Reeder M. Robinson

522 total citations
21 papers, 415 citations indexed

About

Reeder M. Robinson is a scholar working on Molecular Biology, Pollution and Cell Biology. According to data from OpenAlex, Reeder M. Robinson has authored 21 papers receiving a total of 415 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 6 papers in Pollution and 5 papers in Cell Biology. Recurrent topics in Reeder M. Robinson's work include Amino Acid Enzymes and Metabolism (5 papers), Protein Degradation and Inhibitors (5 papers) and Endoplasmic Reticulum Stress and Disease (4 papers). Reeder M. Robinson is often cited by papers focused on Amino Acid Enzymes and Metabolism (5 papers), Protein Degradation and Inhibitors (5 papers) and Endoplasmic Reticulum Stress and Disease (4 papers). Reeder M. Robinson collaborates with scholars based in United States, Italy and Poland. Reeder M. Robinson's co-authors include Pablo Sobrado, Pedro Rodríguez, Nathan G. Dolloff, Leticia Reyes, Yefim Manevich, Somayesadat Badieyan, John J. Tanner, Brian G. Van Ness, Mieczysław Komarnicki and Julia S. Martín del Campo and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Reeder M. Robinson

20 papers receiving 412 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Reeder M. Robinson United States 12 259 70 63 62 52 21 415
Jun Yong Ha South Korea 12 351 1.4× 55 0.8× 13 0.2× 71 1.1× 27 0.5× 19 502
Hanna Tarhonskaya United Kingdom 13 344 1.3× 43 0.6× 29 0.5× 245 4.0× 13 0.3× 19 573
T.M. Leissing United Kingdom 10 400 1.5× 39 0.6× 15 0.2× 151 2.4× 17 0.3× 12 607
Ang Gao China 16 400 1.5× 26 0.4× 11 0.2× 97 1.6× 20 0.4× 42 756
Keith A. Koch United States 15 611 2.4× 11 0.2× 20 0.3× 39 0.6× 37 0.7× 21 908
Luc-Alain Savoy Switzerland 12 265 1.0× 9 0.1× 38 0.6× 50 0.8× 25 0.5× 17 563
Volker Seibert Germany 15 445 1.7× 12 0.2× 116 1.8× 36 0.6× 7 0.1× 17 630
Md. Saiful Islam United Kingdom 7 365 1.4× 32 0.5× 10 0.2× 116 1.9× 7 0.1× 16 495
Markus Ruetz United States 17 518 2.0× 43 0.6× 12 0.2× 5 0.1× 37 0.7× 40 670
Kevin P. McCusker United States 7 189 0.7× 15 0.2× 16 0.3× 86 1.4× 7 0.1× 10 345

Countries citing papers authored by Reeder M. Robinson

Since Specialization
Citations

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

Fields of papers citing papers by Reeder M. Robinson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Reeder M. Robinson. 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 Reeder M. Robinson. The network helps show where Reeder M. Robinson may publish in the future.

Co-authorship network of co-authors of Reeder M. Robinson

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

All Works

20 of 20 papers shown
1.
Robinson, Reeder M., et al.. (2022). PDI inhibitor LTI6426 enhances panobinostat efficacy in preclinical models of multiple myeloma. Cancer Chemotherapy and Pharmacology. 89(5). 643–653. 2 indexed citations
2.
Reyes, Leticia, Reeder M. Robinson, Sara A. Murphy, et al.. (2020). ATF3 Coordinates Antitumor Synergy between Epigenetic Drugs and Protein Disulfide Isomerase Inhibitors. Cancer Research. 80(16). 3279–3291. 22 indexed citations
3.
Robinson, Reeder M., et al.. (2020). Structural Determinants of Flavin Dynamics in a Class B Monooxygenase. Biochemistry. 59(48). 4609–4616. 8 indexed citations
4.
Robinson, Reeder M., et al.. (2019). Abstract 3863: Specifically targeting PDIA1 with indene inhibitors leads to bortezomib-potentiation in multiple myeloma. Cancer Research. 79(13_Supplement). 3863–3863. 1 indexed citations
5.
Robinson, Reeder M., et al.. (2019). Tuning isoform selectivity and bortezomib sensitivity with a new class of alkenyl indene PDI inhibitor. European Journal of Medicinal Chemistry. 186. 111906–111906. 16 indexed citations
6.
Robinson, Reeder M., et al.. (2019). Syrbactin proteasome inhibitor TIR-199 overcomes bortezomib chemoresistance and inhibits multiple myeloma tumor growth in vivo. Leukemia Research. 88. 106271–106271. 11 indexed citations
7.
Robinson, Reeder M., Leticia Reyes, Allen B. Reitz, et al.. (2018). Inhibitors of the protein disulfide isomerase family for the treatment of multiple myeloma. Leukemia. 33(4). 1011–1022. 42 indexed citations
8.
Robinson, Reeder M., et al.. (2018). Flavin oxidation in flavin‐dependent N‐monooxygenases. Protein Science. 28(1). 90–99. 9 indexed citations
9.
Dytfeld, Dominik, Leticia Reyes, Reeder M. Robinson, et al.. (2017). Glutaminase inhibitor CB-839 synergizes with carfilzomib in resistant multiple myeloma cells. Oncotarget. 8(22). 35863–35876. 102 indexed citations
10.
Robinson, Reeder M., et al.. (2016). Identification of structural determinants of NAD(P)H selectivity and lysine binding in lysine N-monooxygenase. Archives of Biochemistry and Biophysics. 606. 180–188. 5 indexed citations
11.
Robinson, Reeder M., et al.. (2015). Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Archives of Biochemistry and Biophysics. 585. 25–31. 13 indexed citations
12.
Binda, Claudia, Reeder M. Robinson, Julia S. Martín del Campo, et al.. (2015). An Unprecedented NADPH Domain Conformation in Lysine Monooxygenase NbtG Provides Insights into Uncoupling of Oxygen Consumption from Substrate Hydroxylation. Journal of Biological Chemistry. 290(20). 12676–12688. 43 indexed citations
13.
Robinson, Reeder M., S. Franceschini, Pedro Rodríguez, et al.. (2014). Arg279 is the key regulator of coenzyme selectivity in the flavin-dependent ornithine monooxygenase SidA. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(4). 778–784. 17 indexed citations
14.
Robinson, Reeder M., Pedro Rodríguez, & Pablo Sobrado. (2014). Mechanistic studies on the flavin-dependent N6-lysine monooxygenase MbsG reveal an unusual control for catalysis. Archives of Biochemistry and Biophysics. 550-551. 58–66. 24 indexed citations
15.
Robinson, Reeder M., et al.. (2013). Tryptophan-47 in the active site of Methylophaga sp. strain SK1 flavin-monooxygenase is important for hydride transfer. Archives of Biochemistry and Biophysics. 532(1). 46–53. 4 indexed citations
16.
Robinson, Reeder M., Somayesadat Badieyan, & Pablo Sobrado. (2013). C4a-Hydroperoxyflavin Formation in N-Hydroxylating Flavin Monooxygenases Is Mediated by the 2′-OH of the Nicotinamide Ribose of NADP+. Biochemistry. 52(51). 9089–9091. 26 indexed citations
17.
Singh, Harkewal, et al.. (2012). Identification of the NAD(P)H Binding Site of Eukaryotic UDP-Galactopyranose Mutase. Journal of the American Chemical Society. 134(43). 18132–18138. 24 indexed citations
18.
Romero, Elvira, Reeder M. Robinson, & Pablo Sobrado. (2012). Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry. Journal of Visualized Experiments. 11 indexed citations
19.
Qi, Jun, et al.. (2012). A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases. Analytical Biochemistry. 425(1). 80–87. 13 indexed citations

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