Jay M. Janz

1.2k total citations
20 papers, 883 citations indexed

About

Jay M. Janz is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Oncology. According to data from OpenAlex, Jay M. Janz has authored 20 papers receiving a total of 883 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 11 papers in Cellular and Molecular Neuroscience and 3 papers in Oncology. Recurrent topics in Jay M. Janz's work include Receptor Mechanisms and Signaling (13 papers), Photoreceptor and optogenetics research (7 papers) and Retinal Development and Disorders (6 papers). Jay M. Janz is often cited by papers focused on Receptor Mechanisms and Signaling (13 papers), Photoreceptor and optogenetics research (7 papers) and Retinal Development and Disorders (6 papers). Jay M. Janz collaborates with scholars based in United States, Canada and United Kingdom. Jay M. Janz's co-authors include David Farrens, Jonathan F. Fay, Thomas P. Sakmar, Kenneth E. Carlson, S. Hunt, Yong Ren, Michel Bouvier, Jeffrey Benovic, Julie Quoyer and Viktoria Lukashova and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Jay M. Janz

20 papers receiving 876 citations

Peers

Jay M. Janz
Walter Strapps United States
Fu‐Yue Zeng United States
Robbin Brodbeck United States
Terri Messier United States
Tom S. Wehrman United States
Shawn K. Milano United States
Lynn Wang United States
W. David Culp United States
R. Scott Struthers United States
Lorena A. Kallal United States
Walter Strapps United States
Jay M. Janz
Citations per year, relative to Jay M. Janz Jay M. Janz (= 1×) peers Walter Strapps

Countries citing papers authored by Jay M. Janz

Since Specialization
Citations

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

Fields of papers citing papers by Jay M. Janz

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jay M. Janz

This figure shows the co-authorship network connecting the top 25 collaborators of Jay M. Janz. A scholar is included among the top collaborators of Jay M. Janz 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 Jay M. Janz. Jay M. Janz 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.
Kelly, John J., Dale Tranter, Els Pardon, et al.. (2022). Snapshots of actin and tubulin folding inside the TRiC chaperonin. Nature Structural & Molecular Biology. 29(5). 420–429. 27 indexed citations
2.
Knee, Kelly M., Reema Jasuja, J. Jasti, et al.. (2021). PF‐07059013: A non‐covalent hemoglobin modulator favorably impacts disease state in a mouse model of sickle cell disease. American Journal of Hematology. 96(8). E272–E275. 4 indexed citations
3.
Knee, Kelly M., Reema Jasuja, Parag V. Sahasrabudhe, et al.. (2019). A Novel Non-Covalent Modulator of Hemoglobin Improves Anemia and Reduces Sickling in a Mouse Model of Sickle Cell Disease. Blood. 134(Supplement_1). 207–207. 1 indexed citations
4.
Fox, Nicholas G., Alain Martelli, Joseph F. Nabhan, et al.. (2018). Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity. Biochimie. 152. 211–218. 15 indexed citations
5.
Fay, Jonathan F., et al.. (2016). Decay of an active GPCR: Conformational dynamics govern agonist rebinding and persistence of an active, yet empty, receptor state. Proceedings of the National Academy of Sciences. 113(42). 11961–11966. 29 indexed citations
6.
Carr, Richard W., Yang Du, Julie Quoyer, et al.. (2014). Development and Characterization of Pepducins as Gs-biased Allosteric Agonists*. Journal of Biological Chemistry. 289(52). 35668–35684. 70 indexed citations
7.
McCorvie, Thomas J., J. Kopec, Suk‐Joon Hyung, et al.. (2014). Inter-domain Communication of Human Cystathionine β-Synthase. Journal of Biological Chemistry. 289(52). 36018–36030. 43 indexed citations
8.
Quoyer, Julie, Jay M. Janz, Jiansong Luo, et al.. (2013). Pepducin targeting the C-X-C chemokine receptor type 4 acts as a biased agonist favoring activation of the inhibitory G protein. Proceedings of the National Academy of Sciences. 110(52). E5088–97. 133 indexed citations
9.
Carlson, Kenneth E., Michel Bouvier, Craig Gérard, et al.. (2011). G protein–coupled receptor modulation with pepducins: moving closer to the clinic. Annals of the New York Academy of Sciences. 1226(1). 34–49. 36 indexed citations
10.
Janz, Jay M., Yong Ren, Richard Looby, et al.. (2011). Direct Interaction between an Allosteric Agonist Pepducin and the Chemokine Receptor CXCR4. Journal of the American Chemical Society. 133(40). 15878–15881. 62 indexed citations
11.
Tchernychev, Boris, Yong Ren, Perminder S. Sachdev, et al.. (2010). Discovery of a CXCR4 agonist pepducin that mobilizes bone marrow hematopoietic cells. Proceedings of the National Academy of Sciences. 107(51). 22255–22259. 87 indexed citations
12.
Janz, Jay M., et al.. (2010). Rapid Binding and Transmembrane Diffusion of Pepducins in Phospholipid Bilayers. Biophysical Journal. 98(3). 278a–278a. 4 indexed citations
13.
Janz, Jay M., Thomas P. Sakmar, & K. Christopher Min. (2007). A Novel Interaction between Atrophin-interacting Protein 4 and β-p21-activated Kinase-interactive Exchange Factor Is Mediated by an SH3 Domain. Journal of Biological Chemistry. 282(39). 28893–28903. 22 indexed citations
14.
Hoelz, André, et al.. (2006). Crystal Structure of the SH3 Domain of βPIX in Complex with a High Affinity Peptide from PAK2. Journal of Molecular Biology. 358(2). 509–522. 42 indexed citations
15.
Janz, Jay M. & David Farrens. (2004). Role of the Retinal Hydrogen Bond Network in Rhodopsin Schiff Base Stability and Hydrolysis. Journal of Biological Chemistry. 279(53). 55886–55894. 64 indexed citations
16.
Janz, Jay M. & David Farrens. (2004). Rhodopsin Activation Exposes a Key Hydrophobic Binding Site for the Transducin α-Subunit C Terminus. Journal of Biological Chemistry. 279(28). 29767–29773. 87 indexed citations
18.
Janz, Jay M. & David Farrens. (2003). Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms. Vision Research. 43(28). 2991–3002. 30 indexed citations
19.
Janz, Jay M., Jonathan F. Fay, & David Farrens. (2003). Stability of Dark State Rhodopsin Is Mediated by a Conserved Ion Pair in Intradiscal Loop E-2. Journal of Biological Chemistry. 278(19). 16982–16991. 76 indexed citations
20.
Janz, Jay M. & David Farrens. (2001). Engineering a Functional Blue-Wavelength-Shifted Rhodopsin Mutant. Biochemistry. 40(24). 7219–7227. 49 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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