V.L. Linhard

499 total citations
17 papers, 283 citations indexed

About

V.L. Linhard is a scholar working on Molecular Biology, Computational Theory and Mathematics and Cellular and Molecular Neuroscience. According to data from OpenAlex, V.L. Linhard has authored 17 papers receiving a total of 283 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 6 papers in Computational Theory and Mathematics and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in V.L. Linhard's work include Computational Drug Discovery Methods (6 papers), Axon Guidance and Neuronal Signaling (5 papers) and Enzyme Structure and Function (3 papers). V.L. Linhard is often cited by papers focused on Computational Drug Discovery Methods (6 papers), Axon Guidance and Neuronal Signaling (5 papers) and Enzyme Structure and Function (3 papers). V.L. Linhard collaborates with scholars based in Germany, United States and Sweden. V.L. Linhard's co-authors include Harald Schwalbe, Sridhar Sreeramulu, S.L. Gande, D. Kudlinzki, Krishna Saxena, Stephanie Heinzlmeir, Bernhard Küster, Christian Richter, Guillaume Médard and Daniel Merk and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Journal of Molecular Biology.

In The Last Decade

V.L. Linhard

15 papers receiving 282 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
V.L. Linhard Germany 9 179 81 55 40 27 17 283
Palani Kirubakaran India 12 262 1.5× 80 1.0× 38 0.7× 116 2.9× 20 0.7× 22 416
Adrien Herlédan France 12 260 1.5× 63 0.8× 55 1.0× 38 0.9× 10 0.4× 21 441
Hitoshi Sakashita Japan 10 220 1.2× 50 0.6× 45 0.8× 54 1.4× 19 0.7× 19 409
Monimoy Banerjee United States 13 279 1.6× 60 0.7× 18 0.3× 49 1.2× 34 1.3× 23 420
Wenzhong Yan China 12 280 1.6× 64 0.8× 93 1.7× 42 1.1× 9 0.3× 19 433
Jesús Vázquez Spain 10 265 1.5× 65 0.8× 42 0.8× 54 1.4× 8 0.3× 12 368
Scott E. Warder United States 16 416 2.3× 86 1.1× 111 2.0× 45 1.1× 20 0.7× 27 590
Juan Martinez‐Sanz France 6 244 1.4× 83 1.0× 18 0.3× 109 2.7× 49 1.8× 9 329
Christian Meyners Germany 13 358 2.0× 98 1.2× 18 0.3× 18 0.5× 30 1.1× 40 485
Nandhitha Subramanian Australia 12 219 1.2× 137 1.7× 42 0.8× 24 0.6× 15 0.6× 13 320

Countries citing papers authored by V.L. Linhard

Since Specialization
Citations

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

Fields of papers citing papers by V.L. Linhard

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by V.L. Linhard. 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 V.L. Linhard. The network helps show where V.L. Linhard may publish in the future.

Co-authorship network of co-authors of V.L. Linhard

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

All Works

17 of 17 papers shown
1.
Минеев, Константин С., et al.. (2024). NMR resonance assignment of a ligand-binding domain of ephrin receptor A2. Biomolecular NMR Assignments. 19(1). 23–28.
2.
Kudlinzki, D., Sridhar Sreeramulu, S.L. Gande, et al.. (2023). Optimization of the Lead Compound NVP‐BHG712 as a Colorectal Cancer Inhibitor. Chemistry - A European Journal. 29(23). e202203967–e202203967. 8 indexed citations
3.
Bellomo, Giovanni, Alexey V. Cherepanov, Elke Stirnal, et al.. (2023). Modulation of Aβ42 Aggregation Kinetics and Pathway by Low‐Molecular‐Weight Inhibitors. ChemBioChem. 24(7). e202200760–e202200760.
4.
Gallo, Angelo, Sridhar Sreeramulu, Frank Löhr, et al.. (2022). Binding Adaptation of GS-441524 Diversifies Macro Domains and Downregulates SARS-CoV-2 de-MARylation Capacity. Journal of Molecular Biology. 434(16). 167720–167720. 7 indexed citations
5.
Heering, Jan, Evelyn Peelen, Hella Kohlhof, et al.. (2022). Mechanistic Impact of Different Ligand Scaffolds on FXR Modulation Suggests Avenues to Selective Modulators. ACS Chemical Biology. 17(11). 3159–3168. 6 indexed citations
6.
Linhard, V.L., Sara Weirich, Anja Köhler, et al.. (2022). The MECP2‐TRD domain interacts with the DNMT3A‐ADD domain at the H3‐tail binding site. Protein Science. 32(1). e4542–e4542. 6 indexed citations
7.
Merk, Daniel, Sridhar Sreeramulu, D. Kudlinzki, et al.. (2019). Molecular tuning of farnesoid X receptor partial agonism. Nature Communications. 10(1). 2915–2915. 78 indexed citations
8.
Wulsdorf, Tobias, Hendrik R. A. Jonker, Krishna Saxena, et al.. (2018). On the Implication of Water on Fragment‐to‐Ligand Growth in Kinase Binding Thermodynamics. ChemMedChem. 13(18). 1988–1996. 8 indexed citations
9.
Jonker, Hendrik R. A., et al.. (2018). The domain architecture of PtkA, the first tyrosine kinase from Mycobacterium tuberculosis, differs from the conventional kinase architecture. Journal of Biological Chemistry. 293(30). 11823–11836. 6 indexed citations
10.
Heinzlmeir, Stephanie, Benedict‐Tilman Berger, S.L. Gande, et al.. (2018). NVP‐BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family. ChemMedChem. 13(16). 1629–1633. 24 indexed citations
11.
Heinzlmeir, Stephanie, D. Kudlinzki, V.L. Linhard, et al.. (2017). Chemoproteomics‐Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors. ChemMedChem. 12(12). 999–1011. 22 indexed citations
12.
Heinzlmeir, Stephanie, D. Kudlinzki, Sridhar Sreeramulu, et al.. (2016). Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs. ACS Chemical Biology. 11(12). 3400–3411. 37 indexed citations
13.
Gande, S.L., Krishna Saxena, Sridhar Sreeramulu, et al.. (2016). Expression and Purification of EPHA2 Tyrosine Kinase Domain for Crystallographic and NMR Studies. ChemBioChem. 17(23). 2257–2263. 5 indexed citations
14.
Chatterjee, Deep, D. Kudlinzki, V.L. Linhard, et al.. (2015). Structure and Biophysical Characterization of the S-Adenosylmethionine-dependent O-Methyltransferase PaMTH1, a Putative Enzyme Accumulating during Senescence of Podospora anserina. Journal of Biological Chemistry. 290(26). 16415–16430. 20 indexed citations
15.
Kudlinzki, D., V.L. Linhard, Krishna Saxena, et al.. (2015). High-resolution crystal structure of cAMP-dependent protein kinase fromCricetulus griseus. Acta Crystallographica Section F Structural Biology Communications. 71(8). 1088–1093. 7 indexed citations
16.
Toal, Siobhan, et al.. (2015). Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor Interactions between Unlike Residues. Chemistry - A European Journal. 21(13). 5173–5192. 30 indexed citations
17.
Ma, Xueyan, Juergen Koepke, V.L. Linhard, et al.. (2004). Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1701(1-2). 129–132. 19 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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