Jan Sap

3.9k total citations · 1 hit paper
34 papers, 3.2k citations indexed

About

Jan Sap is a scholar working on Molecular Biology, Immunology and Immunology and Allergy. According to data from OpenAlex, Jan Sap has authored 34 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 15 papers in Immunology and 7 papers in Immunology and Allergy. Recurrent topics in Jan Sap's work include Protein Tyrosine Phosphatases (20 papers), Galectins and Cancer Biology (11 papers) and Cell Adhesion Molecules Research (7 papers). Jan Sap is often cited by papers focused on Protein Tyrosine Phosphatases (20 papers), Galectins and Cancer Biology (11 papers) and Cell Adhesion Molecules Research (7 papers). Jan Sap collaborates with scholars based in United States, France and Denmark. Jan Sap's co-authors include Björn Vennström, Alberto Múñoz, Hartmut Beug, Klaus Damm, Jacques Ghysdael, Achim Leutz, Yves Goldberg, Jing Su, Madhavi Muranjan and Henk G. Stunnenberg and has published in prestigious journals such as Nature, Cell and Journal of Biological Chemistry.

In The Last Decade

Jan Sap

34 papers receiving 3.2k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

The c-erb-A protein is a high-affinity receptor for thyroid hormone

1986 1.1k citations Jan Sap, Alberto Múñoz et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jan Sap United States	25	2.0k	917	767	680	510	34	3.2k
Lucio Nitsch Italy	36	2.2k 1.1×	819 0.9×	373 0.5×	234 0.3×	938 1.8×	118	3.8k
M G Rosenfeld United States	40	3.1k 1.5×	906 1.0×	1.0k 1.4×	340 0.5×	535 1.0×	52	4.7k
Francis James Grant United States	22	1.5k 0.8×	373 0.4×	292 0.4×	352 0.5×	281 0.6×	33	3.1k
Yves Goldberg France	18	2.9k 1.4×	740 0.8×	650 0.8×	300 0.4×	466 0.9×	24	3.9k
Glen A. Evans United States	36	2.3k 1.2×	861 0.9×	194 0.3×	808 1.2×	205 0.4×	80	4.0k
Li‐Yuan Yu‐Lee United States	42	2.3k 1.2×	659 0.7×	620 0.8×	970 1.4×	576 1.1×	99	4.7k
Hugues Loosfelt France	25	1.4k 0.7×	1.3k 1.4×	803 1.0×	452 0.7×	143 0.3×	35	3.0k
Steven P. Smeekens United States	20	1.7k 0.8×	391 0.4×	424 0.6×	291 0.4×	953 1.9×	25	3.5k
Denis Banville Canada	25	1.5k 0.7×	245 0.3×	327 0.4×	563 0.8×	231 0.5×	37	2.4k
Ned Mantei Switzerland	40	2.9k 1.5×	1.5k 1.6×	187 0.2×	941 1.4×	467 0.9×	58	5.5k

Countries citing papers authored by Jan Sap

Since Specialization

Citations

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

Fields of papers citing papers by Jan Sap

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jan Sap

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

All Works

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20 of 20 papers shown

Cressant, Arnaud, Véronique Dubreuil, Jing Kong, et al.. (2016). Loss-of-function of PTPR γ and ζ, observed in sporadic schizophrenia, causes brain region-specific deregulation of monoamine levels and altered behavior in mice. Psychopharmacology. 234(4). 575–587. 18 indexed citations

Aschner, Yael, Anthony P. Khalifah, Natalie Briones, et al.. (2014). Protein Tyrosine Phosphatase α Mediates Profibrotic Signaling in Lung Fibroblasts through TGF-β Responsiveness. American Journal Of Pathology. 184(5). 1489–1502. 25 indexed citations

Dubreuil, Véronique, Jan Sap, & Sheila Harroch. (2014). Protein tyrosine phosphatase regulation of stem and progenitor cell biology. Seminars in Cell and Developmental Biology. 37. 82–89. 3 indexed citations

Truffi, Marta, Véronique Dubreuil, Xuan Liang, et al.. (2014). Receptor protein tyrosine phosphatase RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src signaling to cortactin. Journal of Cell Science. 127(Pt 11). 2420–32. 27 indexed citations

Ambjørn, Malene, Véronique Dubreuil, Fabienne Nigon, et al.. (2013). A Loss-of-Function Screen for Phosphatases that Regulate Neurite Outgrowth Identifies PTPN12 as a Negative Regulator of TrkB Tyrosine Phosphorylation. PLoS ONE. 8(6). e65371–e65371. 11 indexed citations

Yahiro, Kinnosuke, Mamoru Satoh, Masayuki Nakano, et al.. (2012). Low-density Lipoprotein Receptor-related Protein-1 (LRP1) Mediates Autophagy and Apoptosis Caused by Helicobacter pylori VacA. Journal of Biological Chemistry. 287(37). 31104–31115. 104 indexed citations

Takahashi, Nagahide, Branko Aleksić, Steffen E. Petersen, et al.. (2011). Loss of Function Studies in Mice and Genetic Association Link Receptor Protein Tyrosine Phosphatase α to Schizophrenia. Biological Psychiatry. 70(7). 626–635. 21 indexed citations

Batista, Wagner L., Edlaine Linares, Fábio Dupart Nascimento, et al.. (2010). Regulatory Effects of Nitric Oxide on Src Kinase, FAK, p130Cas, and Receptor Protein Tyrosine Phosphatase Alpha (PTP-α): A Role for the Cellular Redox Environment. Antioxidants and Redox Signaling. 13(2). 109–125. 20 indexed citations

Vacaresse, Nathalie, Bente K. Møller, E. Michael Danielsen, Masato Okada, & Jan Sap. (2008). Activation of c-Src and Fyn Kinases by Protein-tyrosine Phosphatase RPTPα Is Substrate-specific and Compatible with Lipid Raft Localization. Journal of Biological Chemistry. 283(51). 35815–35824. 37 indexed citations

10.

Peretz, Asher, et al.. (2006). Tyrosine Phosphatases ε and α Perform Specific and Overlapping Functions in Regulation of Voltage-gated Potassium Channels in Schwann Cells. Molecular Biology of the Cell. 17(10). 4330–4342. 26 indexed citations

11.

Yahiro, Kinnosuke, Akihiro Wada, Eiki Yamasaki, et al.. (2004). Essential Domain of Receptor Tyrosine Phosphatase β (RPTPβ) for Interaction with Helicobacter pylori Vacuolating Cytotoxin. Journal of Biological Chemistry. 279(49). 51013–51021. 36 indexed citations

12.

Yang, Liang‐Tung, Konstantina Alexandropoulos, & Jan Sap. (2002). c-SRC Mediates Neurite Outgrowth through Recruitment of Crk to the Scaffolding Protein Sin/Efs without Altering the Kinetics of ERK Activation. Journal of Biological Chemistry. 277(20). 17406–17414. 47 indexed citations

13.

Lu, Huogen, Poonam Shah, David Ennis, et al.. (2002). The Differentiation of Skeletal Muscle Cells Involves a Protein-tyrosine Phosphatase-α-mediated C-Src Signaling Pathway. Journal of Biological Chemistry. 277(48). 46687–46695. 27 indexed citations

14.

Su, Jing, Madhavi Muranjan, & Jan Sap. (1999). Receptor protein tyrosine phosphatase α activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Current Biology. 9(10). 505–511. 230 indexed citations

15.

Cong, Li-Na, et al.. (1999). Overexpression of Protein Tyrosine Phosphatase-α (PTP-α) but not PTP-κ Inhibits Translocation of GLUT4 in Rat Adipose Cells. Biochemical and Biophysical Research Communications. 255(2). 200–207. 25 indexed citations

16.

Sap, Jan, et al.. (1998). Receptor-like Protein-tyrosine Phosphatase α Specifically Inhibits Insulin-increased Prolactin Gene Expression. Journal of Biological Chemistry. 273(8). 4800–4809. 36 indexed citations

17.

Su, Jing, Liang‐Tung Yang, & Jan Sap. (1996). Association between Receptor Protein-tyrosine Phosphatase RPTPα and the Grb2 Adaptor. Journal of Biological Chemistry. 271(45). 28086–28096. 54 indexed citations

18.

Zondag, Gerben, Gregory M. Koningstein, Yingping Jiang, et al.. (1995). Homophilic Interactions Mediated by Receptor Tyrosine Phosphatases μ and κ. A CRITICAL ROLE FOR THE NOVEL EXTRACELLULAR MAM DOMAIN. Journal of Biological Chemistry. 270(24). 14247–14250. 145 indexed citations

19.

Rao, V.V.N. Gopal, et al.. (1992). The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH). Genomics. 13(3). 906–907. 1 indexed citations

20.

Múñoz, Alberto, Wolfgang Höppner, Jan Sap, et al.. (1990). The Chicken c-erbA α-Product Induces Expression of Thyroid Hormone-Responsive Genes in 3,5,3′-Triiodothyronine Receptor- Deficient Rat Hepatoma Cells. Molecular Endocrinology. 4(2). 312–320. 18 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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