H.A. Barker

10.4k total citations
112 papers, 4.5k citations indexed

About

H.A. Barker is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, H.A. Barker has authored 112 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 75 papers in Molecular Biology, 38 papers in Biochemistry and 20 papers in Materials Chemistry. Recurrent topics in H.A. Barker's work include Amino Acid Enzymes and Metabolism (30 papers), Enzyme Structure and Function (20 papers) and Porphyrin Metabolism and Disorders (16 papers). H.A. Barker is often cited by papers focused on Amino Acid Enzymes and Metabolism (30 papers), Enzyme Structure and Function (20 papers) and Porphyrin Metabolism and Disorders (16 papers). H.A. Barker collaborates with scholars based in United States, United Kingdom and Australia. H.A. Barker's co-authors include Herbert Weissbach, Robert D. Smyth, John I. Toohey, J.N. Ladd, Thressa C. Stadtman, B. E. Volcani, Wolfgang Buckel, Harry P. C. Hogenkamp, Rebecca M. Wilson and Roscoe O. Brady and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Annual Review of Biochemistry.

In The Last Decade

H.A. Barker

112 papers receiving 4.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
H.A. Barker United States 40 3.2k 868 675 648 350 112 4.5k
Saburo Fukui Japan 37 4.1k 1.3× 643 0.7× 430 0.6× 482 0.7× 298 0.9× 238 4.9k
G. Gottschalk Germany 45 3.8k 1.2× 147 0.2× 876 1.3× 557 0.9× 230 0.7× 108 5.9k
Lars G. Ljungdahl United States 48 3.3k 1.0× 248 0.3× 577 0.9× 171 0.3× 149 0.4× 103 6.1k
W.A. Wood United States 39 2.0k 0.6× 99 0.1× 809 1.2× 959 1.5× 176 0.5× 130 4.0k
Nobuyoshi Esaki Japan 51 4.9k 1.5× 444 0.5× 2.0k 3.0× 2.3k 3.5× 324 0.9× 284 8.1k
K. S. Dodgson United Kingdom 33 2.1k 0.7× 168 0.2× 131 0.2× 416 0.6× 175 0.5× 129 5.8k
Thomas Leisinger Switzerland 50 3.8k 1.2× 106 0.1× 732 1.1× 630 1.0× 128 0.4× 160 7.4k
Jan R. Andreesen Germany 44 2.6k 0.8× 69 0.1× 595 0.9× 542 0.8× 315 0.9× 122 4.8k
H. Rosenberg Australia 35 1.8k 0.6× 94 0.1× 419 0.6× 495 0.8× 206 0.6× 117 4.0k
Tatsuo Kurihara Japan 41 2.9k 0.9× 169 0.2× 785 1.2× 519 0.8× 110 0.3× 154 4.5k

Countries citing papers authored by H.A. Barker

Since Specialization
Citations

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

Fields of papers citing papers by H.A. Barker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of H.A. Barker

This figure shows the co-authorship network connecting the top 25 collaborators of H.A. Barker. A scholar is included among the top collaborators of H.A. Barker 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 H.A. Barker. H.A. Barker 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.
Barker, H.A.. (1992). The Path from Acetylphosphate to Acetyl CoA. The FASEB Journal. 6(11). 3014–3016. 4 indexed citations
2.
Barker, H.A.. (1985). Pathway of 5-Aminovalerate Degradation by Clostridium aminovalericum. Current topics in cellular regulation. 26. 349–354. 4 indexed citations
3.
Barker, H.A., et al.. (1980). Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp. Journal of Bacteriology. 143(3). 1165–1170. 7 indexed citations
4.
Buckel, Wolfgang & H.A. Barker. (1974). Two Pathways of Glutamate Fermentation by Anaerobic Bacteria. Journal of Bacteriology. 117(3). 1248–1260. 186 indexed citations
5.
Herbst‐Kralovetz, Melissa M., et al.. (1973). Enzymic Preparation ofL-β-Lysine. Preparative Biochemistry. 3(1). 47–52. 4 indexed citations
6.
Zappia, Vincenzo, et al.. (1970). Lysine 2,3-Aminomutase. Journal of Biological Chemistry. 245(7). 1778–1789. 153 indexed citations
7.
Barker, H.A., et al.. (1969). Activation of L-Citramalate Hydrolyase from Clostridium tetanomorphum. Journal of Biological Chemistry. 244(10). 2527–2538. 9 indexed citations
8.
Blair, A. H. & H.A. Barker. (1966). Assay and Purification of (+)-Citramalate Hydro-lyase Components from Clostridium tetanomorphum. Journal of Biological Chemistry. 241(2). 400–408. 26 indexed citations
9.
Costilow, Ralph N., Olga Rochovansky, & H.A. Barker. (1966). Isolation and Identification of β-Lysine as an Intermediate in Lysine Fermentation. Journal of Biological Chemistry. 241(7). 1573–1580. 46 indexed citations
10.
Volcani, B. E., John I. Toohey, & H.A. Barker. (1961). Detection of cobamide coenzymes in microorganisms by the ionophoretic-bioautographic method. Archives of Biochemistry and Biophysics. 92(3). 381–391. 29 indexed citations
11.
Ladd, J.N., Harry P. C. Hogenkamp, & H.A. Barker. (1961). Structure of Cobamide Coenzymes: Influence of pH on Absorption Spectra and Ionophoretic Mobilities. Journal of Biological Chemistry. 236(7). 2114–2118. 53 indexed citations
12.
Barker, H.A., Robert D. Smyth, Herbert Weissbach, et al.. (1960). Assay, Purification, and Properties of the Adenylcobamide Coenzyme. Journal of Biological Chemistry. 235(1). 181–190. 157 indexed citations
13.
Ladd, J.N., Harry P. C. Hogenkamp, & H.A. Barker. (1960). Observations on the structure of cobamide coenzymes. Biochemical and Biophysical Research Communications. 2(3). 143–146. 12 indexed citations
14.
Ellenbogen, Leon, et al.. (1960). Inhibition of cobamide coenzyme activity by intrinsic factor. Biochemical and Biophysical Research Communications. 3(2). 178–181. 7 indexed citations
15.
Weissbach, Herbert, John I. Toohey, & H.A. Barker. (1959). ISOLATION AND PROPERTIES OF B 12 COENZYMES CONTAINING BENZIMIDAZOLE OR DIMETHYLBENZIMIDAZOLE. Proceedings of the National Academy of Sciences. 45(4). 521–525. 70 indexed citations
16.
Peel, J. L. & H.A. Barker. (1956). The reduction of vinylacetate by Clostridium kluyveri and its dependence on catalytic amounts of high-energy acetate. Biochemical Journal. 62(2). 323–332. 6 indexed citations
17.
Pine, Leo, Victoria Haas, & H.A. Barker. (1954). METABOLISM OF GLUCOSE BY BUTYRIBACTERIUM RETTGERI. Journal of Bacteriology. 68(2). 227–230. 10 indexed citations
18.
Katz, Joseph, I Lieberman, & H.A. Barker. (1953). Formation of Propionyl-, Butyryl-, and other Acylglycines by Enzymes of Clostridium Kluyveri. Journal of Biological Chemistry. 200(1). 431–441. 10 indexed citations
19.
Stadtman, Thressa C. & H.A. Barker. (1951). STUDIES ON THE METHANE FERMENTATION IX. Journal of Bacteriology. 61(1). 81–86. 64 indexed citations
20.
Stadtman, Thressa C. & H.A. Barker. (1951). STUDIES ON THE METHANE FERMENTATION VIII. Journal of Bacteriology. 61(1). 67–80. 39 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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