Bing‐Hao Luo

4.1k total citations · 1 hit paper
38 papers, 3.3k citations indexed

About

Bing‐Hao Luo is a scholar working on Molecular Biology, Immunology and Allergy and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Bing‐Hao Luo has authored 38 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 25 papers in Immunology and Allergy and 10 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Bing‐Hao Luo's work include Cell Adhesion Molecules Research (25 papers), Biochemical and Structural Characterization (13 papers) and Monoclonal and Polyclonal Antibodies Research (10 papers). Bing‐Hao Luo is often cited by papers focused on Cell Adhesion Molecules Research (25 papers), Biochemical and Structural Characterization (13 papers) and Monoclonal and Polyclonal Antibodies Research (10 papers). Bing‐Hao Luo collaborates with scholars based in United States, Japan and China. Bing‐Hao Luo's co-authors include Timothy A. Springer, Christopher V. Carman, Junichi Takagi, Jianghai Zhu, Tsan Sam Xiao, N. Nishida, Ping Hu, Cheng‐Zhong Zhang, Wei Wang and Jieqing Zhu and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Blood.

In The Last Decade

Bing‐Hao Luo

38 papers receiving 3.2k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Structural Basis of Integrin Regulation and Signaling

2007 1.3k citations Bing‐Hao Luo, Christopher V. Carman et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Bing‐Hao Luo United States	18	2.1k	1.4k	872	817	501	38	3.3k
Chungho Kim South Korea	21	1.6k 0.8×	1.4k 1.0×	1.0k 1.2×	511 0.6×	450 0.9×	53	3.0k
Janet A. Askari United Kingdom	30	2.2k 1.1×	1.5k 1.1×	1.6k 1.9×	535 0.7×	247 0.5×	43	3.6k
José M. de Pereda Spain	29	2.0k 1.0×	2.0k 1.4×	2.2k 2.5×	479 0.6×	403 0.8×	58	4.2k
Jari Ylänne Finland	37	2.2k 1.0×	2.1k 1.5×	1.8k 2.1×	529 0.6×	850 1.7×	75	4.8k
Nelly Kieffer Luxembourg	29	1.2k 0.6×	1.0k 0.7×	888 1.0×	383 0.5×	705 1.4×	61	2.9k
Eugene E. Marcantonio United States	27	1.9k 0.9×	1.7k 1.2×	1.6k 1.8×	468 0.6×	217 0.4×	50	3.6k
Kyle R. Legate Germany	18	1.8k 0.9×	1.6k 1.2×	1.5k 1.8×	606 0.7×	231 0.5×	24	3.7k
Sara W. Feigelson Israel	29	1.7k 0.8×	839 0.6×	600 0.7×	1.8k 2.2×	503 1.0×	55	3.2k
Susan J. Monkley United Kingdom	33	1.8k 0.9×	2.5k 1.8×	1.9k 2.2×	1.0k 1.3×	486 1.0×	53	5.3k
Adam Byron United Kingdom	30	1.7k 0.8×	1.9k 1.4×	1.6k 1.9×	548 0.7×	147 0.3×	59	4.3k

Countries citing papers authored by Bing‐Hao Luo

Since Specialization

Citations

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

Fields of papers citing papers by Bing‐Hao Luo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Bing‐Hao Luo. 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 Bing‐Hao Luo. The network helps show where Bing‐Hao Luo may publish in the future.

Co-authorship network of co-authors of Bing‐Hao Luo

This figure shows the co-authorship network connecting the top 25 collaborators of Bing‐Hao Luo. A scholar is included among the top collaborators of Bing‐Hao Luo 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 Bing‐Hao Luo. Bing‐Hao Luo 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

Luo, Bing‐Hao, et al.. (2022). The β₈ integrin EGF domains support a constitutive extended conformation, and the cytoplasmic domain impairs outside‐in signaling. Journal of Cellular Physiology. 237(11). 4251–4261. 1 indexed citations

Wang, Chen, Svetlana Pakhomova, Marcia E. Newcomer, Brent C. Christner, & Bing‐Hao Luo. (2017). Structural basis of antifreeze activity of a bacterial multi-domain antifreeze protein. PLoS ONE. 12(11). e0187169–e0187169. 18 indexed citations

Hu, Ping & Bing‐Hao Luo. (2016). Integrin α_vβ₈Adopts a High Affinity State for Soluble Ligands Under Physiological Conditions. Journal of Cellular Biochemistry. 118(8). 2044–2052. 5 indexed citations

Hu, Ping & Bing‐Hao Luo. (2015). Integrin αIIbβ3 Transmembrane Domain Separation Mediates Bi-Directional Signaling across the Plasma Membrane. PLoS ONE. 10(1). e0116208–e0116208. 10 indexed citations

Brown, Jennifer, Joseph D. Seymour, Mark Skidmore, et al.. (2014). Recrystallization inhibition in ice due to ice binding protein activity detected by nuclear magnetic resonance. Biotechnology Reports. 3. 60–64. 11 indexed citations

Hu, Ping & Bing‐Hao Luo. (2012). Integrin bi‐directional signaling across the plasma membrane. Journal of Cellular Physiology. 228(2). 306–312. 90 indexed citations

Luo, Bing‐Hao, et al.. (2011). Mutagenesis studies of the β I domain metal ion binding sites on integrin αVβ3 ligand binding affinity. Journal of Cellular Biochemistry. 113(4). 1190–1197. 8 indexed citations

Wang, Wei, et al.. (2011). Overview: Structural Biology of Integrins. Methods in molecular biology. 757. 81–99. 30 indexed citations

Wang, Wei, Jieqing Zhu, Timothy A. Springer, & Bing‐Hao Luo. (2010). Tests of Integrin Transmembrane Domain Homo-oligomerization during Integrin Ligand Binding and Signaling. Journal of Biological Chemistry. 286(3). 1860–1867. 15 indexed citations

10.

Wang, Wei & Bing‐Hao Luo. (2009). Structural basis of integrin transmembrane activation. Journal of Cellular Biochemistry. 109(3). 447–452. 34 indexed citations

11.

Zhu, Jianghai, Bing‐Hao Luo, Tsan Sam Xiao, et al.. (2008). Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied Forces. Molecular Cell. 32(6). 849–861. 390 indexed citations

12.

Zhu, Jieqing, Christopher V. Carman, Minsoo Kim, et al.. (2007). Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling. Blood. 110(7). 2475–2483. 101 indexed citations

13.

Zhu, Jieqing, Brian Boylan, Bing‐Hao Luo, Peter J. Newman, & Timothy A. Springer. (2007). Tests of the Extension and Deadbolt Models of Integrin Activation. Journal of Biological Chemistry. 282(16). 11914–11920. 53 indexed citations

14.

Luo, Bing‐Hao & Timothy A. Springer. (2006). Integrin structures and conformational signaling. Current Opinion in Cell Biology. 18(5). 579–586. 222 indexed citations

15.

Luo, Bing‐Hao, Christopher V. Carman, Junichi Takagi, & Timothy A. Springer. (2005). Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proceedings of the National Academy of Sciences. 102(10). 3679–3684. 117 indexed citations

16.

Luo, Bing‐Hao, et al.. (2004). Allosteric β1 Integrin Antibodies That Stabilize the Low Affinity State by Preventing the Swing-out of the Hybrid Domain. Journal of Biological Chemistry. 279(26). 27466–27471. 61 indexed citations

17.

Chen, Jianfeng, Junichi Takagi, Can Xie, et al.. (2004). The Relative Influence of Metal Ion Binding Sites in the I-like Domain and the Interface with the Hybrid Domain on Rolling and Firm Adhesion by Integrin α4β7. Journal of Biological Chemistry. 279(53). 55556–55561. 39 indexed citations

18.

Luo, Bing‐Hao, Timothy A. Springer, & Junichi Takagi. (2003). Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand. Proceedings of the National Academy of Sciences. 100(5). 2403–2408. 126 indexed citations

19.

Luo, Bing‐Hao, et al.. (2002). Important region in the β‐spectrin C‐terminus for spectrin tetramer formation. European Journal Of Haematology. 68(2). 73–79. 9 indexed citations

20.

Aster, Jon C., Warren S. Pear, Robert P. Hasserjian, et al.. (1994). Functional Analysis of the TAN-1 Gene, a Human Homolog of Drosophila Notch. Cold Spring Harbor Symposia on Quantitative Biology. 59(0). 125–136. 80 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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