenko. (2006). Improving mass accuracy of high performance liquid chromatography/electrospray ionization time-of-flight mass spectrometry of intact antibodies. Journal of the American Society for Mass Spectrometry. 17(6). 867–872. 65 indexed citations

12.

Rajan, Rahul S., Tiansheng Li, Mohini Aras, et al.. (2006). Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study. Protein Science. 15(5). 1063–1075. 95 indexed citations

13.

Pipes, Gary D., et al.. (2005). Optimization and Applications of CDAP Labeling for the Assignment of Cysteines. Pharmaceutical Research. 22(7). 1059–1068. 23 indexed citations

14.

Treuheit, Michael J., Andrew A. Kosky, & David N. Brems. (2002). Inverse Relationship of Protein Concentration and Aggregation. Pharmaceutical Research. 19(4). 511–516. 154 indexed citations

15.

Kosky, Andrew A., et al.. (1998). PEGylation Prevents the N-Terminal Degradation of Megakaryocyte Growth and Development Factor. Pharmaceutical Research. 15(12). 1822–1827. 20 indexed citations

16.

Lauren, Scott L. & Michael J. Treuheit. (1998). Removal of the fluorescent 4-(aminosulfonyl)-2,1,3-benzoxadiazole label from cysteine-containing peptides. Journal of Chromatography A. 798(1-2). 47–54. 3 indexed citations

17.

Litzinger, David C., et al.. (1995). A method for preparing chelate-cytokine conjugates with retention of protein structure, biological activity, and pharmacokinetic properties. Journal of Immunological Methods. 187(1). 151–161. 6 indexed citations

18.

Treuheit, Michael J., et al.. (1995). Site-Specific Conjugation of Diethylenetriaminepentaacetic Acid to Recombinant Human Granulocyte-Colony-Stimulating Factor: Preservation of Protein Structure and Function. Biochemistry. 34(14). 4889–4897. 4 indexed citations

19.

Pedemonte, Carlos H., Terence L. Kirley, Michael J. Treuheit, & Jack H. Kaplan. (1992). Inactivation of the Na,K‐ATPase by modification of Lys‐501 with 4‐acetamido‐4′‐isothiocyanatostilbene‐2,2′‐disulfonic acid (SITS). FEBS Letters. 314(1). 97–100. 11 indexed citations

20.

Treuheit, Michael J. & H. Brian Halsall. (1992). Isolation of clobazam–orosomucoid complexes from Patients' sera. Biomedical Chromatography. 6(1). 50–52. 6 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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