Salla Ruskamo

976 total citations
28 papers, 660 citations indexed

About

Salla Ruskamo is a scholar working on Cell Biology, Molecular Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Salla Ruskamo has authored 28 papers receiving a total of 660 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Cell Biology, 16 papers in Molecular Biology and 12 papers in Cellular and Molecular Neuroscience. Recurrent topics in Salla Ruskamo's work include Hereditary Neurological Disorders (12 papers), RNA Research and Splicing (7 papers) and Endoplasmic Reticulum Stress and Disease (5 papers). Salla Ruskamo is often cited by papers focused on Hereditary Neurological Disorders (12 papers), RNA Research and Splicing (7 papers) and Endoplasmic Reticulum Stress and Disease (5 papers). Salla Ruskamo collaborates with scholars based in Finland, Norway and Germany. Salla Ruskamo's co-authors include Petri Kursula, Jari Ylänne, Matti Myllykoski, Iain D. Campbell, Arne Raasakka, Pengju Jiang, Huijong Han, David Calderwood, Yatish Lad and Chaozhan Wang and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Scientific Reports.

In The Last Decade

Salla Ruskamo

27 papers receiving 652 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Salla Ruskamo Finland 16 388 233 188 73 65 28 660
Christel Poujol France 21 651 1.7× 225 1.0× 351 1.9× 137 1.9× 63 1.0× 39 1.5k
Tomoki Nishioka Japan 20 589 1.5× 255 1.1× 230 1.2× 16 0.2× 71 1.1× 41 910
Marina Fasolini Italy 10 592 1.5× 124 0.5× 241 1.3× 32 0.4× 22 0.3× 12 818
Norikazu Mizuno Japan 16 763 2.0× 141 0.6× 264 1.4× 81 1.1× 52 0.8× 20 1.0k
Edith López Mexico 17 426 1.1× 135 0.6× 159 0.8× 92 1.3× 40 0.6× 34 797
Steven G. Matsumoto United States 14 467 1.2× 191 0.8× 218 1.2× 26 0.4× 52 0.8× 22 841
Séverine M. Sigoillot France 13 386 1.0× 86 0.4× 147 0.8× 30 0.4× 47 0.7× 18 600
Sventja von Daake United States 12 525 1.4× 120 0.5× 128 0.7× 17 0.2× 41 0.6× 12 668
Jan Schepens Netherlands 24 1.0k 2.7× 299 1.3× 237 1.3× 34 0.5× 126 1.9× 47 1.4k
Ruth Herbst Austria 17 675 1.7× 192 0.8× 166 0.9× 18 0.2× 76 1.2× 28 989

Countries citing papers authored by Salla Ruskamo

Since Specialization
Citations

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

Fields of papers citing papers by Salla Ruskamo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Salla Ruskamo

This figure shows the co-authorship network connecting the top 25 collaborators of Salla Ruskamo. A scholar is included among the top collaborators of Salla Ruskamo 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 Salla Ruskamo. Salla Ruskamo 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.
Nguyen, Giang Thi Tuyet, et al.. (2023). Conserved intramolecular networks in GDAP1 are closely connected to CMT-linked mutations and protein stability. PLoS ONE. 18(4). e0284532–e0284532. 2 indexed citations
2.
3.
Ruskamo, Salla, Arne Raasakka, Jan Skov Pedersen, et al.. (2022). Human myelin proteolipid protein structure and lipid bilayer stacking. Cellular and Molecular Life Sciences. 79(8). 419–419. 21 indexed citations
4.
Laulumaa, Saara, et al.. (2021). Human myelin protein P2: from crystallography to time‐lapse membrane imaging and neuropathy‐associated variants. FEBS Journal. 288(23). 6716–6735. 10 indexed citations
5.
Tuusa, Jussi, M. Kristian Koski, Salla Ruskamo, & Kaisa Tasanen. (2020). The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment. Amino Acids. 52(4). 619–627. 4 indexed citations
6.
Ruskamo, Salla, Julia Kowal, Arne Raasakka, et al.. (2020). Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice. Journal of Biological Chemistry. 295(26). 8692–8705. 11 indexed citations
7.
Raasakka, Arne, Salla Ruskamo, Julia Kowal, et al.. (2019). Molecular structure and function of myelin protein P0 in membrane stacking. Scientific Reports. 9(1). 642–642. 39 indexed citations
8.
Laulumaa, Saara, Arne Raasakka, Guillaume Brysbaert, et al.. (2018). Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins. BMC Structural Biology. 18(1). 8–8. 15 indexed citations
9.
Raasakka, Arne, Salla Ruskamo, Julia Kowal, et al.. (2017). Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line. Scientific Reports. 7(1). 4974–4974. 56 indexed citations
10.
Ruskamo, Salla, Anne Baumann, Arne Raasakka, et al.. (2017). Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2. Scientific Reports. 7(1). 6510–6510. 26 indexed citations
11.
Raasakka, Arne, et al.. (2015). The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. Amino Acids. 47(8). 1567–1577. 7 indexed citations
12.
Sethi, Ritika, Helena Tossavainen, Mikko Ylilauri, et al.. (2014). A Novel Structural Unit in the N-terminal Region of Filamins. Journal of Biological Chemistry. 289(12). 8588–8598. 17 indexed citations
13.
Zenker, Jennifer, Mark Stettner, Salla Ruskamo, et al.. (2014). A role of peripheral myelin protein 2 in lipid homeostasis of myelinating schwann cells. Glia. 62(9). 1502–1512. 56 indexed citations
14.
Ruskamo, Salla, Ravi Prakash Yadav, Satyan Sharma, et al.. (2013). Atomic resolution view into the structure–function relationships of the human myelin peripheral membrane protein P2. Acta Crystallographica Section D Biological Crystallography. 70(1). 165–176. 38 indexed citations
15.
Han, Huijong, Matti Myllykoski, Salla Ruskamo, Chaozhan Wang, & Petri Kursula. (2013). Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules. BioFactors. 39(3). 233–241. 65 indexed citations
16.
Laulumaa, Saara, et al.. (2012). Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(11). 1359–1362. 10 indexed citations
17.
Pentikäinen, Ulla, Pengju Jiang, Heikki Takala, et al.. (2011). Assembly of a Filamin Four-domain Fragment and the Influence of Splicing Variant-1 on the Structure. Journal of Biological Chemistry. 286(30). 26921–26930. 16 indexed citations
18.
Ruskamo, Salla & Jari Ylänne. (2009). Structure of the human filamin A actin-binding domain. Acta Crystallographica Section D Biological Crystallography. 65(11). 1217–1221. 13 indexed citations
19.
Ruskamo, Salla, Petr V. Konarev, Dmitri I. Svergun, et al.. (2009). Atomic Structures of Two Novel Immunoglobulin-like Domain Pairs in the Actin Cross-linking Protein Filamin. Journal of Biological Chemistry. 284(37). 25450–25458. 46 indexed citations
20.
Lad, Yatish, Pengju Jiang, Salla Ruskamo, et al.. (2008). Structural Basis of the Migfilin-Filamin Interaction and Competition with Integrin β Tails. Journal of Biological Chemistry. 283(50). 35154–35163. 92 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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