Thomas M. Wengenack

2.8k total citations
40 papers, 2.3k citations indexed

About

Thomas M. Wengenack is a scholar working on Physiology, Molecular Biology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Thomas M. Wengenack has authored 40 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Physiology, 23 papers in Molecular Biology and 8 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Thomas M. Wengenack's work include Alzheimer's disease research and treatments (29 papers), Prion Diseases and Protein Misfolding (15 papers) and Neuroscience and Neuropharmacology Research (5 papers). Thomas M. Wengenack is often cited by papers focused on Alzheimer's disease research and treatments (29 papers), Prion Diseases and Protein Misfolding (15 papers) and Neuroscience and Neuropharmacology Research (5 papers). Thomas M. Wengenack collaborates with scholars based in United States, Finland and Poland. Thomas M. Wengenack's co-authors include Joseph F. Poduslo, Geoffry L. Curran, Clifford R. Jack, Michael Garwood, Geoffrey L. Curran, Bret Borowski, Silvina S. Holasek, Karunya K. Kandimalla, Małgorzata Marjańska and Joseph Lin 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

Thomas M. Wengenack

39 papers receiving 2.3k citations

Peers

Thomas M. Wengenack
Geoffry L. Curran United States
Mei‐Ping Kung United States
Bin Ji Japan
Stephen T. Kajdasz United States
Christine A. Parker United Kingdom
Anna Katrin Szardenings United States
Stina Syvänen Sweden
Michelle T. Fodero‐Tavoletti Australia
Susanne Ostrowitzki Switzerland
Dag Sehlin Sweden
Geoffry L. Curran United States
Thomas M. Wengenack
Citations per year, relative to Thomas M. Wengenack Thomas M. Wengenack (= 1×) peers Geoffry L. Curran

Countries citing papers authored by Thomas M. Wengenack

Since Specialization
Citations

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

Fields of papers citing papers by Thomas M. Wengenack

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas M. Wengenack. 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 Thomas M. Wengenack. The network helps show where Thomas M. Wengenack may publish in the future.

Co-authorship network of co-authors of Thomas M. Wengenack

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas M. Wengenack. A scholar is included among the top collaborators of Thomas M. Wengenack 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 Thomas M. Wengenack. Thomas M. Wengenack 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.
Marjańska, Małgorzata, Stephen D. Weigand, Gregory M. Preboske, et al.. (2013). Treatment effects in a transgenic mouse model of Alzheimer’s disease: A magnetic resonance spectroscopy study after passive immunization. Neuroscience. 259. 94–100. 15 indexed citations
2.
Sarkar, Gobinda, Geoffry L. Curran, Teresa Decklever, et al.. (2011). A Carrier for Non-Covalent Delivery of Functional Beta-Galactosidase and Antibodies against Amyloid Plaques and IgM to the Brain. PLoS ONE. 6(12). e28881–e28881. 44 indexed citations
3.
Wengenack, Thomas M., Denise A. Reyes, Geoffry L. Curran, et al.. (2010). Regional differences in MRI detection of amyloid plaques in AD transgenic mouse brain. NeuroImage. 54(1). 113–122. 33 indexed citations
4.
Chamberlain, Ryan, Denise A. Reyes, Geoffrey L. Curran, et al.. (2009). Comparison of amyloid plaque contrast generated by T2‐weighted, T‐weighted, and susceptibility‐weighted imaging methods in transgenic mouse models of Alzheimer's disease. Magnetic Resonance in Medicine. 61(5). 1158–1164. 53 indexed citations
5.
Ramakrishnan, Muthu, Thomas M. Wengenack, Karunya K. Kandimalla, et al.. (2008). Selective Contrast Enhancement of Individual Alzheimer’s Disease Amyloid Plaques Using a Polyamine and Gd-DOTA Conjugated Antibody Fragment Against Fibrillar Aβ42 for Magnetic Resonance Molecular Imaging. Pharmaceutical Research. 25(8). 1861–1872. 37 indexed citations
6.
Wengenack, Thomas M., Clifford R. Jack, Michael Garwood, & Joseph F. Poduslo. (2008). MR Microimaging of amyloid plaques in Alzheimer’s disease transgenic mice. European Journal of Nuclear Medicine and Molecular Imaging. 35(S1). 82–88. 31 indexed citations
7.
Poduslo, Joseph F., Muthu Ramakrishnan, Silvina S. Holasek, et al.. (2007). In vivo targeting of antibody fragments to the nervous system for Alzheimer’s disease immunotherapy and molecular imaging of amyloid plaques. Journal of Neurochemistry. 102(2). 420–433. 76 indexed citations
8.
Kandimalla, Karunya K., Thomas M. Wengenack, Geoffry L. Curran, Emily J. Gilles, & Joseph F. Poduslo. (2007). Pharmacokinetics and Amyloid Plaque Targeting Ability of a Novel Peptide-Based Magnetic Resonance Contrast Agent in Wild-Type and Alzheimer’s Disease Transgenic Mice. Journal of Pharmacology and Experimental Therapeutics. 322(2). 541–549. 15 indexed citations
9.
Hartman, Tyler, Thomas M. Wengenack, Joseph F. Poduslo, & Jan M. van Deursen. (2006). Mutant mice with small amounts of BubR1 display accelerated age-related gliosis. Neurobiology of Aging. 28(6). 921–927. 39 indexed citations
10.
Kandimalla, Karunya K., Geoffry L. Curran, Silvina S. Holasek, et al.. (2005). Pharmacokinetic Analysis of the Blood-Brain Barrier Transport of 125I-Amyloid β Protein 40 in Wild-Type and Alzheimer’s Disease Transgenic Mice (APP,PS1) and Its Implications for Amyloid Plaque Formation. Journal of Pharmacology and Experimental Therapeutics. 313(3). 1370–1378. 52 indexed citations
11.
Jack, Clifford R., Thomas M. Wengenack, Denise A. Reyes, et al.. (2005). In VivoMagnetic Resonance Microimaging of Individual Amyloid Plaques in Alzheimer's Transgenic Mice. Journal of Neuroscience. 25(43). 10041–10048. 127 indexed citations
12.
Jack, Clifford R., Michael Garwood, Thomas M. Wengenack, et al.. (2004). In vivo visualization of Alzheimer's amyloid plaques by magnetic resonance imaging in transgenic mice without a contrast agent. Magnetic Resonance in Medicine. 52(6). 1263–1271. 162 indexed citations
13.
14.
Poduslo, Joseph F., Thomas M. Wengenack, Geoffry L. Curran, et al.. (2002). Molecular Targeting of Alzheimer's Amyloid Plaques for Contrast-Enhanced Magnetic Resonance Imaging. Neurobiology of Disease. 11(2). 315–329. 165 indexed citations
15.
Wengenack, Thomas M., et al.. (2000). Targeting Alzheimer amyloid plaques in vivo. Nature Biotechnology. 18(8). 868–872. 76 indexed citations
16.
Wengenack, Thomas M., et al.. (1997). Putrescine-modified catalase with preserved enzymatic activity exhibits increased permeability at the blood-nerve and blood-brain barriers. Brain Research. 767(1). 128–135. 21 indexed citations
17.
Wengenack, Thomas M., Geoffry L. Curran, & Joseph F. Poduslo. (1997). Postischemic, systemic administration of polyamine-modified superoxide dismutase reduces hippocampal CA1 neurodegeneration in rat global cerebral ischemia. Brain Research. 754(1-2). 46–54. 40 indexed citations
18.
Slemmon, J. Randall, Thomas M. Wengenack, & Dorothy G. Flood. (1997). Profiling of endogenous peptides as a tool for studying development and neurological disease. Biopolymers. 43(2). 157–170. 22 indexed citations
19.
Slemmon, J. Randall, James P. Morgan, Stephanie M. Fullerton, et al.. (1996). Camstatins Are Peptide Antagonists of Calmodulin Based Upon a Conserved Structural Motif in PEP-19, Neurogranin, and Neuromodulin. Journal of Biological Chemistry. 271(27). 15911–15917. 78 indexed citations
20.
Wengenack, Thomas M., J. Randall Slemmon, J. M. Ordy, William P. Dunlap, & Paul D. Coleman. (1994). Vascular and Cellular Protein Changes Precede Hippocampal Pyramidal Cell Loss Following Global Ischemia in the Rat. Advances in experimental medicine and biology. 366. 436–438. 1 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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