John M. Sipes

1.4k total citations
26 papers, 1.2k citations indexed

About

John M. Sipes is a scholar working on Molecular Biology, Cancer Research and Immunology and Allergy. According to data from OpenAlex, John M. Sipes has authored 26 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 14 papers in Cancer Research and 12 papers in Immunology and Allergy. Recurrent topics in John M. Sipes's work include Cell Adhesion Molecules Research (12 papers), Protease and Inhibitor Mechanisms (11 papers) and Angiogenesis and VEGF in Cancer (11 papers). John M. Sipes is often cited by papers focused on Cell Adhesion Molecules Research (12 papers), Protease and Inhibitor Mechanisms (11 papers) and Angiogenesis and VEGF in Cancer (11 papers). John M. Sipes collaborates with scholars based in United States, United Kingdom and Poland. John M. Sipes's co-authors include David D. Roberts, Henry C. Krutzsch, Marı́a J. Calzada, Deane F. Mosher, Douglas S. Annis, Neng‐Hua Guo, Zhuqing Li, Светлана А. Кузнецова, Jack Lawler and Ning Guo and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Cell Biology and Circulation Research.

In The Last Decade

John M. Sipes

25 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John M. Sipes United States	19	682	365	236	233	196	26	1.2k
Bettina Hartenstein Germany	20	942 1.4×	244 0.7×	140 0.6×	487 2.1×	128 0.7×	24	1.7k
Joanna Liliental United States	5	1.0k 1.5×	195 0.5×	153 0.6×	150 0.6×	187 1.0×	7	1.3k
Ai-Guo Gao United States	6	426 0.6×	397 1.1×	367 1.6×	168 0.7×	143 0.7×	6	923
Lily King United States	14	520 0.8×	187 0.5×	252 1.1×	151 0.6×	142 0.7×	18	1.2k
Anastasia Sacharidou United States	21	948 1.4×	221 0.6×	202 0.9×	263 1.1×	398 2.0×	36	1.8k
Sharon Klein United States	10	937 1.4×	111 0.3×	284 1.2×	191 0.8×	408 2.1×	10	1.4k
Charlotte Rorsman Sweden	10	668 1.0×	206 0.6×	144 0.6×	126 0.5×	112 0.6×	15	1.1k
R.S. Lemons United States	8	871 1.3×	216 0.6×	183 0.8×	376 1.6×	135 0.7×	9	1.3k
Anthony Jackson United States	10	997 1.5×	183 0.5×	99 0.4×	173 0.7×	355 1.8×	10	1.2k
Ann M. Pace United States	6	977 1.4×	304 0.8×	74 0.3×	154 0.7×	192 1.0×	6	1.8k

Countries citing papers authored by John M. Sipes

Since Specialization

Citations

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

Fields of papers citing papers by John M. Sipes

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John M. Sipes

This figure shows the co-authorship network connecting the top 25 collaborators of John M. Sipes. A scholar is included among the top collaborators of John M. Sipes 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 John M. Sipes. John M. Sipes is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Kaur, Sukhbir, Светлана А. Кузнецова, John M. Sipes, et al.. (2025). T Cell Activation Induces Synthesis of CD47 Proteoglycan Isoforms and Their Release in Extracellular Vesicles. International Journal of Molecular Sciences. 26(17). 8377–8377.

Schwartz, Anthony L., Pulak Ranjan Nath, Michael Allgäuer, et al.. (2019). Antisense targeting of CD47 enhances human cytotoxic T-cell activity and increases survival of mice bearing B16 melanoma when combined with anti-CTLA4 and tumor irradiation. Cancer Immunology Immunotherapy. 68(11). 1805–1817. 47 indexed citations

Nath, Pulak Ranjan, Arunakumar Gangaplara, Ajeet Mandal, et al.. (2018). CD47 Expression in Natural Killer Cells Regulates Homeostasis and Modulates Immune Response to Lymphocytic Choriomeningitis Virus. Frontiers in Immunology. 9. 2985–2985. 53 indexed citations

Sipes, John M., Joanne E. Murphy-Ullrich, & David D. Roberts. (2017). Thrombospondins: Purification of human platelet thrombospondin-1. Methods in cell biology. 143. 347–369. 11 indexed citations

Soto‐Pantoja, David R., John M. Sipes, Gema Martin‐Manso, et al.. (2016). Dietary fat overcomes the protective activity of thrombospondin-1 signaling in the ApcMin/+ model of colon cancer. Oncogenesis. 5(5). e230–e230. 15 indexed citations

Miller, Thomas W., David R. Soto‐Pantoja, Anthony L. Schwartz, et al.. (2015). CD47 Receptor Globally Regulates Metabolic Pathways That Control Resistance to Ionizing Radiation. Journal of Biological Chemistry. 290(41). 24858–24874. 56 indexed citations

Soto‐Pantoja, David R., et al.. (2014). Abstract 2434: Therapeutic targeting of CD47 regulates cell bioenergetics and autophagy to reduce breast tumor growth and protect against anthracycline-mediated cardiac toxicity. Cancer Research. 74(19_Supplement). 2434–2434. 2 indexed citations

Kaur, Sukhbir, Светлана А. Кузнецова, Michael L. Pendrak, et al.. (2011). Heparan Sulfate Modification of the Transmembrane Receptor CD47 Is Necessary for Inhibition of T Cell Receptor Signaling by Thrombospondin-1. Journal of Biological Chemistry. 286(17). 14991–15002. 79 indexed citations

Martin‐Manso, Gema, Marı́a J. Calzada, Yoshiro Chuman, et al.. (2011). sFRP-1 binds via its netrin-related motif to the N-module of thrombospondin-1 and blocks thrombospondin-1 stimulation of MDA-MB-231 breast carcinoma cell adhesion and migration. Archives of Biochemistry and Biophysics. 509(2). 147–156. 32 indexed citations

10.

Isenberg, Jeff S., Yan Qin, Justin B. Maxhimer, et al.. (2009). Thrombospondin-1 and CD47 regulate blood pressure and cardiac responses to vasoactive stress. Matrix Biology. 28(2). 110–119. 88 indexed citations

11.

Jia, Yifeng, Shiaw‐Lin Wu, Jeff S. Isenberg, et al.. (2009). Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton. Cell Stress and Chaperones. 15(2). 165–181. 35 indexed citations

12.

Calzada, Marı́a J., Светлана А. Кузнецова, John M. Sipes, et al.. (2008). Calcium indirectly regulates immunochemical reactivity and functional activities of the N-domain of thrombospondin-1. Matrix Biology. 27(4). 339–351. 18 indexed citations

13.

Кузнецова, Светлана А., David Mahoney, Gema Martin‐Manso, et al.. (2007). TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. Matrix Biology. 27(3). 201–210. 36 indexed citations

14.

Calzada, Marı́a J., Longen Zhou, John M. Sipes, et al.. (2003). α ₄ β ₁ Integrin Mediates Selective Endothelial Cell Responses to Thrombospondins 1 and 2 In Vitro and Modulates Angiogenesis In Vivo. Circulation Research. 94(4). 462–470. 83 indexed citations

15.

Calzada, Marı́a J., John M. Sipes, Henry C. Krutzsch, et al.. (2003). Recognition of the N-terminal Modules of Thrombospondin-1 and Thrombospondin-2 by α6β1 Integrin. Journal of Biological Chemistry. 278(42). 40679–40687. 84 indexed citations

16.

Guo, Neng‐Hua, Longen Zhou, John M. Sipes, et al.. (2001). Conformational Regulation of the Fibronectin Binding and α3β1 Integrin-mediated Adhesive Activities of Thrombospondin-1. Journal of Biological Chemistry. 276(30). 27913–27922. 26 indexed citations

17.

Yu, Haini, D.J. Tyrrell, Neng‐Hua Guo, et al.. (2000). Specificities of Heparin-binding Sites from the Amino-Terminus and Type 1 Repeats of Thrombospondin-1. Archives of Biochemistry and Biophysics. 374(1). 13–23. 27 indexed citations

18.

Sipes, John M., Henry C. Krutzsch, Jack Lawler, & David D. Roberts. (1999). Cooperation between Thrombospondin-1 Type 1 Repeat Peptides and αvβ3 Integrin Ligands to Promote Melanoma Cell Spreading and Focal Adhesion Kinase Phosphorylation. Journal of Biological Chemistry. 274(32). 22755–22762. 60 indexed citations

19.

Krutzsch, Henry C., et al.. (1999). Identification of an α3β1 Integrin Recognition Sequence in Thrombospondin-1. Journal of Biological Chemistry. 274(34). 24080–24086. 75 indexed citations

20.

Guo, Ning, Vivian Zabrenetzky, Lakshmi Chandrasekaran, et al.. (1998). Differential roles of protein kinase C and pertussis toxin-sensitive G-binding proteins in modulation of melanoma cell proliferation and motility by thrombospondin 1.. PubMed. 58(14). 3154–62. 47 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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