Rina Timberg

2.4k total citations
28 papers, 2.0k citations indexed

About

Rina Timberg is a scholar working on Molecular Biology, Pharmacology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Rina Timberg has authored 28 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 10 papers in Pharmacology and 4 papers in Cellular and Molecular Neuroscience. Recurrent topics in Rina Timberg's work include Cholinesterase and Neurodegenerative Diseases (10 papers), Nicotinic Acetylcholine Receptors Study (5 papers) and Sperm and Testicular Function (4 papers). Rina Timberg is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (10 papers), Nicotinic Acetylcholine Receptors Study (5 papers) and Sperm and Testicular Function (4 papers). Rina Timberg collaborates with scholars based in Israel, United States and Switzerland. Rina Timberg's co-authors include Joseph Orly, Hermona Soreq, Douglas M. Stocco, Gadi Schuster, Yigal Farkash, Sarah Eimerl, Meira Sternfeld, Dale B. Hales, Karen H. Hales and Shlomo Seidman and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Neuroscience.

In The Last Decade

Rina Timberg

28 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rina Timberg Israel 20 1.1k 458 299 290 278 28 2.0k
Albert J. Baukal United States 39 2.4k 2.2× 130 0.3× 275 0.9× 650 2.2× 983 3.5× 70 3.8k
John E. Bleasdale United States 25 1.8k 1.7× 184 0.4× 187 0.6× 612 2.1× 236 0.8× 56 3.7k
Zhixing Yao United States 18 996 0.9× 152 0.3× 181 0.6× 280 1.0× 249 0.9× 30 2.1k
Ilona I. Concha Chile 31 1.2k 1.1× 122 0.3× 280 0.9× 319 1.1× 175 0.6× 70 2.8k
Fuad Fares Israel 25 984 0.9× 116 0.3× 322 1.1× 320 1.1× 190 0.7× 83 2.2k
Rivka Ofir Israel 31 1.6k 1.5× 144 0.3× 406 1.4× 284 1.0× 99 0.4× 93 3.1k
Stefaan Wera Belgium 23 1.8k 1.6× 261 0.6× 101 0.3× 223 0.8× 138 0.5× 49 2.6k
Ricardo D. Moreno Chile 29 1.8k 1.7× 955 2.1× 546 1.8× 201 0.7× 121 0.4× 97 4.4k
Bradley C. Wise United States 24 1.7k 1.6× 161 0.4× 149 0.5× 719 2.5× 107 0.4× 35 2.8k
Camila V. Esguerra Belgium 26 973 0.9× 218 0.5× 227 0.8× 613 2.1× 71 0.3× 55 2.5k

Countries citing papers authored by Rina Timberg

Since Specialization
Citations

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

Fields of papers citing papers by Rina Timberg

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rina Timberg

This figure shows the co-authorship network connecting the top 25 collaborators of Rina Timberg. A scholar is included among the top collaborators of Rina Timberg 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 Rina Timberg. Rina Timberg 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.
Granot, Zvi, Ruth Geiss‐Friedlander, Naomi Melamed‐Book, et al.. (2003). Proteolysis of Normal and Mutated Steroidogenic Acute Regulatory Proteins in the Mitochondria: the Fate of Unwanted Proteins. Molecular Endocrinology. 17(12). 2461–2476. 75 indexed citations
2.
Granot, Zvi, Ruth Geiss‐Friedlander, Naomi Melamed‐Book, et al.. (2002). THE LIFE CYCLE OF THE STEROIDOGENIC ACUTE REGULATORY (StAR) PROTEIN: FROM TRANSCRIPTION THROUGH PROTEOLYSIS. Endocrine Research. 28(4). 375–386. 31 indexed citations
3.
Ishii, Tomohiro, Tomonobu Hasegawa, Rina Timberg, et al.. (2002). The Roles of Circulating High-Density Lipoproteins and Trophic Hormones in the Phenotype of Knockout Mice Lacking the Steroidogenic Acute Regulatory Protein. Molecular Endocrinology. 16(10). 2297–2309. 40 indexed citations
4.
Larisch, Sarit, Youngsuk Yi, Rona Lotan, et al.. (2000). A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif. Nature Cell Biology. 2(12). 915–921. 200 indexed citations
5.
Broide, Ron S., Mirta Grifman, Dan Grisaru, et al.. (1999). Manipulations of ACHE gene expression suggest non-catalytic involvement of acetylcholinesterase in the functioning of mammalian photoreceptors but not in retinal degeneration. Molecular Brain Research. 71(2). 137–148. 14 indexed citations
6.
7.
Sternfeld, Meira, Guo‐li Ming, Hong-jun Song, et al.. (1998). Acetylcholinesterase Enhances Neurite Growth and Synapse Development through Alternative Contributions of Its Hydrolytic Capacity, Core Protein, and Variable C Termini. Journal of Neuroscience. 18(4). 1240–1249. 174 indexed citations
9.
Sternfeld, Meira, Jacob Rachmilewitz, Christian Andrés, et al.. (1997). Normal and Atypical Butyrylcholinesterases in Placental Development, Function, and Malfunction. Cellular and Molecular Neurobiology. 17(3). 315–332. 15 indexed citations
10.
Beeri, Rachel, Christian Andrés, Efrat Lev-Lehman, et al.. (1995). Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice. Current Biology. 5(9). 1063–1073. 106 indexed citations
12.
Seidman, Shlomo, et al.. (1995). Synaptic and Epidermal Accumulations of Human Acetylcholinesterase Are Encoded by Alternative 3′-Terminal Exons. Molecular and Cellular Biology. 15(6). 2993–3002. 57 indexed citations
13.
Seidman, Shlomo, Rina Timberg, Yael Loewenstein, et al.. (1994). Overexpressed Monomeric Human Acetylcholinesterase Induces Subtle Ultrastructural Modifications in Developing Neuromuscular Junctions of Xenopus laevis Embryos. Journal of Neurochemistry. 62(5). 1670–1681. 34 indexed citations
14.
Seidman, Shlomo, et al.. (1993). Expression of a human acetylcholinesterase promoter-reporter construct in developing neuromuscular junctions of Xenopus embryos.. Proceedings of the National Academy of Sciences. 90(6). 2471–2475. 64 indexed citations
15.
16.
Minke, Baruch, et al.. (1990). Phorbol ester induces photoreceptor-specific degeneration in a Drosophila mutant.. Proceedings of the National Academy of Sciences. 87(1). 113–117. 40 indexed citations
17.
Milner, Yoram, et al.. (1989). Binding modes of IgG from Pemphigus autoimmune sera onto guinea pig keratinocytes and the fate of bound IgGs. Journal of Cellular Physiology. 139(2). 441–454. 10 indexed citations
19.
Timberg, Rina, et al.. (1985). Pigment and Plastid Ultrastructural Changes in Kumquat (Fortunella margarita) «Nagami» during Ripening. Journal of Plant Physiology. 118(1). 61–72. 14 indexed citations
20.
Castel, Mona, et al.. (1985). Ultrastructural localization of immunoreactive neurophysins using monoclonal antibodies and protein A-gold.. Journal of Histochemistry & Cytochemistry. 33(10). 1015–1025. 19 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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