Marja Makarow

2.6k total citations
51 papers, 2.0k citations indexed

About

Marja Makarow is a scholar working on Molecular Biology, Cell Biology and Immunology. According to data from OpenAlex, Marja Makarow has authored 51 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 30 papers in Cell Biology and 7 papers in Immunology. Recurrent topics in Marja Makarow's work include Endoplasmic Reticulum Stress and Disease (23 papers), Fungal and yeast genetics research (20 papers) and Heat shock proteins research (17 papers). Marja Makarow is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (23 papers), Fungal and yeast genetics research (20 papers) and Heat shock proteins research (17 papers). Marja Makarow collaborates with scholars based in Finland, United States and Italy. Marja Makarow's co-authors include Eija Jämsä, Silvia Brambillasca, Johan C. Kapteyn, H. van den Ende, Frans M. Klis, Monica Yabal, Nica Borgese, Eeva Sievi, Marjo Simonen and Patrick Russo and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Cell Biology.

In The Last Decade

Marja Makarow

51 papers receiving 1.9k citations

Peers

Marja Makarow
Claudia Abeijón United States
Daniel J. Kelleher United States
Michael J. Holland United States
T J Koerner United States
Neta Dean United States
Carl T. Yamashiro United States
Claudia Abeijón United States
Marja Makarow
Citations per year, relative to Marja Makarow Marja Makarow (= 1×) peers Claudia Abeijón

Countries citing papers authored by Marja Makarow

Since Specialization
Citations

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

Fields of papers citing papers by Marja Makarow

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Marja Makarow

This figure shows the co-authorship network connecting the top 25 collaborators of Marja Makarow. A scholar is included among the top collaborators of Marja Makarow 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 Marja Makarow. Marja Makarow 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.
Brambillasca, Silvia, Monica Yabal, Marja Makarow, & Nica Borgese. (2006). Unassisted translocation of large polypeptide domains across phospholipid bilayers. The Journal of Cell Biology. 175(5). 767–777. 95 indexed citations
2.
Makarow, Marja, Anna‐Liisa Hänninen, Taina Suntio, & Ricardo Bastos. (2005). Production of Heterologous Proteins in Yeast With the Aid of the Hsp150D Carrier. Humana Press eBooks. 313. 333–344. 2 indexed citations
3.
Karhinen, Leena, Ricardo Bastos, Eija Jokitalo, & Marja Makarow. (2005). Endoplasmic Reticulum Exit of a Secretory Glycoprotein in the Absence of Sec24p Family Proteins in Yeast. Traffic. 6(7). 562–574. 15 indexed citations
4.
Brambillasca, Silvia, Monica Yabal, Paolo Soffientini, et al.. (2005). Transmembrane topogenesis of a tail‐anchored protein is modulated by membrane lipid composition. The EMBO Journal. 24(14). 2533–2542. 107 indexed citations
5.
Salo, Hanna, Eeva Sievi, Taina Suntio, et al.. (2004). Co-expression of two mammalian glycosyltransferases in the yeast cell wall allows synthesis of sLex. FEMS Yeast Research. 5(4-5). 341–350. 9 indexed citations
6.
Hänninen, Anna‐Liisa, et al.. (2004). Upregulation of the Hsp104 chaperone at physiological temperature during recovery from thermal insult. Molecular Microbiology. 52(1). 217–225. 17 indexed citations
7.
Sievi, Eeva, Anna‐Liisa Hänninen, Hanna Salo, Vijay Kumar, & Marja Makarow. (2003). Validation of the Hsp150 Polypeptide Carrier and HSP150 Promoter in Expression of Rat α2,3-Sialyltransferase in Yeasts. Biotechnology Progress. 19(4). 1368–1371. 10 indexed citations
8.
Yabal, Monica, Silvia Brambillasca, Paolo Soffientini, et al.. (2003). Translocation of the C Terminus of a Tail-anchored Protein across the Endoplasmic Reticulum Membrane in Yeast Mutants Defective in Signal Peptide-driven Translocation. Journal of Biological Chemistry. 278(5). 3489–3496. 53 indexed citations
9.
Suntio, Taina, et al.. (2002). Selective Protein Exit from Yeast Endoplasmic Reticulum in Absence of Functional COPII Coat Component Sec13p. Molecular Biology of the Cell. 13(12). 4130–4140. 28 indexed citations
10.
Visapää, Ilona, Vineta Fellman, Jouni Vesa, et al.. (2002). GRACILE Syndrome, a Lethal Metabolic Disorder with Iron Overload, Is Caused by a Point Mutation in BCS1L. The American Journal of Human Genetics. 71(4). 863–876. 199 indexed citations
11.
Kapteyn, Johan C., Lois L. Hoyer, Wally H. Müller, et al.. (2000). The cell wall architecture of Candida albicans wild‐type cells and cell wall‐defective mutants. Molecular Microbiology. 35(3). 601–611. 276 indexed citations
12.
Kapteyn, Johan C., Piet van Egmond, Eeva Sievi, et al.. (1999). The contribution of the O‐glycosylated protein Pir2p/Hsp150 to the construction of the yeast cell wall in wild‐type cells and β1,6‐glucan‐deficient mutants. Molecular Microbiology. 31(6). 1835–1844. 145 indexed citations
13.
Sievi, Eeva, Jari Helin, Riikka Heikinheimo, & Marja Makarow. (1998). Glycan engineering of proteins with whole living yeast cells expressing rat liver α2,3‐sialytransferase in the porous cell wall. FEBS Letters. 441(2). 177–180. 8 indexed citations
14.
Suntio, Taina, et al.. (1998). Folding of Active β-Lactamase in the Yeast Cytoplasm before Translocation into the Endoplasmic Reticulum. Molecular Biology of the Cell. 9(4). 817–827. 28 indexed citations
15.
Makarow, Marja, et al.. (1998). Different degradation pathways for heterologous glycoproteins in yeast. FEBS Letters. 429(2). 162–166. 55 indexed citations
16.
Vihinen, Helena, et al.. (1996). Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae. FEBS Letters. 383(3). 255–258. 6 indexed citations
17.
Jämsä, Eija, Marjo Simonen, & Marja Makarow. (1994). Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent. Yeast. 10(3). 355–370. 101 indexed citations
18.
Russo, Patrick, et al.. (1992). A heat shock gene from Saccharomyces cerevisiae encoding a secretory glycoprotein.. Proceedings of the National Academy of Sciences. 89(9). 3671–3675. 127 indexed citations
19.
Makarow, Marja, et al.. (1991). Uptake of endocytic markers into mitotic yeast cells. FEBS Letters. 282(1). 166–169. 5 indexed citations
20.
Louhelainen, Jari, et al.. (1989). Post‐translational modifications in mitotic yeast cells. European Journal of Biochemistry. 184(1). 165–172. 12 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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