Mark S. Sands

10.6k total citations
150 papers, 7.8k citations indexed

About

Mark S. Sands is a scholar working on Physiology, Molecular Biology and Cell Biology. According to data from OpenAlex, Mark S. Sands has authored 150 papers receiving a total of 7.8k indexed citations (citations by other indexed papers that have themselves been cited), including 101 papers in Physiology, 69 papers in Molecular Biology and 45 papers in Cell Biology. Recurrent topics in Mark S. Sands's work include Lysosomal Storage Disorders Research (100 papers), Cellular transport and secretion (43 papers) and Trypanosoma species research and implications (27 papers). Mark S. Sands is often cited by papers focused on Lysosomal Storage Disorders Research (100 papers), Cellular transport and secretion (43 papers) and Trypanosoma species research and implications (27 papers). Mark S. Sands collaborates with scholars based in United States, United Kingdom and Canada. Mark S. Sands's co-authors include Carole Vogler, Beth Levy, E H Birkenmeier, William S. Sly, Shannon L. Macauley, Jane E. Barker, Jonathan D. Cooper, Mark E. Haskins, Beverly L. Davidson and Nancy Galvin and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Mark S. Sands

150 papers receiving 7.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark S. Sands United States 55 4.1k 3.6k 2.2k 1.6k 1.5k 150 7.8k
David A. Wenger United States 55 6.4k 1.6× 4.1k 1.2× 734 0.3× 2.0k 1.3× 1.8k 1.2× 221 9.2k
Cynthia J. Tifft United States 30 1.5k 0.4× 1.9k 0.5× 1.2k 0.6× 724 0.4× 613 0.4× 111 4.0k
Ann M. Lawler United States 20 1.7k 0.4× 5.3k 1.5× 1.4k 0.7× 871 0.5× 323 0.2× 25 7.4k
Steven J. Burden United States 54 1.3k 0.3× 8.2k 2.3× 506 0.2× 2.5k 1.5× 912 0.6× 112 11.3k
John McAnally United States 55 1.2k 0.3× 14.0k 3.9× 1.8k 0.8× 1.4k 0.9× 774 0.5× 82 16.9k
Niklas Dahl Sweden 50 822 0.2× 5.9k 1.6× 2.9k 1.3× 1.3k 0.8× 676 0.4× 245 9.8k
Sandro Banfi Italy 46 793 0.2× 7.4k 2.1× 1.4k 0.6× 1.1k 0.6× 1.2k 0.8× 144 9.8k
Marina Mora Italy 41 798 0.2× 4.7k 1.3× 584 0.3× 1.0k 0.6× 903 0.6× 159 6.7k
Jocelyn Laporte France 56 874 0.2× 7.0k 1.9× 1.0k 0.5× 4.5k 2.8× 666 0.4× 260 9.6k
Marco A. Passini United States 36 1.4k 0.3× 2.8k 0.8× 1.0k 0.5× 760 0.5× 509 0.3× 52 4.5k

Countries citing papers authored by Mark S. Sands

Since Specialization
Citations

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

Fields of papers citing papers by Mark S. Sands

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mark S. Sands. 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 Mark S. Sands. The network helps show where Mark S. Sands may publish in the future.

Co-authorship network of co-authors of Mark S. Sands

This figure shows the co-authorship network connecting the top 25 collaborators of Mark S. Sands. A scholar is included among the top collaborators of Mark S. Sands 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 Mark S. Sands. Mark S. Sands 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.
Rensing, Nicholas, Hemanth R. Nelvagal, Steven Q. Le, et al.. (2025). GABAergic interneurons contribute to the fatal seizure phenotype of CLN2 disease mice. JCI Insight. 10(19). 1 indexed citations
2.
Dickson, Patricia, et al.. (2025). Neuronal ceroid lipofuscinosis: underlying mechanisms and emerging therapeutic targets. Nature Reviews Neurology. 21(11). 606–622. 1 indexed citations
3.
Eteleeb, Abdallah M., Niko-Petteri Nykänen, Oscar Harari, et al.. (2023). circRNAs mediate the effect of chronic lysosomal dysfunction on Alzheimer’s disease pathology. Alzheimer s & Dementia. 19(S13). 1 indexed citations
4.
Rensing, Nicholas, Hemanth R. Nelvagal, Joshua T. Dearborn, et al.. (2023). Gene therapy ameliorates spontaneous seizures associated with cortical neuron loss in a Cln2R207X mouse model. Journal of Clinical Investigation. 133(12). 5 indexed citations
5.
Kan, Shih‐hsin, Steven Q. Le, Jonathan D. Cooper, et al.. (2021). Biochemical evaluation of intracerebroventricular rhNAGLU-IGF2 enzyme replacement therapy in neonatal mice with Sanfilippo B syndrome. Molecular Genetics and Metabolism. 133(2). 185–192. 2 indexed citations
6.
Li, Yedda, Yue Xu, Bruno A. Benítez, et al.. (2019). Genetic ablation of acid ceramidase in Krabbe disease confirms the psychosine hypothesis and identifies a new therapeutic target. Proceedings of the National Academy of Sciences. 116(40). 20097–20103. 75 indexed citations
7.
Sidhu, Rohini, Hideji Fujiwara, Mark S. Sands, et al.. (2018). A HILIC‐MS/MS method for simultaneous quantification of the lysosomal disease markers galactosylsphingosine and glucosylsphingosine in mouse serum. Biomedical Chromatography. 32(7). e4235–e4235. 16 indexed citations
8.
Bongarzone, Ernesto R., Maria L. Escolar, Steven J. Gray, et al.. (2016). Insights into the Pathogenesis and Treatment of Krabbe Disease.. PubMed. 13 Suppl 1. 689–96. 20 indexed citations
9.
Li, Yedda & Mark S. Sands. (2014). Experimental Therapies in the Murine Model of Globoid Cell Leukodystrophy. Pediatric Neurology. 51(5). 600–606. 24 indexed citations
10.
Jiang, Xuntian, Paul H. Schlesinger, Ernesto R. Bongarzone, et al.. (2013). Psychosine, the cytotoxic sphingolipid that accumulates in globoid cell leukodystrophy, alters membrane architecture. Journal of Lipid Research. 54(12). 3303–3311. 60 indexed citations
11.
Heldermon, Coy D., Erik D. Herzog, Jeremy R. Glissen Brown, et al.. (2013). Disease correction by combined neonatal intracranial AAV and systemic lentiviral gene therapy in Sanfilippo Syndrome type B mice. Gene Therapy. 20(9). 913–921. 31 indexed citations
12.
Kolber, Benedict J., et al.. (2008). Central amygdala glucocorticoid receptor action promotes fear-associated CRH activation and conditioning. Proceedings of the National Academy of Sciences. 105(33). 12004–12009. 117 indexed citations
13.
Woloszynek, Josh C., Trey Coleman, Clay F. Semenkovich, & Mark S. Sands. (2007). Lysosomal Dysfunction Results in Altered Energy Balance. Journal of Biological Chemistry. 282(49). 35765–35771. 57 indexed citations
14.
Zhao, Haibo, Hideki Kitaura, Mark S. Sands, et al.. (2005). Critical Role of β3 Integrin in Experimental Postmenopausal Osteoporosis. Journal of Bone and Mineral Research. 20(12). 2116–2123. 48 indexed citations
15.
Xu, Lingfei, Mark S. Sands, Bin Wang, et al.. (2004). In vivo transduction of hematopoietic stem cells after neonatal intravenous injection of an amphotropic retroviral vector in mice. Molecular Therapy. 10(1). 37–44. 18 indexed citations
16.
Kitaura, Hideki, Mark S. Sands, Ping Zhou, et al.. (2004). Marrow Stromal Cells and Osteoclast Precursors Differentially Contribute to TNF-α-Induced Osteoclastogenesis In Vivo. The Journal of Immunology. 173(8). 4838–4846. 161 indexed citations
17.
Vogler, Carole, Beth Levy, Nancy Galvin, et al.. (2001). A Novel Model of Murine Mucopolysaccharidosis Type VII due to an Intracisternal A Particle Element Transposition into the β-Glucuronidase Gene: Clinical and Pathologic Findings. Pediatric Research. 49(3). 342–348. 18 indexed citations
18.
O’Connor, Lynn H., Lawrence C. Erway, Carole Vogler, et al.. (1998). Enzyme replacement therapy for murine mucopolysaccharidosis type VII leads to improvements in behavior and auditory function.. Journal of Clinical Investigation. 101(7). 1394–1400. 101 indexed citations
19.
Gwynn, Babette, Kira K. Lueders, Mark S. Sands, & E H Birkenmeier. (1998). Intracisternal A-Particle Element Transposition into the Murine β-Glucuronidase Gene Correlates with Loss of Enzyme Activity: a New Model for β-Glucuronidase Deficiency in the C3H Mouse. Molecular and Cellular Biology. 18(11). 6474–6481. 37 indexed citations
20.
Sands, Mark S., et al.. (1992). Binding of TFIIIA to derivatives of 5S RNA containing sequence substitutions or deletions defines a minimal TFIIIA binding site. Nucleic Acids Research. 20(11). 2639–2645. 9 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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