Mark A. Hancock

3.1k total citations
53 papers, 2.2k citations indexed

About

Mark A. Hancock is a scholar working on Molecular Biology, Cancer Research and Physiology. According to data from OpenAlex, Mark A. Hancock has authored 53 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 11 papers in Cancer Research and 9 papers in Physiology. Recurrent topics in Mark A. Hancock's work include Protease and Inhibitor Mechanisms (9 papers), Alzheimer's disease research and treatments (9 papers) and Bacterial Genetics and Biotechnology (8 papers). Mark A. Hancock is often cited by papers focused on Protease and Inhibitor Mechanisms (9 papers), Alzheimer's disease research and treatments (9 papers) and Bacterial Genetics and Biotechnology (8 papers). Mark A. Hancock collaborates with scholars based in Canada, United States and Germany. Mark A. Hancock's co-authors include Marlys L. Koschinsky, Peter Grütter, Jeffrey M. Mativetsky, Brett A. Kaufman, Eric A. Shoubridge, Nela Durisic, Santiago Costantino, Santica M. Marcovina, Michael B. Boffa and Hanadi F. Sleiman and has published in prestigious journals such as Science, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Mark A. Hancock

53 papers receiving 2.1k 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 A. Hancock Canada 25 1.2k 299 255 234 224 53 2.2k
Claire Summers United Kingdom 7 1.1k 1.0× 238 0.8× 199 0.8× 201 0.9× 241 1.1× 12 2.6k
Allan G. Murray Canada 23 1.1k 1.0× 255 0.9× 381 1.5× 600 2.6× 81 0.4× 64 2.5k
Leena Valmu Finland 30 1.2k 1.0× 218 0.7× 214 0.8× 552 2.4× 74 0.3× 60 2.4k
Sei Yoshida Japan 23 1.1k 1.0× 222 0.7× 238 0.9× 300 1.3× 92 0.4× 41 2.6k
Kristian Prydz Norway 29 2.0k 1.7× 250 0.8× 282 1.1× 605 2.6× 112 0.5× 81 3.4k
George M. C. Janssen Netherlands 37 2.3k 2.0× 389 1.3× 307 1.2× 915 3.9× 110 0.5× 82 4.1k
Kaoru Tominaga Japan 24 2.6k 2.2× 470 1.6× 126 0.5× 653 2.8× 146 0.7× 74 3.5k
Chiara Urbinati Italy 29 1.3k 1.1× 172 0.6× 115 0.5× 420 1.8× 114 0.5× 55 2.1k
Santosh Renuse United States 27 1.2k 1.0× 194 0.6× 122 0.5× 154 0.7× 123 0.5× 73 2.1k
Kaori Suzuki Japan 29 1.3k 1.1× 777 2.6× 339 1.3× 429 1.8× 214 1.0× 56 2.6k

Countries citing papers authored by Mark A. Hancock

Since Specialization
Citations

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

Fields of papers citing papers by Mark A. Hancock

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark A. Hancock

This figure shows the co-authorship network connecting the top 25 collaborators of Mark A. Hancock. A scholar is included among the top collaborators of Mark A. Hancock 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 A. Hancock. Mark A. Hancock 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.
Hancock, Mark A., Mariusz Madej, Jan Potempa, et al.. (2024). Unveiling the molecular mechanisms of the type IX secretion system's response regulator: Structural and functional insights. PNAS Nexus. 3(8). pgae316–pgae316. 2 indexed citations
2.
Shobo, Adeola, et al.. (2024). Inhibition of BACE1 affected both its Aβ producing and degrading activities and increased Aβ42 and Aβ40 levels at high-level BACE1 expression. Journal of Biological Chemistry. 300(8). 107510–107510. 10 indexed citations
3.
Bharadwaj, Alamelu G., John Woods, Victoria A. Miller, et al.. (2023). Identification and characterization of calreticulin as a novel plasminogen receptor. Journal of Biological Chemistry. 300(1). 105465–105465. 3 indexed citations
4.
Shobo, Adeola, et al.. (2022). Biophysical characterization as a tool to predict amyloidogenic and toxic properties of amyloid‐β42 peptides. FEBS Letters. 596(11). 1401–1411. 5 indexed citations
5.
Shobo, Adeola, Daniel Dai, Corbin Black, et al.. (2021). The amyloid-β1–42-oligomer interacting peptide D-AIP possesses favorable biostability, pharmacokinetics, and brain region distribution. Journal of Biological Chemistry. 298(1). 101483–101483. 3 indexed citations
6.
Zandarashvili, Levani, Marie-France Langelier, Uday Kiran Velagapudi, et al.. (2020). Structural basis for allosteric PARP-1 retention on DNA breaks. Science. 368(6486). 233 indexed citations
7.
Sidorova, Yulia, et al.. (2020). Small-Molecule Ligands that Bind the RET Receptor Activate Neuroprotective Signals Independent of but Modulated by Coreceptor GFRα1. Molecular Pharmacology. 98(1). 1–12. 8 indexed citations
8.
Veit, Guido, Ariel Roldán, Mark A. Hancock, et al.. (2020). Allosteric folding correction of F508del and rare CFTR mutants by elexacaftor-tezacaftor-ivacaftor (Trikafta) combination. JCI Insight. 5(18). 178 indexed citations
9.
Kulic, Luka, Charlotte E. Teunissen, Adeola Shobo, et al.. (2019). Aβ34 is a BACE1-derived degradation intermediate associated with amyloid clearance and Alzheimer’s disease progression. Nature Communications. 10(1). 2240–2240. 47 indexed citations
10.
Maysinger, Dušica, Alexandre Moquin, Shireen Hossain, et al.. (2017). Dendritic Polyglycerol Sulfates in the Prevention of Synaptic Loss and Mechanism of Action on Glia. ACS Chemical Neuroscience. 9(2). 260–271. 31 indexed citations
11.
Hancock, Mark A., et al.. (2016). Structural Analysis and Inhibition of TraE from the pKM101 Type IV Secretion System. Journal of Biological Chemistry. 291(45). 23817–23829. 33 indexed citations
12.
Wang, Ni, Roni Rayes, Seyyed Mehdy Elahi, et al.. (2015). The IGF-Trap: Novel Inhibitor of Carcinoma Growth and Metastasis. Molecular Cancer Therapeutics. 14(4). 982–993. 38 indexed citations
13.
LeBlanc, Philippe M., Teresa A. Doggett, Jayoung Choi, et al.. (2014). An Immunogenic Peptide in the A-box of HMGB1 Protein Reverses Apoptosis-induced Tolerance through RAGE Receptor. Journal of Biological Chemistry. 289(11). 7777–7786. 57 indexed citations
14.
Hancock, Mark A., et al.. (2011). Biochemical and biological characterization of Escherichia coli STb His12 to Asn variant. Toxicon. 59(2). 300–305. 4 indexed citations
15.
Kornblatt, M.J., Jack A. Kornblatt, & Mark A. Hancock. (2011). The Interaction of Canine Plasminogen with Streptococcus pyogenes Enolase: They Bind to One Another but What Is the Nature of the Structures Involved?. PLoS ONE. 6(12). e28481–e28481. 13 indexed citations
16.
Kim, Jaeseung, Stéphane G. Paquette, Hubert Gagnon, et al.. (2010). Interaction between MMACHC and MMADHC, two human proteins participating in intracellular vitamin B12 metabolism. Molecular Genetics and Metabolism. 102(2). 139–148. 43 indexed citations
17.
Kaufman, Brett A., Nela Durisic, Jeffrey M. Mativetsky, et al.. (2007). The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures. Molecular Biology of the Cell. 18(9). 3225–3236. 330 indexed citations
18.
Carter, David M., Isabelle R. Miousse, Eric Martínez, et al.. (2006). Interactions between TonB from Escherichia coli and the Periplasmic Protein FhuD. Journal of Biological Chemistry. 281(46). 35413–35424. 43 indexed citations
19.
Hancock, Mark A., Michael B. Boffa, Santica M. Marcovina, Michael E. Nesheim, & Marlys L. Koschinsky. (2003). Inhibition of Plasminogen Activation by Lipoprotein(a). Journal of Biological Chemistry. 278(26). 23260–23269. 108 indexed citations
20.
Bdeir, Khalil, Gabriela Canziani, Irwin Chaiken, et al.. (1999). Defensin Promotes the Binding of Lipoprotein(a) to Vascular Matrix. Blood. 94(6). 2007–2019. 63 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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