Erkki Raulo

1.6k total citations
17 papers, 1.4k citations indexed

About

Erkki Raulo is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Erkki Raulo has authored 17 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 12 papers in Cell Biology and 3 papers in Cellular and Molecular Neuroscience. Recurrent topics in Erkki Raulo's work include Proteoglycans and glycosaminoglycans research (12 papers), Glycosylation and Glycoproteins Research (3 papers) and Hippo pathway signaling and YAP/TAZ (3 papers). Erkki Raulo is often cited by papers focused on Proteoglycans and glycosaminoglycans research (12 papers), Glycosylation and Glycoproteins Research (3 papers) and Hippo pathway signaling and YAP/TAZ (3 papers). Erkki Raulo collaborates with scholars based in Finland, Japan and United States. Erkki Raulo's co-authors include Heikki Rauvala, Riitta Nolo, Jussi Merenmies, Tarja Kinnunen, Marko Kaksonen, Michael A. Chernousov, DJ Carey, Ilkka Kilpeläinen, Marc Baumann and Shinji Imai and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Neuroscience and The Journal of Cell Biology.

In The Last Decade

Erkki Raulo

17 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Erkki Raulo Finland 15 847 782 265 250 169 17 1.4k
Tarja Kinnunen Finland 17 700 0.8× 706 0.9× 226 0.9× 193 0.8× 43 0.3× 22 1.2k
Inger Eriksson Sweden 19 1.4k 1.7× 1.2k 1.5× 141 0.5× 175 0.7× 104 0.6× 32 1.9k
Nieves Movilla Spain 13 819 1.0× 256 0.3× 58 0.2× 122 0.5× 124 0.7× 19 1.2k
R. Mailhammer Germany 10 794 0.9× 281 0.4× 312 1.2× 212 0.8× 13 0.1× 10 1.3k
Cynthia Zerillo United States 13 714 0.8× 435 0.6× 258 1.0× 143 0.6× 8 0.0× 17 1.2k
Absorn Sriratana Australia 16 792 0.9× 406 0.5× 73 0.3× 48 0.2× 26 0.2× 22 1.2k
Jun-Lin Guan United States 10 695 0.8× 354 0.5× 100 0.4× 387 1.5× 11 0.1× 10 1.2k
Soline Estrach France 20 1.3k 1.5× 652 0.8× 507 1.9× 172 0.7× 9 0.1× 27 2.0k
Mayumi Matsunaga Japan 19 756 0.9× 214 0.3× 313 1.2× 153 0.6× 11 0.1× 36 1.3k
Pamela J. Swiatek United States 16 896 1.1× 376 0.5× 79 0.3× 192 0.8× 9 0.1× 22 1.4k

Countries citing papers authored by Erkki Raulo

Since Specialization
Citations

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

Fields of papers citing papers by Erkki Raulo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Erkki Raulo

This figure shows the co-authorship network connecting the top 25 collaborators of Erkki Raulo. A scholar is included among the top collaborators of Erkki Raulo 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 Erkki Raulo. Erkki Raulo 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.
Pääkkönen, Kimmo, Helena Tossavainen, Perttu Permi, et al.. (2006). Solution structures of the first and fourth TSR domains of F‐spondin. Proteins Structure Function and Bioinformatics. 64(3). 665–672. 32 indexed citations
2.
Tossavainen, Helena, Tero Pihlajamaa, Erkki Raulo, et al.. (2006). The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site. Protein Science. 15(7). 1760–1768. 55 indexed citations
3.
Raulo, Erkki, Sarka Tumova, Ivan Pavlov, et al.. (2006). The Two Thrombospondin Type I Repeat Domains of HB-GAM Display a Cooperative Function in N-syndecan Binding and Regulation of Synaptic Plasticity. The Scientific World JOURNAL. 6. 406–409. 4 indexed citations
4.
Raulo, Erkki, Sarka Tumova, Ivan Pavlov, et al.. (2005). The Two Thrombospondin Type I Repeat Domains of the Heparin-binding Growth-associated Molecule Bind to Heparin/Heparan Sulfate and Regulate Neurite Extension and Plasticity in Hippocampal Neurons. Journal of Biological Chemistry. 280(50). 41576–41583. 36 indexed citations
5.
Hienola, Anni, Mari Pekkanen-Mattila, Erkki Raulo, Päivi Vanttola, & Heikki Rauvala. (2004). HB-GAM inhibits proliferation and enhances differentiation of neural stem cells. Molecular and Cellular Neuroscience. 26(1). 75–88. 53 indexed citations
6.
Rauvala, Heikki, Henri J. Huttunen, Carole Fages, et al.. (2000). Heparin-binding proteins HB-GAM (pleiotrophin) and amphoterin in the regulation of cell motility. Matrix Biology. 19(5). 377–387. 125 indexed citations
7.
Kilpeläinen, Ilkka, Marko Kaksonen, Tarja Kinnunen, et al.. (2000). Heparin-binding Growth-associated Molecule Contains Two Heparin-binding β-Sheet Domains That Are Homologous to the Thrombospondin Type I Repeat. Journal of Biological Chemistry. 275(18). 13564–13570. 96 indexed citations
8.
Imai, Shinji, Marko Kaksonen, Erkki Raulo, et al.. (1998). Osteoblast Recruitment and Bone Formation Enhanced by Cell Matrix–associated Heparin-binding Growth-associated Molecule (HB-GAM). The Journal of Cell Biology. 143(4). 1113–1128. 98 indexed citations
9.
Kinnunen, Tarja, Erkki Raulo, Riitta Nolo, et al.. (1996). Neurite Outgrowth in Brain Neurons Induced by Heparin-binding Growth-associated Molecule (HB-GAM) Depends on the Specific Interaction of HB-GAM with Heparan Sulfate at the Cell Surface. Journal of Biological Chemistry. 271(4). 2243–2248. 109 indexed citations
10.
Wısnıewskı, Thomas, Maciej Łałowski, Marc Baumann, et al.. (1996). HB-GAM is a cytokine present in Alzheimerʼs and Downʼs syndrome lesions. Neuroreport. 7(2). 667–671. 31 indexed citations
11.
Nolo, Riitta, Marko Kaksonen, Erkki Raulo, & Heikki Rauvala. (1995). Co-expression of heparin-binding growth-associated molecule (HB-GAM) and N-syndecan (syndecan-3) in developing rat brain. Neuroscience Letters. 191(1-2). 39–42. 41 indexed citations
12.
Dai, Zonghan, et al.. (1995). The role of heparin-binding growth-associated molecule (HB-GAM) in the postsynaptic induction in cultured muscle cells. Journal of Neuroscience. 15(4). 3027–3038. 88 indexed citations
14.
Raulo, Erkki, Michael A. Chernousov, DJ Carey, Riitta Nolo, & Heikki Rauvala. (1994). Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3).. Journal of Biological Chemistry. 269(17). 12999–13004. 247 indexed citations
15.
Parkkinen, J, Erkki Raulo, Jussi Merenmies, et al.. (1993). Amphoterin, the 30-kDa protein in a family of HMG1-type polypeptides. Enhanced expression in transformed cells, leading edge localization, and interactions with plasminogen activation.. Journal of Biological Chemistry. 268(26). 19726–19738. 182 indexed citations
17.
Kaihovaara, Pertti, Erkki Raulo, & Paavo K.J. Kinnunen. (1991). Changes in lipid distribution and dynamics in degranulated rat liver rough endoplasmic reticulum due to the membrane attachment of polyribosomes. Biochemistry. 30(34). 8380–8386. 14 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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