N.O. Concha

4.9k total citations
23 papers, 2.0k citations indexed

About

N.O. Concha is a scholar working on Molecular Biology, Infectious Diseases and Organic Chemistry. According to data from OpenAlex, N.O. Concha has authored 23 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Infectious Diseases and 4 papers in Organic Chemistry. Recurrent topics in N.O. Concha's work include Antibiotic Resistance in Bacteria (4 papers), Synthesis and Catalytic Reactions (3 papers) and Cell death mechanisms and regulation (3 papers). N.O. Concha is often cited by papers focused on Antibiotic Resistance in Bacteria (4 papers), Synthesis and Catalytic Reactions (3 papers) and Cell death mechanisms and regulation (3 papers). N.O. Concha collaborates with scholars based in United States, United Kingdom and Germany. N.O. Concha's co-authors include John Dedman, Barbara A. Seaton, Osnat Herzberg, Beth A. Rasmussen, Karen Bush, Marcia A. Kaetzel, Manal A. Swairjo, J. W. Head, M. A. Kaetzel and Hongwei Qi and has published in prestigious journals such as Science, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

N.O. Concha

23 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N.O. Concha United States 17 1.2k 555 209 207 182 23 2.0k
Aiming Sun United States 29 947 0.8× 533 1.0× 455 2.2× 149 0.7× 151 0.8× 42 2.1k
Natale D’Alessandro Italy 23 887 0.7× 311 0.6× 104 0.5× 222 1.1× 362 2.0× 57 1.6k
Xianzhang Bu China 31 2.0k 1.7× 271 0.5× 147 0.7× 275 1.3× 601 3.3× 103 3.3k
Anna M. Rydzik United Kingdom 20 607 0.5× 425 0.8× 207 1.0× 212 1.0× 65 0.4× 42 1.1k
Günther Kern United States 19 913 0.8× 412 0.7× 173 0.8× 309 1.5× 150 0.8× 49 2.0k
Yamei Yu China 27 842 0.7× 121 0.2× 177 0.8× 170 0.8× 207 1.1× 81 2.0k
Xiangqian Kong China 24 1.2k 1.0× 108 0.2× 89 0.4× 115 0.6× 195 1.1× 77 1.9k
Alice H. Lin United States 18 782 0.7× 109 0.2× 198 0.9× 318 1.5× 150 0.8× 29 2.0k
Pierre Falson France 29 1.6k 1.3× 122 0.2× 235 1.1× 102 0.5× 826 4.5× 114 2.6k
Michael Brands Germany 20 1.1k 0.9× 124 0.2× 68 0.3× 353 1.7× 360 2.0× 46 2.1k

Countries citing papers authored by N.O. Concha

Since Specialization
Citations

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

Fields of papers citing papers by N.O. Concha

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by N.O. Concha. 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 N.O. Concha. The network helps show where N.O. Concha may publish in the future.

Co-authorship network of co-authors of N.O. Concha

This figure shows the co-authorship network connecting the top 25 collaborators of N.O. Concha. A scholar is included among the top collaborators of N.O. Concha 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 N.O. Concha. N.O. Concha 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.
Concha, N.O., et al.. (2024). Structural insight into the DNMT1 reaction cycle by cryo-electron microscopy. PLoS ONE. 19(9). e0307850–e0307850. 2 indexed citations
2.
Williams, Shawn P., David P. Dixon, Paris Ward, et al.. (2021). Novel Bent Conformation of CD4 Induced by HIV-1 Inhibitor Indirectly Prevents Productive Viral Attachment. Journal of Molecular Biology. 434(2). 167395–167395. 1 indexed citations
3.
Concha, N.O., Angela Smallwood, William G. Bonnette, et al.. (2015). Long-Range Inhibitor-Induced Conformational Regulation of Human IRE1α Endoribonuclease Activity. Molecular Pharmacology. 88(6). 1011–1023. 42 indexed citations
4.
Cleasby, Anne, Jeff Yon, Philip J. Day, et al.. (2014). Structure of the BTB Domain of Keap1 and Its Interaction with the Triterpenoid Antagonist CDDO. PLoS ONE. 9(6). e98896–e98896. 202 indexed citations
5.
Rendina, Alan R., Beth Pietrak, Angela Smallwood, et al.. (2013). Mutant IDH1 Enhances the Production of 2-Hydroxyglutarate Due to Its Kinetic Mechanism. Biochemistry. 52(26). 4563–4577. 64 indexed citations
6.
Schneck, Jessica L., Jacques Briand, Stephanie Chen, et al.. (2010). Kinetic Mechanism and Rate-Limiting Steps of Focal Adhesion Kinase-1. Biochemistry. 49(33). 7151–7163. 11 indexed citations
7.
Seefeld, Mark A., Meagan B. Rouse, Jizhou Wang, et al.. (2009). Discovery of 5-pyrrolopyridinyl-2-thiophenecarboxamides as potent AKT kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 19(8). 2244–2248. 21 indexed citations
8.
Rouse, Meagan B., Mark A. Seefeld, Jack D. Leber, et al.. (2009). Aminofurazans as potent inhibitors of AKT kinase. Bioorganic & Medicinal Chemistry Letters. 19(5). 1508–1511. 33 indexed citations
9.
Lin, Hong, Dennis S. Yamashita, Jin Zeng, et al.. (2009). 2,3,5-Trisubstituted pyridines as selective AKT inhibitors—Part I: Substitution at 2-position of the core pyridine for ROCK1 selectivity. Bioorganic & Medicinal Chemistry Letters. 20(2). 673–678. 11 indexed citations
10.
Shaw, Antony N., Rosanna Tedesco, Ramesh Bambal, et al.. (2009). Substituted benzothiadizine inhibitors of Hepatitis C virus polymerase. Bioorganic & Medicinal Chemistry Letters. 19(15). 4350–4353. 37 indexed citations
11.
Zhao, Baoguang, Michael J. Bower, Patrick McDevitt, et al.. (2002). Structural Basis for Chk1 Inhibition by UCN-01. Journal of Biological Chemistry. 277(48). 46609–46615. 169 indexed citations
12.
Concha, N.O. & S. Abdel‐Meguid. (2002). Controlling Apoptosis by Inhibition of Caspases. Current Medicinal Chemistry. 9(6). 713–726. 40 indexed citations
13.
Head, Martha S., Margret Ryan, Dennis Lee, et al.. (2001). Structure-based combinatorial library design: Discovery of non-peptidic inhibitors of caspases 3 and 8. Journal of Computer-Aided Molecular Design. 15(12). 1105–1117. 3 indexed citations
14.
15.
Concha, N.O., et al.. (1997). Crystal structures of the cadmium‐ and mercury‐substituted metallo‐β‐lactamase from Bacteroides fragilis. Protein Science. 6(12). 2671–2676. 41 indexed citations
16.
Concha, N.O., Beth A. Rasmussen, Karen Bush, & Osnat Herzberg. (1996). Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure. 4(7). 823–836. 302 indexed citations
17.
Swairjo, Manal A., N.O. Concha, Marcia A. Kaetzel, John Dedman, & Barbara A. Seaton. (1995). Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nature Structural & Molecular Biology. 2(11). 968–974. 253 indexed citations
18.
Castillo‐Durán, Carlos, et al.. (1994). Zinc supplementation increases growth velocity of male children and adolescents with short stature. Acta Paediatrica. 83(8). 833–837. 75 indexed citations
19.
Concha, N.O., J. W. Head, M. A. Kaetzel, John Dedman, & Barbara A. Seaton. (1993). Rat Annexin V Crystal Structure: Ca 2+ -Induced Conformational Changes. Science. 261(5126). 1321–1324. 152 indexed citations
20.
Concha, N.O., J. W. Head, Marcia A. Kaetzel, John Dedman, & Barbara A. Seaton. (1992). Annexin V forms calcium‐dependent trimeric units on phospholipid vesicles. FEBS Letters. 314(2). 159–162. 83 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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