Ritva Heljäsvaara

3.7k total citations
65 papers, 2.7k citations indexed

About

Ritva Heljäsvaara is a scholar working on Molecular Biology, Immunology and Allergy and Cancer Research. According to data from OpenAlex, Ritva Heljäsvaara has authored 65 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 33 papers in Immunology and Allergy and 15 papers in Cancer Research. Recurrent topics in Ritva Heljäsvaara's work include Cell Adhesion Molecules Research (33 papers), Angiogenesis and VEGF in Cancer (19 papers) and Protease and Inhibitor Mechanisms (12 papers). Ritva Heljäsvaara is often cited by papers focused on Cell Adhesion Molecules Research (33 papers), Angiogenesis and VEGF in Cancer (19 papers) and Protease and Inhibitor Mechanisms (12 papers). Ritva Heljäsvaara collaborates with scholars based in Finland, Norway and United States. Ritva Heljäsvaara's co-authors include Taina Pihlajaniemi, Tuula Salo, Timo Sorsa, Pia Nyberg, Marko Rehn, Mari Aikio, Kati Richter, Thomas Kietzmann, Pia Heikkilä and Raija Sormunen and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Clinical Investigation.

In The Last Decade

Ritva Heljäsvaara

65 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ritva Heljäsvaara Finland 31 1.3k 591 548 546 418 65 2.7k
Liisa Nissinen Finland 32 1.2k 0.9× 683 1.2× 492 0.9× 537 1.0× 439 1.1× 74 2.8k
Ryoji Tsuboi Japan 27 1.2k 0.9× 531 0.9× 338 0.6× 338 0.6× 495 1.2× 90 2.8k
David W. Griggs United States 22 993 0.8× 265 0.4× 423 0.8× 434 0.8× 266 0.6× 39 2.5k
Paola Zigrino Germany 37 1.5k 1.2× 818 1.4× 1.0k 1.9× 730 1.3× 556 1.3× 86 3.5k
Hervé Emonard France 36 1000 0.8× 1.4k 2.4× 827 1.5× 570 1.0× 440 1.1× 81 3.2k
B. Voß Germany 23 1.5k 1.2× 343 0.6× 579 1.1× 460 0.8× 547 1.3× 80 2.9k
Caroline E. Ford Australia 27 1.0k 0.8× 361 0.6× 647 1.2× 253 0.5× 171 0.4× 73 2.0k
Olivier Lefèbvre France 33 1.7k 1.3× 934 1.6× 904 1.6× 730 1.3× 468 1.1× 68 3.6k
Sakuhei Fujiwara Japan 26 830 0.7× 237 0.4× 266 0.5× 699 1.3× 786 1.9× 141 2.6k
William T. Roswit United States 22 680 0.5× 610 1.0× 651 1.2× 338 0.6× 251 0.6× 25 2.2k

Countries citing papers authored by Ritva Heljäsvaara

Since Specialization
Citations

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

Fields of papers citing papers by Ritva Heljäsvaara

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ritva Heljäsvaara

This figure shows the co-authorship network connecting the top 25 collaborators of Ritva Heljäsvaara. A scholar is included among the top collaborators of Ritva Heljäsvaara 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 Ritva Heljäsvaara. Ritva Heljäsvaara 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.
Pihlajaniemi, Taina, et al.. (2023). Collagens Regulating Adipose Tissue Formation and Functions. Biomedicines. 11(5). 1412–1412. 25 indexed citations
2.
Izzi, Valerio, Hellevi Peltoketo, Saila Kauppila, et al.. (2023). Targeting collagen XVIII improves the efficiency of ErbB inhibitors in breast cancer models. Journal of Clinical Investigation. 133(18). 11 indexed citations
3.
Vicente, David, Kari A. Mäkelä, Mikko Finnilä, et al.. (2020). Lack of collagen XVIII leads to lipodystrophy and perturbs hepatic glucose and lipid homeostasis. The Journal of Physiology. 598(16). 3373–3393. 14 indexed citations
4.
Izzi, Valerio, et al.. (2019). Pan-Cancer analysis of the expression and regulation of matrisome genes across 32 tumor types. SHILAP Revista de lepidopterología. 1. 100004–100004. 29 indexed citations
5.
Izzi, Valerio, Ritva Heljäsvaara, Anne Heikkinen, et al.. (2019). Exploring the roles of MACIT and multiplexin collagens in stem cells and cancer. Seminars in Cancer Biology. 62. 134–148. 24 indexed citations
6.
Åström, Pirjo, Ritva Heljäsvaara, Pia Nyberg, Ahmed Al‐Samadi, & Tuula Salo. (2018). Human Tumor Tissue-Based 3D In Vitro Invasion Assays. Methods in molecular biology. 1731. 213–221. 13 indexed citations
7.
Izzi, Valerio, et al.. (2017). Expression of a specific extracellular matrix signature is a favorable prognostic factor in acute myeloid leukemia. Leukemia Research Reports. 9. 9–13. 10 indexed citations
8.
Heljäsvaara, Ritva, Mari Aikio, Heli Ruotsalainen, & Taina Pihlajaniemi. (2016). Collagen XVIII in tissue homeostasis and dysregulation — Lessons learned from model organisms and human patients. Matrix Biology. 57-58. 55–75. 102 indexed citations
9.
Karppinen, Sanna‐Maria, Ritva Heljäsvaara, Pilvi Riihilä, et al.. (2015). Collagens XV and XVIII show different expression and localisation in cutaneous squamous cell carcinoma: type XV appears in tumor stroma, while XVIII becomes upregulated in tumor cells and lost from microvessels. Experimental Dermatology. 25(5). 348–354. 29 indexed citations
10.
Farshchian, Mehdi, Liisa Nissinen, Elina Siljamäki, et al.. (2015). EphB2 Promotes Progression of Cutaneous Squamous Cell Carcinoma. Journal of Investigative Dermatology. 135(7). 1882–1892. 45 indexed citations
11.
Holopainen, Tanja, Wei Zheng, Ritva Heljäsvaara, et al.. (2012). Deletion of the Endothelial Bmx Tyrosine Kinase Decreases Tumor Angiogenesis and Growth. Cancer Research. 72(14). 3512–3521. 27 indexed citations
12.
Perkins, Gavin D., Nazim Nathani, Alex Richter, et al.. (2009). Type XVIII collagen degradation products in acute lung injury. Critical Care. 13(2). R52–R52. 11 indexed citations
13.
Lavergne, Elise, Harri Elamaa, Ritva Heljäsvaara, et al.. (2008). A Cryptic Frizzled Module in Cell Surface Collagen 18 Inhibits Wnt/β−Catenin Signaling. PLoS ONE. 3(4). e1878–e1878. 44 indexed citations
14.
Richter, Alex, Sridhar Rathinam, Lorraine Harper, et al.. (2008). Soluble endostatin is a novel inhibitor of epithelial repair in idiopathic pulmonary fibrosis. Thorax. 64(2). 156–161. 49 indexed citations
15.
Sormunen, Raija, et al.. (2008). Lack of collagen XVIII accelerates cutaneous wound healing, while overexpression of its endostatin domain leads to delayed healing. Matrix Biology. 27(6). 535–546. 47 indexed citations
16.
Parikka, Mataleena, Tiina Kainulainen, Marko Rehn, et al.. (2006). Collagen XVIII modulation is altered during progression of oral dysplasia and carcinoma. Journal of Oral Pathology and Medicine. 36(1). 35–42. 11 indexed citations
17.
Määttã, Marko, Ritva Heljäsvaara, Taina Pihlajaniemi, & Marita Uusitalo. (2006). Collagen XVIII/endostatin shows a ubiquitous distribution in human ocular tissues and endostatin-containing fragments accumulate in ocular fluid samples. Graefe s Archive for Clinical and Experimental Ophthalmology. 245(1). 74–81. 33 indexed citations
18.
Gervásio, Othon, Cristina Guatimosim, Ritva Heljäsvaara, et al.. (2005). Collagen XVIII/endostatin is associated with the epithelial–mesenchymal transformation in the atrioventricular valves during cardiac development. Developmental Dynamics. 235(1). 132–142. 33 indexed citations
19.
Pirilä, Emma, Andrew B. Sharabi, Tuula Salo, et al.. (2003). Matrix metalloproteinases process the laminin-5 γ2-chain and regulate epithelial cell migration. Biochemical and Biophysical Research Communications. 303(4). 1012–1017. 91 indexed citations
20.
Risco, Cristina, Juan Rodríguez, Walter E. Demkowicz, et al.. (1999). The Vaccinia Virus 39-kDa Protein Forms a Stable Complex with the p4a/4a Major Core Protein Early in Morphogenesis. Virology. 265(2). 375–386. 35 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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