John A. Newitt

2.1k total citations · 1 hit paper
25 papers, 1.5k citations indexed

About

John A. Newitt is a scholar working on Molecular Biology, Organic Chemistry and Genetics. According to data from OpenAlex, John A. Newitt has authored 25 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 6 papers in Organic Chemistry and 5 papers in Genetics. Recurrent topics in John A. Newitt's work include Melanoma and MAPK Pathways (6 papers), Bacterial Genetics and Biotechnology (4 papers) and Synthesis and biological activity (3 papers). John A. Newitt is often cited by papers focused on Melanoma and MAPK Pathways (6 papers), Bacterial Genetics and Biotechnology (4 papers) and Synthesis and biological activity (3 papers). John A. Newitt collaborates with scholars based in United States, Germany and India. John A. Newitt's co-authors include Nancy D. Ulbrandt, Harris Bernstein, Susan E. Kiefer, Harris D. Bernstein, Kevin Kish, Dianlin Xie, Louis J. Lombardo, John S. Tokarski, Herbert E. Klei and Yaqun Zhang and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

John A. Newitt

25 papers receiving 1.5k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

The Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain Elucidates Its Inhibitory Activity against Imatinib-Resistant ABL Mutants

2006 522 citations John S. Tokarski, John A. Newitt et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John A. Newitt United States	16	790	406	342	286	207	25	1.5k
Hiroshi Takemoto Japan	24	1.1k 1.4×	99 0.2×	144 0.4×	89 0.3×	364 1.8×	65	1.7k
Bárbara Guerra Denmark	28	2.0k 2.6×	72 0.2×	150 0.4×	142 0.5×	168 0.8×	76	2.7k
Stefan Dove Germany	30	1.5k 1.9×	94 0.2×	92 0.3×	73 0.3×	373 1.8×	75	2.1k
Sharon Sweitzer United States	17	1.1k 1.4×	49 0.1×	172 0.5×	83 0.3×	31 0.1×	20	2.1k
Greet Vanhoof Belgium	23	964 1.2×	134 0.3×	70 0.2×	62 0.2×	172 0.8×	54	1.8k
Choel Kim United States	27	2.0k 2.6×	89 0.2×	238 0.7×	28 0.1×	177 0.9×	56	2.6k
Cecilia Chiu United States	16	1.1k 1.4×	45 0.1×	255 0.7×	51 0.2×	309 1.5×	19	1.7k
Anna Rodina United States	20	1.6k 2.1×	91 0.2×	52 0.2×	117 0.4×	83 0.4×	32	2.1k
Rohinton Edalji United States	24	1.1k 1.4×	114 0.3×	58 0.2×	336 1.2×	92 0.4×	41	1.8k
Hans‐Dieter Pohlenz Germany	19	817 1.0×	41 0.1×	112 0.3×	62 0.2×	45 0.2×	29	1.3k

Countries citing papers authored by John A. Newitt

Since Specialization

Citations

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

Fields of papers citing papers by John A. Newitt

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John A. Newitt. 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 John A. Newitt. The network helps show where John A. Newitt may publish in the future.

Co-authorship network of co-authors of John A. Newitt

This figure shows the co-authorship network connecting the top 25 collaborators of John A. Newitt. A scholar is included among the top collaborators of John A. Newitt 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 John A. Newitt. John A. Newitt is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Xie, Tao, Max Ruzanov, David Critton, et al.. (2025). Orthosteric STING inhibition elucidates molecular correction of SAVI STING. Nature Communications. 16(1). 5695–5695. 2 indexed citations

Velaparthi, Upender, Mark G. Saulnier, David B. Frennesson, et al.. (2022). The discovery of BMS-737 as a potent, CYP17 lyase-selective inhibitor for the treatment of castration-resistant prostate cancer. Bioorganic & Medicinal Chemistry Letters. 75. 128951–128951. 7 indexed citations

Wagner, Nicole D., Jing Yan, Jing Li, et al.. (2021). Native mass spectrometry and gas-phase fragmentation provide rapid and in-depth topological characterization of a PROTAC ternary complex. Cell chemical biology. 28(10). 1528–1538.e4. 20 indexed citations

Lau, Wai Leung, Bradley C. Pearce, Dianlin Xie, et al.. (2020). Using yeast surface display to engineer a soluble and crystallizable construct of hematopoietic progenitor kinase 1 (HPK1). Acta Crystallographica Section F Structural Biology Communications. 77(1). 22–28. 11 indexed citations

Nelp, Micah T., John T. Hunt, John A. Newitt, et al.. (2018). Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form. Proceedings of the National Academy of Sciences. 115(13). 3249–3254. 140 indexed citations

Sack, John S., Mian Gao, Susan E. Kiefer, et al.. (2016). Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor. Acta Crystallographica Section F Structural Biology Communications. 72(2). 129–134. 47 indexed citations

Tebben, Andrew J., Mian Gao, Dianlin Xie, et al.. (2016). Crystal structures of apo and inhibitor-bound TGFβR2 kinase domain: insights into TGFβR isoform selectivity. Acta Crystallographica Section D Structural Biology. 72(5). 658–674. 22 indexed citations

Sivaprakasam, Prasanna, Xiaojun Han, Rita L. Civiello, et al.. (2015). Discovery of new acylaminopyridines as GSK-3 inhibitors by a structure guided in-depth exploration of chemical space around a pyrrolopyridinone core. Bioorganic & Medicinal Chemistry Letters. 25(9). 1856–1863. 100 indexed citations

Yamniuk, Aaron P., John A. Newitt, Michael L. Doyle, et al.. (2015). Development of a Model Protein Interaction Pair as a Benchmarking Tool for the Quantitative Analysis of 2-Site Protein-Protein Interactions. Journal of Biomolecular Techniques JBT. 26(4). 125–141. 3 indexed citations

10.

Ni, Yan G., Xiling Yuan, John A. Newitt, et al.. (2015). Development and Fit-for-Purpose Validation of a Soluble Human Programmed Death-1 Protein Assay. The AAPS Journal. 17(4). 976–987. 9 indexed citations

11.

Wrobleski, Stephen T., Shuqun Lin, T. G. Murali Dhar, et al.. (2013). The identification of novel p38α isoform selective kinase inhibitors having an unprecedented p38α binding mode. Bioorganic & Medicinal Chemistry Letters. 23(14). 4120–4126. 15 indexed citations

12.

Dyckman, Alaric J., Tianle Li, Sidney Pitt, et al.. (2011). Discovery of pyrrolo[2,1-f][1,2,4]triazine C6-ketones as potent, orally active p38α MAP kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 21(15). 4633–4637. 9 indexed citations

13.

Sack, John S., Kevin Kish, Matthew Pokross, et al.. (2008). Structural basis for the high-affinity binding of pyrrolotriazine inhibitors of p38 MAP kinase. Acta Crystallographica Section D Biological Crystallography. 64(7). 705–710. 10 indexed citations

14.

Constantine, Keith L., Luciano Mueller, William J. Metzler, et al.. (2008). Multiple and Single Binding Modes of Fragment-Like Kinase Inhibitors Revealed by Molecular Modeling, Residue Type-Selective Protonation, and Nuclear Overhauser Effects. Journal of Medicinal Chemistry. 51(19). 6225–6229. 11 indexed citations

15.

Tarby, Christine M., Robert F. Kaltenbach, Tram Huynh, et al.. (2006). Inhibitors of human mitotic kinesin Eg5: Characterization of the 4-phenyl-tetrahydroisoquinoline lead series. Bioorganic & Medicinal Chemistry Letters. 16(8). 2095–2100. 36 indexed citations

16.

Tokarski, John S., John A. Newitt, Francis Y. Lee, et al.. (2004). The Crystal Structure of Abl Kinase with BMS-354825, a Dual SRC/ABL Kinase Inhibitor.. Blood. 104(11). 553–553. 21 indexed citations

17.

Newitt, John A., Nancy D. Ulbrandt, & Harris D. Bernstein. (1999). The Structure of Multiple Polypeptide Domains Determines the Signal Recognition Particle Targeting Requirement of Escherichia coli Inner Membrane Proteins. Journal of Bacteriology. 181(15). 4561–4567. 24 indexed citations

18.

Newitt, John A. & Harris D. Bernstein. (1998). A Mutation in the Escherichia coli secY Gene That Produces Distinct Effects on Inner Membrane Protein Insertion and Protein Export. Journal of Biological Chemistry. 273(20). 12451–12456. 46 indexed citations

19.

Ulbrandt, Nancy D., John A. Newitt, & Harris Bernstein. (1997). The E. coli Signal Recognition Particle Is Required for the Insertion of a Subset of Inner Membrane Proteins. Cell. 88(2). 187–196. 293 indexed citations

20.

Newitt, John A. & Harris D. Bernstein. (1997). The N‐Domain of the Signal Recognition Particle 54‐kDa Subunit Promotes Efficient Signal Sequence Binding. European Journal of Biochemistry. 245(3). 720–729. 43 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.

Explore authors with similar magnitude of impact