Rolf Stricker

1.3k total citations
37 papers, 1.1k citations indexed

About

Rolf Stricker is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Rolf Stricker has authored 37 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 16 papers in Cell Biology and 10 papers in Cellular and Molecular Neuroscience. Recurrent topics in Rolf Stricker's work include Cellular transport and secretion (14 papers), Protein Kinase Regulation and GTPase Signaling (11 papers) and Peptidase Inhibition and Analysis (8 papers). Rolf Stricker is often cited by papers focused on Cellular transport and secretion (14 papers), Protein Kinase Regulation and GTPase Signaling (11 papers) and Peptidase Inhibition and Analysis (8 papers). Rolf Stricker collaborates with scholars based in Germany, Russia and United States. Rolf Stricker's co-authors include Georg Reiser, Hong Wang, Tamara Azarashvili, Joachim J. Ubl, Yulia Baburina, Olga Krestinina, Dmitry Grachev, Theodor Hanck, Yingfei Wang and Weibo Luo and has published in prestigious journals such as Journal of Biological Chemistry, Biochemical Journal and Brain Research.

In The Last Decade

Rolf Stricker

37 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Rolf Stricker Germany	18	647	207	185	160	142	37	1.1k
Irina Lonskaya United States	19	642 1.0×	129 0.6×	322 1.7×	110 0.7×	327 2.3×	21	1.5k
Yasuhiro Kita Japan	21	666 1.0×	76 0.4×	144 0.8×	80 0.5×	416 2.9×	47	1.5k
Joachim J. Ubl Germany	17	536 0.8×	76 0.4×	285 1.5×	374 2.3×	107 0.8×	20	1.0k
Mie Nakaya Japan	7	1.1k 1.7×	165 0.8×	276 1.5×	35 0.2×	115 0.8×	8	1.4k
Chen-Hsiung Yeh United States	15	941 1.5×	82 0.4×	378 2.0×	136 0.8×	243 1.7×	35	1.5k
Daniel Palmer United States	19	1.4k 2.2×	169 0.8×	341 1.8×	225 1.4×	356 2.5×	27	2.1k
Koji Mizuno Japan	16	742 1.1×	186 0.9×	215 1.2×	33 0.2×	195 1.4×	47	1.1k
Shelley B. Hooks United States	22	1.2k 1.8×	207 1.0×	189 1.0×	25 0.2×	224 1.6×	41	1.6k
Takatoshi Soga Japan	13	773 1.2×	61 0.3×	237 1.3×	34 0.2×	235 1.7×	21	1.5k
Kristina S. Kovacina United States	16	1.5k 2.3×	240 1.2×	105 0.6×	39 0.2×	379 2.7×	18	2.0k

Countries citing papers authored by Rolf Stricker

Since Specialization

Citations

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

Fields of papers citing papers by Rolf Stricker

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rolf Stricker

This figure shows the co-authorship network connecting the top 25 collaborators of Rolf Stricker. A scholar is included among the top collaborators of Rolf Stricker 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 Rolf Stricker. Rolf Stricker is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Baburina, Yulia, Tamara Azarashvili, Dmitry Grachev, et al.. (2015). Mitochondrial 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNP) interacts with mPTP modulators and functional complexes (I–V) coupled with release of apoptotic factors. Neurochemistry International. 90. 46–55. 36 indexed citations

Krestinina, Olga, Tamara Azarashvili, Yulia Baburina, et al.. (2014). In aging, the vulnerability of rat brain mitochondria is enhanced due to reduced level of 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNP) and subsequently increased permeability transition in brain mitochondria in old animals. Neurochemistry International. 80. 41–50. 39 indexed citations

Azarashvili, Tamara, Olga Krestinina, Dmitry Grachev, et al.. (2014). Identification of phosphorylated form of 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) as 46 kDa phosphoprotein in brain non-synaptic mitochondria overloaded by calcium. Journal of Bioenergetics and Biomembranes. 46(2). 135–145. 13 indexed citations

Zhu, Zhihui, et al.. (2014). The intracellular carboxyl tail of the PAR-2 receptor controls intracellular signaling and cell death. Cell and Tissue Research. 359(3). 817–827. 3 indexed citations

Strukova, S. M., et al.. (2013). NF-κB-dependent and -independent pathways in the protective effects of activated protein C in hippocampal and cortical neurons at excitotoxicity. Neurochemistry International. 63(2). 101–111. 12 indexed citations

Bernstein, Hans‐Gert, Rolf Stricker, Henrik Dobrowolny, et al.. (2013). Nardilysin in human brain diseases: both friend and foe. Amino Acids. 45(2). 269–278. 10 indexed citations

Stricker, Rolf, et al.. (2011). Retinoic acid-induced upregulation of the metalloendopeptidase nardilysin is accelerated by co-expression of the brain-specific protein p42IP4 (centaurin α1; ADAP1) in neuroblastoma cells. Neurochemistry International. 59(6). 936–944. 4 indexed citations

Azarashvili, Tamara, Rolf Stricker, & Georg Reiser. (2010). The mitochondria permeability transition pore complex in the brain with interacting proteins – promising targets for protection in neurodegenerative diseases. Biological Chemistry. 391(6). 619–29. 47 indexed citations

Grachev, Dmitry, Tamara Azarashvili, Yulia Baburina, et al.. (2009). The brain‐specific protein, p42^IP4(ADAP 1) is localized in mitochondria and involved in regulation of mitochondrial Ca²⁺. Journal of Neurochemistry. 109(6). 1701–1713. 12 indexed citations

10.

Azarashvili, Tamara, Olga Krestinina, Dmitry Grachev, et al.. (2009). Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase. American Journal of Physiology-Cell Physiology. 296(6). C1428–C1439. 74 indexed citations

11.

Bernstein, Hans‐Gert, Rolf Stricker, Henrik Dobrowolny, et al.. (2007). Histochemical evidence for wide expression of the metalloendopeptidase nardilysin in human brain neurons. Neuroscience. 146(4). 1513–1523. 12 indexed citations

12.

Luo, Weibo, Yingfei Wang, Theodor Hanck, Rolf Stricker, & Georg Reiser. (2006). Jab1, a Novel Protease-activated Receptor-2 (PAR-2)-interacting Protein, Is Involved in PAR-2-induced Activation of Activator Protein-1. Journal of Biological Chemistry. 281(12). 7927–7936. 29 indexed citations

13.

Stricker, Rolf, et al.. (2006). Interaction of the brain‐specific protein p42^IP4/centaurin‐α1 with the peptidase nardilysin is regulated by the cognate ligands of p42^IP4, PtdIns(3,4,5)P₃ and Ins(1,3,4,5)P₄, with stereospecificity. Journal of Neurochemistry. 98(2). 343–354. 14 indexed citations

14.

Stricker, Rolf, et al.. (2003). Oligomerization controls in tissue-specific manner ligand binding of native, affinity-purified p42IP4/centaurin α1 and cytohesins—proteins with high affinity for the messengers d-inositol 1,3,4,5-tetrakisphosphate/phosphatidylinositol 3,4,5-trisphosphate. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1651(1-2). 102–115. 8 indexed citations

15.

Sedehizade, Fariba, et al.. (2002). Cellular expression and subcellular localization of the human Ins(1,3,4,5)P4-binding protein, p42IP4, in human brain and in neuronal cells. Molecular Brain Research. 99(1). 1–11. 25 indexed citations

16.

Stricker, Rolf, et al.. (1999). Translocation between membranes and cytosol of p42^IP4, a specific inositol 1,3,4,5‐tetrakisphosphate/phosphatidylinositol 3,4,5‐trisphosphate‐receptor protein from brain, is induced by inositol 1,3,4,5‐tetrakisphosphate and regulated by a membrane‐associated 5‐phosphatase. European Journal of Biochemistry. 265(2). 815–824. 14 indexed citations

17.

Stricker, Rolf, et al.. (1997). cDNA cloning of porcine p42^IP4, a membrane‐associated and cytosolic 42 kDa inositol(1,3,4,5)tetrakisphosphate receptor from pig brain with similarly high affinity for phosphatidylinositol (3,4,5)P₃. FEBS Letters. 405(2). 229–236. 44 indexed citations

18.

Kreutz, Michael R., et al.. (1997). Expression and Subcellular Localization of p42^IP4/ Centaurin‐α, a Brain‐specific, High‐affinity Receptor for lnositol 1,3,4,5‐Tetrakisphosphate and Phosphatidylinositol 3,4,5‐Trisphosphate in Rat Brain. European Journal of Neuroscience. 9(10). 2110–2124. 35 indexed citations

19.

Kreutz, Michael R., et al.. (1997). Localization of a 42-kDa inositol 1,3,4,5-tetrakisphosphate receptor protein in retina and change in expression after optic nerve injury. Molecular Brain Research. 45(2). 283–293. 12 indexed citations

20.

Reiser, Georg, et al.. (1995). Peptide-Specific Antibodies Indicate Species Heterogeneity of a 42-kDa High-Affinity Inositol 1,3,4,5-Tetrakisphosphate Receptor Protein from Brain. Biochemical and Biophysical Research Communications. 214(1). 20–27. 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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