J.H. Robinson

423 total citations
25 papers, 343 citations indexed

About

J.H. Robinson is a scholar working on Molecular Biology, Cancer Research and Hematology. According to data from OpenAlex, J.H. Robinson has authored 25 papers receiving a total of 343 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 14 papers in Cancer Research and 13 papers in Hematology. Recurrent topics in J.H. Robinson's work include Protease and Inhibitor Mechanisms (14 papers), Blood Coagulation and Thrombosis Mechanisms (13 papers) and Blood properties and coagulation (6 papers). J.H. Robinson is often cited by papers focused on Protease and Inhibitor Mechanisms (14 papers), Blood Coagulation and Thrombosis Mechanisms (13 papers) and Blood properties and coagulation (6 papers). J.H. Robinson collaborates with scholars based in United Kingdom, United States and Australia. J.H. Robinson's co-authors include Ian B. Dodd, Molly Browne, C. Anthony, W. T. Drabble, C.G. Chapman, J.E. Carey, Robin Fears, A. W. R. TYRRELL, B. Reavy and Claire Entwisle and has published in prestigious journals such as Journal of Biological Chemistry, Circulation and Biochemical Journal.

In The Last Decade

J.H. Robinson

25 papers receiving 258 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.H. Robinson United Kingdom 11 189 184 150 70 49 25 343
Naotika Toki Japan 11 100 0.5× 179 1.0× 79 0.5× 39 0.6× 130 2.7× 51 403
David J. Robison United States 6 67 0.4× 129 0.7× 199 1.3× 32 0.5× 17 0.3× 9 357
Kazuhisa Minamiguchi Japan 12 74 0.4× 145 0.8× 60 0.4× 56 0.8× 109 2.2× 25 404
Jude Alsarraj United States 6 115 0.6× 356 1.9× 64 0.4× 41 0.6× 18 0.4× 6 469
Renee Neades United States 11 59 0.3× 249 1.4× 134 0.9× 19 0.3× 8 0.2× 14 456
E D Aĭngorn Israel 6 50 0.3× 242 1.3× 26 0.2× 15 0.2× 16 0.3× 9 380
Valentine B. Andela United States 9 188 1.0× 257 1.4× 16 0.1× 28 0.4× 13 0.3× 14 423
Silvia Grassilli Italy 14 154 0.8× 308 1.7× 54 0.4× 51 0.7× 10 0.2× 38 493
Keisuke Okazaki Japan 9 42 0.2× 257 1.4× 28 0.2× 23 0.3× 7 0.1× 18 391
Juwon Jang South Korea 12 84 0.4× 350 1.9× 54 0.4× 40 0.6× 8 0.2× 17 542

Countries citing papers authored by J.H. Robinson

Since Specialization
Citations

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

Fields of papers citing papers by J.H. Robinson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.H. Robinson. 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 J.H. Robinson. The network helps show where J.H. Robinson may publish in the future.

Co-authorship network of co-authors of J.H. Robinson

This figure shows the co-authorship network connecting the top 25 collaborators of J.H. Robinson. A scholar is included among the top collaborators of J.H. Robinson 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 J.H. Robinson. J.H. Robinson 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.
Gloger, Israel, et al.. (1995). The importance of genome analysis to the drug discovery process. Molecular Medicine Today. 1(8). 373–377. 10 indexed citations
2.
McHale, Mark, Nicole C. Herrity, Izzy Boyfield, et al.. (1994). Expression and functional characterisation of a synthetic version of the human D4 dopamine receptor in a stable human cell line. FEBS Letters. 345(2-3). 147–150. 10 indexed citations
3.
Wilson, Shelagh, David Cronk, Ian B. Dodd, et al.. (1993). The Use of Active Centre Acylation to Control the Pharmacokinetic Profile of a Recombinant Chimaeric Plasminogen Activator. Thrombosis and Haemostasis. 70(6). 984–988. 1 indexed citations
4.
Dodd, Ian B., et al.. (1993). Susceptibility of mutant, recombinant plasminogen activators to proteolytic breakdown: Removal of the F domain by plasmin. Fibrinolysis and Proteolysis. 7(4). 237–241. 1 indexed citations
5.
Robinson, J.H., Molly Browne, J.E. Carey, et al.. (1992). A recombinant, chimeric enzyme with a novel mechanism of action leading to greater potency and selectivity than tissue-type plasminogen activator.. Circulation. 86(2). 548–552. 7 indexed citations
6.
Browne, Molly, C.G. Chapman, Ian B. Dodd, et al.. (1991). Expression of recombinant human plasminogen and aglycoplasminogen in hela cells. Fibrinolysis and Proteolysis. 5(4). 257–260. 3 indexed citations
7.
Browne, Molly, et al.. (1990). Deletion of a tripeptide sequence from the growth-factor domain of tissue-type plasminogen activator prolongs in vivo circulation. Thrombosis Research. 59(3). 687–692. 13 indexed citations
8.
9.
Ferres, H., et al.. (1990). Efficacy and selectivity of tissue-type and urokinase-type plasminogen activators in a humanised pulmonary embolism model. Fibrinolysis and Proteolysis. 4(2). 87–94. 3 indexed citations
10.
Wilson, Shelagh, et al.. (1990). Interaction of a Plasmin A-Chain/t-PA B-Chain Hybrid Enzyme with Plasma Inhibitors In Vivo and In Vitro. Thrombosis and Haemostasis. 63(3). 459–463. 4 indexed citations
11.
Browne, Molly, et al.. (1989). The role of tissue-type plasminogen activator A-chain domains in plasma clearance. Fibrinolysis and Proteolysis. 3(4). 207–214. 13 indexed citations
12.
Robinson, J.H., et al.. (1988). Slow Clearance of Acylated, Hybrid Thrombolytic Enzymes. Thrombosis and Haemostasis. 59(3). 421–425. 10 indexed citations
13.
14.
Dodd, Ian B., et al.. (1986). Large scale, rapid purification of recombinant tissue‐type plasminogen activator. FEBS Letters. 209(1). 13–17. 29 indexed citations
15.
Browne, Molly, Ian B. Dodd, J.E. Carey, C.G. Chapman, & J.H. Robinson. (1985). Increased Yield of Human Tissue-Type Plasminogen Activator Obtained by Means of Recombinant DNA Technology. Thrombosis and Haemostasis. 54(2). 422–424. 21 indexed citations
16.
Browne, Molly, A. W. R. TYRRELL, C.G. Chapman, et al.. (1985). Isolation of a human tissue-type plasminogen-activator genomic DNA clone and its expression in mouse L cells. Gene. 33(3). 279–284. 27 indexed citations
17.
18.
Robinson, J.H., C. Anthony, & W. T. Drabble. (1973). Regulation of the Acidic Amino-acid Permease of Aspergillus nidulans. Journal of General Microbiology. 79(1). 65–80. 22 indexed citations
19.
Robinson, J.H., C. Anthony, & W. T. Drabble. (1972). Regulation of the acidic amino acid permease of Aspergillus nidulans. Biochemical Journal. 127(3). 71P–72P. 1 indexed citations
20.
Robinson, J.H., C. Anthony, & W. T. Drabble. (1971). Activity and regulation of an acidic amino acid permease of Aspergillus nidulans. Biochemical Journal. 124(5). 75P–75p. 7 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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