H.P.C. Driessen

2.3k total citations
41 papers, 1.9k citations indexed

About

H.P.C. Driessen is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, H.P.C. Driessen has authored 41 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 14 papers in Materials Chemistry and 8 papers in Physiology. Recurrent topics in H.P.C. Driessen's work include Connexins and lens biology (22 papers), Enzyme Structure and Function (14 papers) and Biochemical effects in animals (8 papers). H.P.C. Driessen is often cited by papers focused on Connexins and lens biology (22 papers), Enzyme Structure and Function (14 papers) and Biochemical effects in animals (8 papers). H.P.C. Driessen collaborates with scholars based in United Kingdom, Netherlands and Russia. H.P.C. Driessen's co-authors include C. Slingsby, H. Bloemendal, Peter F. Lindley, W.W. de Jong, D. S. Moss, B.D. Bax, Paul S. Freemont, V. Nalini, Tom L. Blundell and Alice Vrielink and has published in prestigious journals such as Nature, The EMBO Journal and Journal of Molecular Biology.

In The Last Decade

H.P.C. Driessen

41 papers receiving 1.9k 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.P.C. Driessen United Kingdom 24 1.7k 456 330 207 179 41 1.9k
G. Jogl United States 28 1.6k 1.0× 343 0.8× 193 0.6× 127 0.6× 201 1.1× 55 2.2k
Kyoko Ogasahara Japan 33 2.4k 1.4× 1.4k 3.1× 108 0.3× 257 1.2× 82 0.5× 91 2.8k
Manfred Buehner Germany 16 1.3k 0.8× 902 2.0× 102 0.3× 356 1.7× 260 1.5× 20 1.9k
Gregory D. Reinhart United States 25 1.6k 1.0× 463 1.0× 111 0.3× 320 1.5× 132 0.7× 75 2.0k
Heinz Gehring Switzerland 26 1.9k 1.2× 770 1.7× 62 0.2× 173 0.8× 213 1.2× 67 2.4k
Marcello Zambonin Italy 18 1.2k 0.7× 431 0.9× 147 0.4× 205 1.0× 38 0.2× 20 1.6k
Stephen J. Benkovic United States 32 2.7k 1.6× 353 0.8× 68 0.2× 150 0.7× 96 0.5× 57 3.4k
Bernard T. Kaufman United States 22 1.1k 0.6× 342 0.8× 96 0.3× 105 0.5× 138 0.8× 37 1.5k
J. Janin France 22 2.0k 1.2× 794 1.7× 65 0.2× 294 1.4× 40 0.2× 35 2.5k
Chin Yu Taiwan 24 1.2k 0.7× 209 0.5× 156 0.5× 206 1.0× 98 0.5× 83 1.5k

Countries citing papers authored by H.P.C. Driessen

Since Specialization
Citations

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

Fields of papers citing papers by H.P.C. Driessen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by H.P.C. Driessen. 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.P.C. Driessen. The network helps show where H.P.C. Driessen may publish in the future.

Co-authorship network of co-authors of H.P.C. Driessen

This figure shows the co-authorship network connecting the top 25 collaborators of H.P.C. Driessen. A scholar is included among the top collaborators of H.P.C. Driessen 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.P.C. Driessen. H.P.C. Driessen 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.
Tickle, Ian J. & H.P.C. Driessen. (2003). Molecular Replacement Using Known Structural Information. Humana Press eBooks. 56. 173–204. 1 indexed citations
2.
Zhao, Qiang, Sandeep Modi, Graeme C.M. Smith, et al.. (1999). Crystal structure of the FMN‐binding domain of human cytochrome P450 reductase at 1.93 Å resolution. Protein Science. 8(2). 298–306. 71 indexed citations
3.
Norledge, B.V., Eva‐Maria Mayr, Rudi Glockshuber, et al.. (1996). The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. Nature Structural Biology. 3(3). 267–274. 35 indexed citations
4.
Driessen, H.P.C., et al.. (1996). Structure of Bovine Eye Lens γD (γIIIb)-Crystallin at 1.95 Å. Acta Crystallographica Section D Biological Crystallography. 52(4). 712–721. 18 indexed citations
5.
Bammler, Theo K., H.P.C. Driessen, Niklas Finnström, & C. Roland Wolf. (1995). Amino Acid Differences at Positions 10, 11, and 104 Explain the Profound Catalytic Differences between Two Murine Pi-Class Glutathione S-Transferases. Biochemistry. 34(28). 9000–9008. 28 indexed citations
6.
Bateman, O.A., H.P.C. Driessen, Peter F. Lindley, et al.. (1994). The structure of avian eye lens δ-crystallin reveals a new fold for a superfamily of oligomeric enzymes. Nature Structural & Molecular Biology. 1(10). 724–734. 55 indexed citations
7.
Zarina, Shamshad, Zafar H. Zaidi, H.P.C. Driessen, et al.. (1994). Three‐dimensional model and quaternary structure of the human eye lens protein γS‐crystallin based on β‐ and γ‐crystallin X‐ray coordinates and ultracentrifugation. Protein Science. 3(10). 1840–1846. 25 indexed citations
8.
Dealwis, Chris, Carlos Frazão, M. Badasso, et al.. (1994). X-ray Analysis at 2·0 Å Resolution of Mouse Submaxillary Renin Complexed with a Decapeptide Inhibitor CH-66, Based on the 4-16 Fragment of Rat Angiotensinogen. Journal of Molecular Biology. 236(1). 342–360. 34 indexed citations
9.
Nalini, V., B.D. Bax, H.P.C. Driessen, et al.. (1994). Close packing of an oligomeric eye lens β-crystallin induces loss of symmetry and ordering of sequence extensions. Journal of Molecular Biology. 236(4). 1250–1258. 46 indexed citations
10.
Najmudin, Shabir, V. Nalini, H.P.C. Driessen, et al.. (1993). Structure of the bovine eye lens protein γB(γII)-crystallin at 1.47 Å. Acta Crystallographica Section D Biological Crystallography. 49(2). 223–233. 49 indexed citations
11.
Freemont, Paul S., Richard Newman, & H.P.C. Driessen. (1992). Janus-faced proteins. Current Biology. 2(2). 98–100. 3 indexed citations
12.
Dhanaraj, V., Chris Dealwis, Carlos Frazão, et al.. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature. 357(6378). 466–472. 102 indexed citations
13.
Wang, Dawei, H.P.C. Driessen, & Ian J. Tickle. (1991). MOLPACK: molecular graphics, for studying the packing of protein molecules in the crystallographic unit cell. Journal of Molecular Graphics. 9(1). 50–50. 9 indexed citations
14.
Lapatto, Risto, V. Nalini, B.D. Bax, et al.. (1991). High resolution structure of an oligomeric eye lens β-crystallin. Journal of Molecular Biology. 222(4). 1067–1083. 80 indexed citations
16.
Freemont, Paul S., H.P.C. Driessen, Winston Verbi, & Michaël J. Crumpton. (1990). Crystallization and preliminary X-ray crystallographic studies of human placental annexin IV. Journal of Molecular Biology. 216(2). 219–221. 3 indexed citations
17.
Bax, B.D., Risto Lapatto, V. Nalini, et al.. (1990). X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature. 347(6295). 776–780. 219 indexed citations
18.
Slingsby, C., H.P.C. Driessen, Daruka Mahadevan, B.D. Bax, & Tom L. Blundell. (1988). Evolutionary and functional relationships between the basic and acidic β-crystallins. Experimental Eye Research. 46(3). 375–403. 43 indexed citations
19.
White, Helen, H.P.C. Driessen, C. Slingsby, et al.. (1988). The use of pseudosymmetry in the rotation function of γIVa-crystallin. Acta Crystallographica Section B Structural Science. 44(2). 172–178. 5 indexed citations
20.
Driessen, H.P.C., Paul Herbrink, H. Bloemendal, & Wilfried W. de Jong. (1980). The β-crystallin bp chain is internally duplicated and homologous with γ-crystallin. Experimental Eye Research. 31(2). 243–246. 45 indexed citations

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