Mischa Machius

8.2k total citations
90 papers, 6.6k citations indexed

About

Mischa Machius is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Mischa Machius has authored 90 papers receiving a total of 6.6k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 21 papers in Cell Biology and 15 papers in Materials Chemistry. Recurrent topics in Mischa Machius's work include Enzyme Structure and Function (15 papers), Protein Structure and Dynamics (11 papers) and Cellular transport and secretion (11 papers). Mischa Machius is often cited by papers focused on Enzyme Structure and Function (15 papers), Protein Structure and Dynamics (11 papers) and Cellular transport and secretion (11 papers). Mischa Machius collaborates with scholars based in United States, Germany and France. Mischa Machius's co-authors include Diana R. Tomchick, Georg Wiegand, Robert Huber, Chad A. Brautigam, Josep Rizo, Nathalie Declerck, Hongtao Yu, Maojun Yang, Michael K. Rosen and Chinatsu Otomo and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Mischa Machius

89 papers receiving 6.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mischa Machius United States 47 4.4k 1.6k 815 814 695 90 6.6k
D.A.R. Sanders Canada 29 5.4k 1.2× 1.5k 0.9× 259 0.3× 582 0.7× 843 1.2× 89 7.1k
Flavio Meggio Italy 50 6.9k 1.6× 1.1k 0.7× 545 0.7× 887 1.1× 643 0.9× 141 8.7k
Elizabeth J. Goldsmith United States 50 9.8k 2.2× 1.5k 0.9× 331 0.4× 575 0.7× 926 1.3× 108 12.7k
Katalin F. Medzihradszky United States 57 6.7k 1.5× 974 0.6× 220 0.3× 1.1k 1.3× 338 0.5× 188 9.9k
Mick F. Tuite United Kingdom 54 9.4k 2.1× 1.2k 0.7× 314 0.4× 911 1.1× 675 1.0× 196 10.7k
Urszula Derewenda United States 42 4.9k 1.1× 872 0.5× 396 0.5× 239 0.3× 917 1.3× 81 6.5k
Mark J. Zoller United States 40 7.2k 1.6× 1.1k 0.7× 280 0.3× 644 0.8× 741 1.1× 54 10.1k
Claude Cochet France 50 5.8k 1.3× 1.0k 0.6× 327 0.4× 404 0.5× 438 0.6× 191 8.1k
A.S. Arvai United States 43 5.5k 1.3× 634 0.4× 229 0.3× 1.2k 1.5× 670 1.0× 61 7.8k
Marco Nardini Italy 37 3.4k 0.8× 1.4k 0.9× 192 0.2× 483 0.6× 357 0.5× 118 4.9k

Countries citing papers authored by Mischa Machius

Since Specialization
Citations

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

Fields of papers citing papers by Mischa Machius

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mischa Machius. 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 Mischa Machius. The network helps show where Mischa Machius may publish in the future.

Co-authorship network of co-authors of Mischa Machius

This figure shows the co-authorship network connecting the top 25 collaborators of Mischa Machius. A scholar is included among the top collaborators of Mischa Machius 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 Mischa Machius. Mischa Machius 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.
Venkannagari, Harikanth, James M. Kasper, Anurag Misra, et al.. (2020). Highly Conserved Molecular Features in IgLONs Contrast Their Distinct Structural and Biological Outcomes. Journal of Molecular Biology. 432(19). 5287–5303. 14 indexed citations
2.
Zhou, Yin, Harikanth Venkannagari, Galina V. Aglyamova, et al.. (2019). Self-assembly of the bZIP transcription factor ΔFosB. SHILAP Revista de lepidopterología. 2. 1–13. 7 indexed citations
3.
Zhang, Weihe, Dehui� Zhang, Michael A. Stashko, et al.. (2013). Pseudo-Cyclization through Intramolecular Hydrogen Bond Enables Discovery of Pyridine Substituted Pyrimidines as New Mer Kinase Inhibitors. Journal of Medicinal Chemistry. 56(23). 9683–9692. 55 indexed citations
4.
Liu, Jing, Chao Yang, Catherine Simpson, et al.. (2012). Discovery of Small Molecule Mer Kinase Inhibitors for the Treatment of Pediatric Acute Lymphoblastic Leukemia. ACS Medicinal Chemistry Letters. 3(2). 129–134. 66 indexed citations
5.
Bosch, Dustin E., Adam J. Kimple, Alyssa J. Manning, et al.. (2012). Structural Determinants of RGS-RhoGEF Signaling Critical to Entamoeba histolytica Pathogenesis. Structure. 21(1). 65–75. 7 indexed citations
6.
Jones, Janice C., et al.. (2011). The Crystal Structure of a Self-Activating G Protein α Subunit Reveals Its Distinct Mechanism of Signal Initiation. Science Signaling. 4(159). ra8–ra8. 113 indexed citations
7.
Otomo, Takanori, Diana R. Tomchick, Chinatsu Otomo, Mischa Machius, & Michael K. Rosen. (2010). Crystal Structure of the Formin mDia1 in Autoinhibited Conformation. PLoS ONE. 5(9). e12896–e12896. 44 indexed citations
8.
Scheuermann, Thomas H., Diana R. Tomchick, Mischa Machius, et al.. (2009). Artificial ligand binding within the HIF2α PAS-B domain of the HIF2 transcription factor. Proceedings of the National Academy of Sciences. 106(2). 450–455. 225 indexed citations
9.
10.
Kato, Masato, Richard Wynn, Jacinta L. Chuang, et al.. (2008). Structural Basis for Inactivation of the Human Pyruvate Dehydrogenase Complex by Phosphorylation: Role of Disordered Phosphorylation Loops. Structure. 16(12). 1849–1859. 101 indexed citations
11.
Yang, Maojun, Bing Li, Diana R. Tomchick, et al.. (2008). Insights into Mad2 Regulation in the Spindle Checkpoint Revealed by the Crystal Structure of the Symmetric Mad2 Dimer. PLoS Biology. 6(3). e50–e50. 84 indexed citations
12.
Yang, Maojun, Jeffrey C. Culhane, Lawrence M. Szewczuk, et al.. (2007). Structural basis of histone demethylation by LSD1 revealed by suicide inactivation. Nature Structural & Molecular Biology. 14(6). 535–539. 148 indexed citations
13.
Chosed, Renée J., Diana R. Tomchick, Chad A. Brautigam, et al.. (2007). Structural Analysis of Xanthomonas XopD Provides Insights into Substrate Specificity of Ubiquitin-like Protein Proteases. Journal of Biological Chemistry. 282(9). 6773–6782. 62 indexed citations
14.
Yang, Maojun, Christian B. Gocke, Xuelian Luo, et al.. (2006). Structural Basis for CoREST-Dependent Demethylation of Nucleosomes by the Human LSD1 Histone Demethylase. Molecular Cell. 23(3). 377–387. 265 indexed citations
15.
Otomo, Takanori, Chinatsu Otomo, Diana R. Tomchick, Mischa Machius, & Michael K. Rosen. (2005). Structural Basis of Rho GTPase-Mediated Activation of the Formin mDia1. Molecular Cell. 18(3). 273–281. 201 indexed citations
16.
Wynn, Richard, Masato Kato, Mischa Machius, et al.. (2004). Molecular Mechanism for Regulation of the Human Mitochondrial Branched-Chain α-Ketoacid Dehydrogenase Complex by Phosphorylation. Structure. 12(12). 2185–2196. 49 indexed citations
17.
Hu, Xiaojian, Mischa Machius, & Wei Yang. (2003). Monovalent cation dependence and preference of GHKL ATPases and kinases1. FEBS Letters. 544(1-3). 268–273. 39 indexed citations
18.
Declerck, Nathalie, Mischa Machius, Philippe Joyet, et al.. (2002). Engineering the thermostability of Bacillus licheniformis alpha-amylase. Max Planck Institute for Plasma Physics. 57. 203–211. 26 indexed citations
19.
Tomchick, Diana R., et al.. (2002). Three-dimensional structure of the complexin/snare complex. Acta Crystallographica Section A Foundations of Crystallography. 58(s1). c245–c245. 3 indexed citations
20.
Declerck, Nathalie, Mischa Machius, Philippe Joyet, et al.. (2002). Engineering the thermostability of Bacillus licheniformis -amylase. 26 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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