Robert D. Moir

25.5k total citations · 8 hit papers
121 papers, 19.6k citations indexed

About

Robert D. Moir is a scholar working on Physiology, Molecular Biology and Nutrition and Dietetics. According to data from OpenAlex, Robert D. Moir has authored 121 papers receiving a total of 19.6k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Physiology, 63 papers in Molecular Biology and 20 papers in Nutrition and Dietetics. Recurrent topics in Robert D. Moir's work include Alzheimer's disease research and treatments (71 papers), Trace Elements in Health (20 papers) and Nuclear Structure and Function (19 papers). Robert D. Moir is often cited by papers focused on Alzheimer's disease research and treatments (71 papers), Trace Elements in Health (20 papers) and Nuclear Structure and Function (19 papers). Robert D. Moir collaborates with scholars based in United States, Australia and Germany. Robert D. Moir's co-authors include Rudolph E. Tanzi, Ashley I. Bush, Robert D. Goldman, Xudong Huang, Craig Atwood, Lee E. Goldstein, Timothy P. Spann, Mariana A. Hartshorn, Richard C. Scarpa and Miri Yoon and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Robert D. Moir

120 papers receiving 19.2k citations

Hit Papers

Treatment with a Copper-Zinc Chelator Markedly and Rapidl... 1998 2026 2007 2016 2001 1999 1998 2010 2016 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert D. Moir United States 67 10.2k 8.9k 3.2k 2.4k 2.1k 121 19.6k
Roberto Cappai Australia 69 9.1k 0.9× 6.9k 0.8× 3.6k 1.1× 1.9k 0.8× 1.1k 0.5× 235 15.9k
Gerd Multhaup Germany 78 18.5k 1.8× 13.3k 1.5× 4.8k 1.5× 4.0k 1.7× 2.1k 1.0× 180 27.0k
Catriona McLean Australia 69 6.4k 0.6× 7.1k 0.8× 1.7k 0.5× 1.6k 0.7× 952 0.5× 471 19.5k
Robert W. Mahley United States 116 12.5k 1.2× 17.2k 1.9× 2.1k 0.7× 2.3k 1.0× 2.9k 1.4× 303 44.3k
Mario Salmona Italy 67 4.7k 0.5× 9.6k 1.1× 2.0k 0.6× 1.4k 0.6× 956 0.5× 437 17.1k
Thomas Wısnıewskı United States 76 11.7k 1.1× 8.8k 1.0× 1.4k 0.4× 2.3k 1.0× 1.0k 0.5× 389 20.5k
Claudio Soto United States 79 8.4k 0.8× 13.4k 1.5× 2.8k 0.9× 2.3k 1.0× 1.8k 0.9× 239 21.5k
Paul E. Fraser Canada 62 7.4k 0.7× 8.6k 1.0× 1.6k 0.5× 929 0.4× 1.5k 0.7× 153 13.7k
Nigel M. Hooper United Kingdom 73 4.3k 0.4× 9.2k 1.0× 1.9k 0.6× 1.5k 0.7× 1.9k 0.9× 281 18.2k
David Schubert United States 73 6.8k 0.7× 11.0k 1.2× 767 0.2× 2.0k 0.8× 2.1k 1.0× 196 20.4k

Countries citing papers authored by Robert D. Moir

Since Specialization
Citations

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

Fields of papers citing papers by Robert D. Moir

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert D. Moir. 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 Robert D. Moir. The network helps show where Robert D. Moir may publish in the future.

Co-authorship network of co-authors of Robert D. Moir

This figure shows the co-authorship network connecting the top 25 collaborators of Robert D. Moir. A scholar is included among the top collaborators of Robert D. Moir 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 Robert D. Moir. Robert D. Moir 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.
Eimer, William A., Alex S. Rodriguez, Joseph Park, et al.. (2025). Phosphorylated tau exhibits antimicrobial activity capable of neutralizing herpes simplex virus 1 infectivity in human neurons. Nature Neuroscience. 29(3). 604–616. 1 indexed citations
2.
Kumar, Deepak Kumar Vijaya, Nanda Kumar N. Shanmugam, Kevin J. Washicosky, et al.. (2018). Alzheimerrs Disease-Associated -amyloid Is Rapidly Seeded by <i>herpesviridae</i> to Protect Against Brain Infection. SSRN Electronic Journal. 2 indexed citations
3.
Ran, Chongzhao, Wei Zhao, Robert D. Moir, & Anna Moore. (2011). Non-Conjugated Small Molecule FRET for Differentiating Monomers from Higher Molecular Weight Amyloid Beta Species. PLoS ONE. 6(4). e19362–e19362. 37 indexed citations
4.
Dong, Yuanlin, Guohua Zhang, Bin Zhang, et al.. (2009). The Common Inhalational Anesthetic Sevoflurane Induces Apoptosis and Increases β-Amyloid Protein Levels. Archives of Neurology. 66(5). 620–31. 228 indexed citations
5.
Moncaster, Juliet A., Robert D. Moir, Anca Mocofanescu, et al.. (2008). In vivo Early Detection of Alzheimer’s Disease-Linked Aβ Peptide Accumulation in the Lens Using Quasi-Elastic Light Scattering. Investigative Ophthalmology & Visual Science. 49(13). 4080–4080. 3 indexed citations
6.
Xie, Zhongcong, Yuanlin Dong, Uta Maeda, et al.. (2007). The Inhalation Anesthetic Isoflurane Induces a Vicious Cycle of Apoptosis and Amyloid β-Protein Accumulation. Journal of Neuroscience. 27(6). 1247–1254. 187 indexed citations
7.
Shumaker, Dale K., Reynold I. Lopez‐Soler, Stephen A. Adam, et al.. (2005). Functions and dysfunctions of the nuclear lamin Ig-fold domain in nuclear assembly, growth, and Emery–Dreifuss muscular dystrophy. Proceedings of the National Academy of Sciences. 102(43). 15494–15499. 42 indexed citations
8.
Hutter‐Paier, Birgit, Henri J. Huttunen, Luigi Puglielli, et al.. (2004). The ACAT Inhibitor CP-113,818 Markedly Reduces Amyloid Pathology in a Mouse Model of Alzheimer's Disease. Neuron. 44(2). 227–238. 221 indexed citations
9.
Xie, Zhongcong, Robert D. Moir, Donna Romano, et al.. (2004). Hypocapnia Induces Caspase-3 Activation and Increases Aβ Production. Neurodegenerative Diseases. 1(1). 29–37. 29 indexed citations
10.
Rogers, Jack T., Jeffrey Randall, Paul S. Eder, et al.. (2002). Alzheimer’s disease drug discovery targeted to the APP mRNA 5′Untranslated region. Journal of Molecular Neuroscience. 19(1-2). 77–82. 50 indexed citations
11.
Liu, Ying, Melina Jones, Cynthia M. Hingtgen, et al.. (2000). Uptake of HIV-1 Tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands. Nature Medicine. 6(12). 1380–1387. 314 indexed citations
12.
Höck, Christoph, Sidonie Golombowski, F. Müller‐Spahn, et al.. (1998). Cerebrospinal Fluid Levels of Amyloid Precursor Protein and Amyloid β-Peptide in Alzheimer’s Disease and Major Depression – Inverse Correlation with Dementia Severity. European Neurology. 39(2). 111–118. 73 indexed citations
13.
Moir, Robert D., Timothy P. Spann, & Robert D. Goldman. (1996). The Dynamic Properties and Possible Functions of Nuclear Lamins. International review of cytology. 162B. 141–182. 150 indexed citations
14.
Goldman, Anne E., et al.. (1992). Pathway of incorporation of microinjected lamin A into the nuclear envelope.. The Journal of Cell Biology. 119(4). 725–735. 133 indexed citations
15.
Bush, Ashley I., Scott Whyte, Timothy G. Williamson, et al.. (1992). An abnormality of plasma amyloid protein precursor in Alzheimer's disease. Annals of Neurology. 32(1). 57–65. 47 indexed citations
16.
Milward, Elizabeth A., Roula Papadopoulos, Stephanie Fuller, et al.. (1992). The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron. 9(1). 129–137. 388 indexed citations
17.
Bush, Ashley I., Ralph N. Martins, B. Rumble, et al.. (1990). The amyloid precursor protein of Alzheimer's disease is released by human platelets.. Journal of Biological Chemistry. 265(26). 15977–15983. 270 indexed citations
18.
Moir, Robert D., Roy A. Quinlan, & Murray Stewart. (1990). Expression and characterization of human lamin C. FEBS Letters. 268(1). 301–305. 25 indexed citations
19.
Quinlan, Roy A., Robert D. Moir, & Murray Stewart. (1989). Expression in Escherichia coli of fragments of glial fibrillary acidic protein: Characterization, assembly properties and paracrystal formation. Journal of Cell Science. 93(1). 71–83. 88 indexed citations
20.
Moir, Robert D. & Gordon H. Dixon. (1988). Characterization of a protamine gene from the chum salmon (Oncorhynchus keta). Journal of Molecular Evolution. 27(1). 8–16. 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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