Åke P. Elhammer

2.2k total citations
47 papers, 1.8k citations indexed

About

Åke P. Elhammer is a scholar working on Molecular Biology, Organic Chemistry and Immunology. According to data from OpenAlex, Åke P. Elhammer has authored 47 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 14 papers in Organic Chemistry and 9 papers in Immunology. Recurrent topics in Åke P. Elhammer's work include Glycosylation and Glycoproteins Research (26 papers), Carbohydrate Chemistry and Synthesis (13 papers) and Metabolism and Genetic Disorders (5 papers). Åke P. Elhammer is often cited by papers focused on Glycosylation and Glycoproteins Research (26 papers), Carbohydrate Chemistry and Synthesis (13 papers) and Metabolism and Genetic Disorders (5 papers). Åke P. Elhammer collaborates with scholars based in United States, Sweden and Japan. Åke P. Elhammer's co-authors include Paul A. Aeed, Stuart Kornfeld, Claire Davis, David W. Russell, Wolfgang J. Schneider, Joseph L. Goldstein, Ferenc J. Kézdy, Stuart Kornfeld, Fred L. Homa and Li Ma and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Cell Biology and Biochemistry.

In The Last Decade

Åke P. Elhammer

47 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Åke P. Elhammer United States 24 1.3k 416 414 283 213 47 1.8k
Thayer White United States 22 1.5k 1.1× 422 1.0× 318 0.8× 288 1.0× 202 0.9× 30 2.7k
Ganesa Yogeeswaran United States 22 1.3k 1.0× 546 1.3× 208 0.5× 108 0.4× 222 1.0× 38 2.0k
Harald S. Conradt Germany 37 2.3k 1.8× 533 1.3× 463 1.1× 145 0.5× 233 1.1× 72 3.2k
Maria A. Kukuruzinska United States 30 1.9k 1.5× 358 0.9× 239 0.6× 126 0.4× 440 2.1× 64 2.5k
James I. Rearick United States 22 1.6k 1.2× 336 0.8× 558 1.3× 110 0.4× 327 1.5× 29 2.0k
Keith R. Marotti United States 19 1.3k 1.0× 702 1.7× 174 0.4× 406 1.4× 150 0.7× 36 2.8k
Aristotelis Antonopoulos United Kingdom 30 1.5k 1.2× 744 1.8× 491 1.2× 102 0.4× 195 0.9× 58 2.2k
Akira Kobata Japan 26 1.7k 1.4× 472 1.1× 579 1.4× 122 0.4× 202 0.9× 59 2.2k
Timothy A. Fritz United States 18 1.5k 1.2× 464 1.1× 643 1.6× 70 0.2× 351 1.6× 21 1.8k
Satoshi Mizuno Japan 22 1.1k 0.9× 360 0.9× 98 0.2× 90 0.3× 168 0.8× 74 1.8k

Countries citing papers authored by Åke P. Elhammer

Since Specialization
Citations

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

Fields of papers citing papers by Åke P. Elhammer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Åke P. Elhammer. 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 Åke P. Elhammer. The network helps show where Åke P. Elhammer may publish in the future.

Co-authorship network of co-authors of Åke P. Elhammer

This figure shows the co-authorship network connecting the top 25 collaborators of Åke P. Elhammer. A scholar is included among the top collaborators of Åke P. Elhammer 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 Åke P. Elhammer. Åke P. Elhammer 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
3.
Gerken, Thomas, Jiexin Zhang, Jessica Levine, & Åke P. Elhammer. (2002). Mucin Core O-Glycosylation Is Modulated by Neighboring Residue Glycosylation Status. Journal of Biological Chemistry. 277(51). 49850–49862. 35 indexed citations
4.
Tenno, Mari, et al.. (2002). Identification of two cysteine residues involved in the binding of UDP‐GalNAc to UDP‐GalNAc:polypeptide N‐acetylgalactosaminyltransferase 1 (GalNAc‐T1). European Journal of Biochemistry. 269(17). 4308–4316. 22 indexed citations
5.
Tenno, Mari, Ferenc J. Kézdy, Åke P. Elhammer, & Akira Kurosaka. (2002). Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1. Biochemical and Biophysical Research Communications. 298(5). 755–759. 24 indexed citations
6.
Tenno, Mari, et al.. (2002). The Lectin Domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase 1 Is Involved in O-Glycosylation of a Polypeptide with Multiple Acceptor Sites. Journal of Biological Chemistry. 277(49). 47088–47096. 38 indexed citations
7.
Kézdy, Ferenc J., et al.. (2002). An efficient assay for dolichyl phosphate–mannose: protein O-mannosyltransferase. Analytical Biochemistry. 307(2). 273–279. 2 indexed citations
8.
Li, Ling, et al.. (2001). Characterization of Glycoprotein Ligands for P-Selectin on a Human Small Cell Lung Cancer Cell Line NCI-H345. Biochemical and Biophysical Research Communications. 288(3). 637–644. 18 indexed citations
9.
Elhammer, Åke P., et al.. (1999). The acceptor specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycoconjugate Journal. 16(2). 171–180. 46 indexed citations
10.
Colca, Jerry R., et al.. (1999). Properties of native and in vitro glycosylated forms of the glucagon-like peptide-1 receptor antagonist exendin (9–39). Metabolism. 48(6). 716–724. 9 indexed citations
11.
Smith, Mark A., et al.. (1996). Quantitative solubilization and analysis of insoluble paired helical filaments from alzheimer disease. Brain Research. 717(1-2). 99–108. 48 indexed citations
12.
Homa, Fred L., et al.. (1995). Conversion of a Bovine UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase, to a Soluble, Secreted Enzyme, and Expression in Sf9 Cells. Protein Expression and Purification. 6(2). 141–148. 12 indexed citations
13.
Baker, Carolyn A., et al.. (1995). cDNA Cloning, Expression, and Chromosomal Localization of a Human UDP-GalNAc: Polypeptide, N-Acetylgalactosaminyltransferase. The Journal of Biochemistry. 118(3). 568–574. 16 indexed citations
14.
Aeed, Paul A., et al.. (1993). Characterization of the oligosaccharide structures on bee venom phospholipase A2. Carbohydrate Research. 247. 291–297. 7 indexed citations
15.
Wathen, Michael W., Paul A. Aeed, & Åke P. Elhammer. (1991). Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in insect cell line Sf9. Biochemistry. 30(11). 2863–2868. 37 indexed citations
16.
Thomsen, Darrell R., Leonard Post, & Åke P. Elhammer. (1990). Structure of O‐glycosidically linked oligosaccharides synthesized by the insect cell line Sf9. Journal of Cellular Biochemistry. 43(1). 67–79. 51 indexed citations
17.
Olsson, Mariann, et al.. (1989). The influence of di(2-ethylhexyl)phthalate on protein turnover in rat liver. Toxicology Letters. 48(2). 185–192. 6 indexed citations
19.
Elhammer, Åke P., Elisabeth Peterson, & Gustav Dallner. (1983). Distribution and transport of apo- and holocytochrome b5 in the endoplasmic reticulum of rat liver. Biochimica et Biophysica Acta (BBA) - Biomembranes. 730(1). 76–84. 5 indexed citations
20.
Elhammer, Åke P., H. Svensson, Francesco Autuori, & Gustav Dallner. (1975). Biogenesis of microsomal membrane glycoproteins in rat liver. III. Release of glycoproteins from the Golgi fraction and their transfer to microsomal membranes.. The Journal of Cell Biology. 67(3). 715–724. 21 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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