Sakari Kellokumpu

3.5k total citations
73 papers, 2.8k citations indexed

About

Sakari Kellokumpu is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Sakari Kellokumpu has authored 73 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Molecular Biology, 32 papers in Cell Biology and 13 papers in Physiology. Recurrent topics in Sakari Kellokumpu's work include Glycosylation and Glycoproteins Research (26 papers), Cellular transport and secretion (20 papers) and Erythrocyte Function and Pathophysiology (10 papers). Sakari Kellokumpu is often cited by papers focused on Glycosylation and Glycoproteins Research (26 papers), Cellular transport and secretion (20 papers) and Erythrocyte Function and Pathophysiology (10 papers). Sakari Kellokumpu collaborates with scholars based in Finland, United States and Sweden. Sakari Kellokumpu's co-authors include Antti Hassinen, Hannu Rajaniemi, Antti Rivinoja, Ilmo Kellokumpu, Nina Kokkonen, Raija Sormunen, Tuomo Glumoff, Marko Suokas, François M. Pujol and Roland Baron and has published in prestigious journals such as Science, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Sakari Kellokumpu

73 papers receiving 2.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sakari Kellokumpu Finland 34 1.8k 792 391 275 251 73 2.8k
James S. Norris United States 39 3.0k 1.7× 656 0.8× 498 1.3× 199 0.7× 358 1.4× 126 4.5k
Eurı́dice Carmona Canada 28 1.3k 0.7× 314 0.4× 312 0.8× 104 0.4× 231 0.9× 60 2.5k
Gennaro Citro Italy 36 2.2k 1.2× 449 0.6× 552 1.4× 123 0.4× 266 1.1× 147 4.3k
Pradipta Ghosh United States 40 3.4k 1.9× 1.5k 1.9× 570 1.5× 252 0.9× 578 2.3× 146 5.3k
Johannes Graumann Germany 36 4.0k 2.3× 902 1.1× 382 1.0× 292 1.1× 421 1.7× 105 5.4k
Doris A. Wall United States 24 1.5k 0.8× 642 0.8× 286 0.7× 76 0.3× 330 1.3× 36 2.8k
Terutoshi Kimura Japan 29 2.3k 1.3× 680 0.9× 247 0.6× 352 1.3× 585 2.3× 119 3.4k
Harald S. Conradt Germany 37 2.3k 1.3× 233 0.3× 533 1.4× 463 1.7× 163 0.6× 72 3.2k
Þorkell Andrésson United States 31 2.3k 1.3× 486 0.6× 417 1.1× 161 0.6× 155 0.6× 75 3.5k
László Gráf Hungary 34 2.6k 1.5× 318 0.4× 490 1.3× 94 0.3× 331 1.3× 115 4.1k

Countries citing papers authored by Sakari Kellokumpu

Since Specialization
Citations

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

Fields of papers citing papers by Sakari Kellokumpu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sakari Kellokumpu

This figure shows the co-authorship network connecting the top 25 collaborators of Sakari Kellokumpu. A scholar is included among the top collaborators of Sakari Kellokumpu 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 Sakari Kellokumpu. Sakari Kellokumpu 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.
Dierker, Tabea, et al.. (2022). A dominant negative splice variant of the heparan sulfate biosynthesis enzyme NDST1 reduces heparan sulfate sulfation. Glycobiology. 32(6). 518–528. 10 indexed citations
2.
Harrus, Déborah, Guillaume Brysbaert, Marc F. Lensink, et al.. (2019). Assembly of B4GALT1/ST6GAL1 heteromers in the Golgi membranes involves lateral interactions via highly charged surface domains. Journal of Biological Chemistry. 294(39). 14383–14393. 34 indexed citations
3.
Mennerich, Daniela, Anatoly Samoylenko, Elitsa Y. Dimova, et al.. (2019). The Pro-Oncogenic Adaptor CIN85 Acts as an Inhibitory Binding Partner of Hypoxia-Inducible Factor Prolyl Hydroxylase 2. Cancer Research. 79(16). 4042–4056. 9 indexed citations
4.
Sosicka, Paulina, et al.. (2019). N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme–multi-transporter assemblies in golgi membranes in vivo. Cellular and Molecular Life Sciences. 76(9). 1821–1832. 43 indexed citations
5.
Harrus, Déborah, et al.. (2018). The dimeric structure of wild-type human glycosyltransferase B4GalT1. PLoS ONE. 13(10). e0205571–e0205571. 20 indexed citations
6.
Kokkonen, Nina, Antti Hassinen, Déborah Harrus, et al.. (2018). Abnormal Golgi pH Homeostasis in Cancer Cells Impairs Apical Targeting of Carcinoembryonic Antigen by Inhibiting Its Glycosyl-Phosphatidylinositol Anchor-Mediated Association with Lipid Rafts. Antioxidants and Redox Signaling. 30(1). 5–21. 19 indexed citations
7.
Harrus, Déborah, Sakari Kellokumpu, & Tuomo Glumoff. (2017). Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers. Cellular and Molecular Life Sciences. 75(5). 833–848. 19 indexed citations
8.
Deen, Ashik Jawahar, Uma Thanigai Arasu, Sanna Pasonen‐Seppänen, et al.. (2016). UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression. Cellular and Molecular Life Sciences. 73(16). 3183–3204. 49 indexed citations
9.
Kellokumpu, Sakari, Antti Hassinen, & Tuomo Glumoff. (2015). Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized. Cellular and Molecular Life Sciences. 73(2). 305–325. 77 indexed citations
10.
Trusch, Franziska, et al.. (2015). Heterodimers of Tyrosylprotein Sulfotransferases Suggest Existence of a Higher Organization Level of Transferases in the Membrane of the trans-Golgi Apparatus. Journal of Molecular Biology. 427(6). 1404–1412. 11 indexed citations
11.
Samoylenko, Anatoly, et al.. (2013). Nutritional Countermeasures Targeting Reactive Oxygen Species in Cancer: From Mechanisms to Biomarkers and Clinical Evidence. Antioxidants and Redox Signaling. 19(17). 2157–2196. 80 indexed citations
12.
Alanen, Heli I., Richard A. Williamson, Mark J. Howard, et al.. (2006). ERp27, a New Non-catalytic Endoplasmic Reticulum-located Human Protein Disulfide Isomerase Family Member, Interacts with ERp57. Journal of Biological Chemistry. 281(44). 33727–33738. 46 indexed citations
13.
Egea, Gustavo, et al.. (2004). The AE2 anion exchanger is necessary for the structural integrity of the Golgi apparatus in mammalian cells. FEBS Letters. 564(1-2). 97–103. 17 indexed citations
14.
Alanen, Heli I., Richard A. Williamson, Mark J. Howard, et al.. (2003). Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member. Journal of Biological Chemistry. 278(31). 28912–28920. 80 indexed citations
15.
Kellokumpu, Sakari, Raija Sormunen, & Ilmo Kellokumpu. (2002). Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra‐Golgi pH. FEBS Letters. 516(1-3). 217–224. 152 indexed citations
16.
Suokas, Marko, et al.. (2001). Identification of the Full-length AE2 (AE2a) Isoform as the Golgi-associated Anion Exchanger in Fibroblasts. Journal of Histochemistry & Cytochemistry. 49(2). 259–269. 29 indexed citations
17.
Vaarala, Markku H., Katja Porvari, Sakari Kellokumpu, Atte P. Kyllönen, & Pirkko Vihko. (2001). Expression of transmembrane serine protease TMPRSS2 in mouse and human tissues. The Journal of Pathology. 193(1). 134–140. 144 indexed citations
18.
Kellokumpu, Ilmo, Leif C. Andersson, & Sakari Kellokumpu. (1997). Detection of colorectal neoplasia with peanut-agglutinin(PNA)-reactive carbohydrate structures in rectal mucus. International Journal of Cancer. 74(6). 648–653. 5 indexed citations
19.
Parkkila, Seppo, Anna‐Kaisa Parkkila, Tatu Juvonen, et al.. (1996). Membrane–Bound Carbonic Anhydrase Iv Is Expressed in the Luminal Plasma Membrane of the Human Gallbladder Epithelium. Hepatology. 24(5). 1104–1108. 54 indexed citations
20.
Parkkila, Seppo, Hannu Rajaniemi, & Sakari Kellokumpu. (1993). Polarized Expression of a Band 3-Related Protein in Mammalian Sperm Cells. Biology of Reproduction. 49(2). 326–331. 41 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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