J. Habash

1.6k total citations
39 papers, 1.3k citations indexed

About

J. Habash is a scholar working on Materials Chemistry, Molecular Biology and Radiation. According to data from OpenAlex, J. Habash has authored 39 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Materials Chemistry, 25 papers in Molecular Biology and 8 papers in Radiation. Recurrent topics in J. Habash's work include Enzyme Structure and Function (24 papers), Protein Structure and Dynamics (13 papers) and Glycosylation and Glycoproteins Research (5 papers). J. Habash is often cited by papers focused on Enzyme Structure and Function (24 papers), Protein Structure and Dynamics (13 papers) and Glycosylation and Glycoproteins Research (5 papers). J. Habash collaborates with scholars based in United Kingdom, France and Israel. J. Habash's co-authors include John R. Helliwell, James Raftery, S.J. Harrop, J. Yariv, William N. Hunter, Trevor J. Greenhough, A. Joseph Kalb, Miroslav Z. Papiz, John W. Campbell and T. Gleichmann and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

J. Habash

39 papers receiving 1.3k 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. Habash United Kingdom 16 895 580 176 148 130 39 1.3k
W. A. Paciorek Switzerland 14 1.8k 2.0× 736 1.3× 127 0.7× 38 0.3× 162 1.2× 28 2.7k
Hideo Ago Japan 25 2.0k 2.2× 668 1.2× 114 0.6× 144 1.0× 171 1.3× 56 3.1k
Nelly R. Hajizadeh Germany 7 1.3k 1.5× 528 0.9× 106 0.6× 64 0.4× 77 0.6× 10 1.9k
E. Gordon France 16 819 0.9× 499 0.9× 80 0.5× 75 0.5× 239 1.8× 23 1.4k
M. Schiltz Switzerland 19 1.0k 1.1× 566 1.0× 97 0.6× 61 0.4× 49 0.4× 46 1.8k
Mirosława Dauter United States 25 1.3k 1.5× 876 1.5× 175 1.0× 94 0.6× 33 0.3× 52 1.9k
Eric de La Fortelle United Kingdom 11 2.2k 2.4× 898 1.5× 78 0.4× 53 0.4× 114 0.9× 14 2.8k
David G. Waterman United Kingdom 16 1.1k 1.3× 686 1.2× 76 0.4× 149 1.0× 84 0.6× 35 1.8k
C. Barberato Brazil 7 2.4k 2.6× 1.2k 2.1× 118 0.7× 53 0.4× 92 0.7× 9 3.1k
Christian Gorba Germany 9 1.3k 1.4× 485 0.8× 66 0.4× 42 0.3× 96 0.7× 9 1.8k

Countries citing papers authored by J. Habash

Since Specialization
Citations

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

Fields of papers citing papers by J. Habash

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Habash

This figure shows the co-authorship network connecting the top 25 collaborators of J. Habash. A scholar is included among the top collaborators of J. Habash 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. Habash. J. Habash 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.
Helliwell, John R., A.M.T. Bell, Patrick Bryant, et al.. (2010). Time-dependent analysis of K2PtBr6binding to lysozyme studied by protein powder and single crystal X-ray analysis. Zeitschrift für Kristallographie. 225(12). 570–575. 10 indexed citations
2.
Habash, J., John R. Helliwell, James Raftery, et al.. (2004). The structure and refinement of apocrustacyanin C2to 1.3 Å resolution and the search for differences between this protein and the homologous apoproteins A1and C1. Acta Crystallographica Section D Biological Crystallography. 60(3). 493–498. 9 indexed citations
3.
Chayen, Naomi E., Michele Cianci, J. Günter Grossmann, et al.. (2003). Unravelling the structural chemistry of the colouration mechanism in lobster shell. Acta Crystallographica Section D Biological Crystallography. 59(12). 2072–2082. 77 indexed citations
4.
Habash, J., et al.. (2003). The properties of (2Fo−Fc) and (Fo− Fc) electron-density maps at medium-to-high resolutions. Acta Crystallographica Section D Biological Crystallography. 59(5). 843–849. 5 indexed citations
5.
Habash, J., Titus J. Boggon, James Raftery, et al.. (2003). Apocrustacyanin C1crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons. Acta Crystallographica Section D Biological Crystallography. 59(7). 1117–1123. 9 indexed citations
6.
Helliwell, John R., J. Habash, Paul Faulder, et al.. (2002). Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase. Faraday Discussions. 122. 131–144. 17 indexed citations
7.
8.
Habash, J., James Raftery, R. H. Nuttall, et al.. (2000). Direct determination of the positions of the deuterium atoms of the bound water in concanavalin A by neutron Laue crystallography. Acta Crystallographica Section D Biological Crystallography. 56(5). 541–550. 50 indexed citations
9.
Chayen, Naomi E., Titus J. Boggon, Alberto Cassetta, et al.. (1996). Trends and Challenges in Experimental Macromolecular Crystallography. Quarterly Reviews of Biophysics. 29(3). 227–278. 68 indexed citations
10.
Naismith, James H., J. Habash, S.J. Harrop, et al.. (1994). Refined structure of concanavalin A complexed with methyl α-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure. Acta Crystallographica Section D Biological Crystallography. 50(6). 847–858. 122 indexed citations
11.
Cassetta, Alberto, Ashley M. Deacon, J. Habash, et al.. (1993). The emergence of the synchrotron Laue method for rapid data collection from protein crystals. Proceedings of the Royal Society of London Series A Mathematical and Physical Sciences. 442(1914). 177–192. 6 indexed citations
12.
Zhang, Yihong, Susan Bailey, James H. Naismith, et al.. (1993). Trypanosoma cruzi Trypanothione Reductase Crystallization, Unit Cell Dimensions and Structure Solution. Journal of Molecular Biology. 232(4). 1217–1220. 7 indexed citations
13.
Naismith, James H., J. Habash, S.J. Harrop, et al.. (1993). Refined structure of cadmium-substituted concanavalin A at 2.0 Å resolution. Acta Crystallographica Section D Biological Crystallography. 49(6). 561–571. 26 indexed citations
14.
Cameron, Alexander D., Stephen J. Smerdon, Anthony J. Wilkinson, et al.. (1993). Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by x-ray crystallography and infrared spectroscopy. Biochemistry. 32(48). 13061–13070. 59 indexed citations
15.
Hunter, William N., Susan Bailey, J. Habash, et al.. (1992). Active site of trypanothione reductase. Journal of Molecular Biology. 227(1). 322–333. 107 indexed citations
16.
Habash, J. & A. J. Smith. (1990). Structure of disodium triaquatri-μ-sulfato-thorate(IV) trihydrate. Acta Crystallographica Section C Crystal Structure Communications. 46(6). 957–960. 4 indexed citations
17.
Hunter, William N., Keith Smith, Zygmunt S. Derewenda, et al.. (1990). Initiating a crystallographic study of trypanothione reductase. Journal of Molecular Biology. 216(2). 235–237. 17 indexed citations
18.
Helliwell, M., et al.. (1989). A comparison of Laue and monochromatic X-ray analyses: the determination of the hydrogen-atom positions of an organic small-molecule crystal. Acta Crystallographica Section B Structural Science. 45(6). 591–596. 13 indexed citations
19.
Yariv, J., A. Joseph Kalb, Miroslav Z. Papiz, et al.. (1987). Properties of a new crystal form of the complex of concanavalin a with methyl α-d-glucopyranoside. Journal of Molecular Biology. 195(3). 759–760. 10 indexed citations
20.
Clifton, I.J., D. W. J. Cruickshank, G. P. Diakun, et al.. (1985). Synchrotron X-radiation protein crystallography: CEA film absorption factor as a function of wavelength 0.3≤λ≤2Å. Journal of Applied Crystallography. 18(5). 296–300. 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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