J. Baz Jackson

2.3k total citations
87 papers, 1.8k citations indexed

About

J. Baz Jackson is a scholar working on Molecular Biology, Materials Chemistry and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, J. Baz Jackson has authored 87 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 78 papers in Molecular Biology, 39 papers in Materials Chemistry and 31 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in J. Baz Jackson's work include ATP Synthase and ATPases Research (48 papers), Enzyme Structure and Function (37 papers) and Photosynthetic Processes and Mechanisms (34 papers). J. Baz Jackson is often cited by papers focused on ATP Synthase and ATPases Research (48 papers), Enzyme Structure and Function (37 papers) and Photosynthetic Processes and Mechanisms (34 papers). J. Baz Jackson collaborates with scholars based in United Kingdom, United States and Netherlands. J. Baz Jackson's co-authors include Nick P.J. Cotton, Tania Bizouarn, Scott A. White, Jamie D. Venning, Philip G. Quirk, Christine P. Diggle, Tracy Palmer, Christopher M. Thomas, Rachel L. Grimley and Stuart J. Ferguson and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

J. Baz Jackson

87 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
J. Baz Jackson United Kingdom	27	1.5k	664	603	164	121	87	1.8k
Yutaka Orii Japan	23	1.1k 0.7×	86 0.1×	100 0.2×	40 0.2×	306 2.5×	83	1.6k
Ronald R. Fisher United States	23	828 0.5×	172 0.3×	145 0.2×	278 1.7×	95 0.8×	54	1.1k
Songzhou Hu United States	18	763 0.5×	330 0.5×	133 0.2×	8 0.0×	80 0.7×	23	1.4k
Chuan-pu Lee United States	18	995 0.6×	52 0.1×	62 0.1×	203 1.2×	193 1.6×	30	1.3k
Margareta Baltscheffsky Sweden	23	1.1k 0.7×	142 0.2×	24 0.0×	32 0.2×	203 1.7×	60	1.3k
Richard D. Spencer United States	13	853 0.6×	196 0.3×	38 0.1×	32 0.2×	144 1.2×	16	1.6k
Lennart Lundberg Sweden	20	762 0.5×	169 0.3×	23 0.0×	20 0.1×	91 0.8×	37	1.1k
I. B. C. Matheson United States	19	413 0.3×	235 0.4×	50 0.1×	19 0.1×	59 0.5×	42	1.1k
R. Timkovich United States	14	454 0.3×	161 0.2×	26 0.0×	16 0.1×	38 0.3×	20	611
C. Salet France	26	902 0.6×	514 0.8×	65 0.1×	54 0.3×	197 1.6×	68	1.9k

Countries citing papers authored by J. Baz Jackson

Since Specialization

Citations

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

Fields of papers citing papers by J. Baz Jackson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Baz Jackson

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Webster, Fiona, et al.. (2012). The impact of a hospitalist on role boundaries in an orthopedic environment. Journal of Multidisciplinary Healthcare. 5. 249–249. 9 indexed citations

Jackson, J. Baz. (2012). A review of the binding-change mechanism for proton-translocating transhydrogenase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(10). 1839–1846. 23 indexed citations

Quirk, Philip G., et al.. (2010). The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807(1). 85–94. 9 indexed citations

Iwaki, Masayo, et al.. (2009). Inhibition of proton-transfer steps in transhydrogenase by transition metal ions. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1787(10). 1276–1288. 15 indexed citations

Strambini, Giovanni B., et al.. (2008). Mutations in Transhydrogenase Change the Fluorescence Emission State of TRP72 from 1La to 1Lb. Biophysical Journal. 95(7). 3419–3428. 7 indexed citations

Quirk, Philip G., et al.. (2006). A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1757(3). 215–223. 5 indexed citations

Jackson, J. Baz, et al.. (2002). A conformational change in the isolated NADP(H)-binding component (dIII) of transhydrogenase induced by low pH: a reflection of events during proton translocation by the complete enzyme?. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1555(1-3). 8–13. 5 indexed citations

Pinheiro, Teresa J. T., Jamie D. Venning, & J. Baz Jackson. (2001). Fast Hydride Transfer in Proton-translocating Transhydrogenase Revealed in a Rapid Mixing Continuous Flow Device. Journal of Biological Chemistry. 276(48). 44757–44761. 20 indexed citations

Jackson, J. Baz, et al.. (2000). The NADP(H)-binding component (dIII) of human heart transhydrogenase: crystallization and preliminary crystallographic analysis. Acta Crystallographica Section D Biological Crystallography. 56(4). 489–491. 2 indexed citations

10.

White, Scott A., et al.. (2000). The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure. 8(1). 1–12. 75 indexed citations

11.

Venning, Jamie D., et al.. (2000). Stopped-flow Reaction Kinetics of Recombinant Components of Proton-translocating Transhydrogenase with Physiological Nucleotides. Journal of Biological Chemistry. 275(26). 19490–19497. 16 indexed citations

12.

Venning, Jamie D., et al.. (1999). Evidence for the stabilization of NADPH relative to NADP+ on the dIII components of proton-translocating transhydrogenases from Homo sapiens and from Rhodospirillum rubrum by measurement of tryptophan fluorescence. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1413(2). 81–91. 16 indexed citations

13.

Quirk, Philip G., et al.. (1999). The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1412(2). 139–148. 17 indexed citations

14.

Gupta, Susmita Sen, Philip G. Quirk, Jamie D. Venning, et al.. (1998). Mutation of amino acid residues in the mobile loop region of the NAD(H)-binding domain of proton-translocating transhydrogenase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1409(1). 25–38. 10 indexed citations

15.

Bizouarn, Tania, et al.. (1997). The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1322(1). 19–32. 24 indexed citations

16.

Bizouarn, Tania, Rachel L. Grimley, Christine P. Diggle, Christopher M. Thomas, & J. Baz Jackson. (1997). Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1320(3). 265–274. 19 indexed citations

17.

Bizouarn, Tania, et al.. (1995). The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1229(1). 49–58. 41 indexed citations

18.

Jackson, J. Baz & Matthew G. Goodwin. (1993). Electrochromic responses of bacteriochlorophyll absorbance bands in purified light-harvesting complexes of Rhodobacter capsulatus reconstituted into liposomes. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1144(2). 199–203. 5 indexed citations

19.

Sazanov, Leonid A. & J. Baz Jackson. (1993). Activation and inhibition of mitochondrial transhydrogenase by metal ions. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1144(2). 225–228. 6 indexed citations

20.

Richardson, David, Alastair G. McEwan, M. Dudley Page, J. Baz Jackson, & Stuart J. Ferguson. (1990). The identification of cytochromes involved in the transfer of electrons to the periplasmic NO⁻₃ reductase of Rhodobacter capsulatus and resolution of a soluble NO⁻₃ ‐reductase − cytochrome‐c₅₅₂ redox complex. European Journal of Biochemistry. 194(1). 263–270. 42 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.

Explore authors with similar magnitude of impact