H. Van Dael

1.0k total citations
37 papers, 885 citations indexed

About

H. Van Dael is a scholar working on Molecular Biology, Materials Chemistry and Food Science. According to data from OpenAlex, H. Van Dael has authored 37 papers receiving a total of 885 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 18 papers in Materials Chemistry and 12 papers in Food Science. Recurrent topics in H. Van Dael's work include Protein Structure and Dynamics (22 papers), Enzyme Structure and Function (18 papers) and Proteins in Food Systems (11 papers). H. Van Dael is often cited by papers focused on Protein Structure and Dynamics (22 papers), Enzyme Structure and Function (18 papers) and Proteins in Food Systems (11 papers). H. Van Dael collaborates with scholars based in Belgium, United Kingdom and United States. H. Van Dael's co-authors include Christopher C. Arico-Muendel, Christopher M. Dobson, Frans Van Cauwelaert, Marcel Joniau, Donald T. Haynie, Peter L. Privalov, Yuri Griko, Ernesto Freire, Rossella Gottardo and Angelo Fontana and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

H. Van Dael

37 papers receiving 866 citations

Peers

H. Van Dael

PHYSI

Ignace Hanssens Belgium

Yuri Griko United States

Kira A. Markossian Russia

Tara Sprules Canada

J R Garel France

Joan F Back Australia

Tatsuki Kashiwagi Japan

Shinya Ohki Japan

Purnananda Guptasarma India

Enrique García‐Hernández Mexico

Ignace Hanssens Belgium

H. Van Dael

480 ×0.7

153 ×0.4

197 ×0.8

149 ×1.4

27 ×0.4

PHYSI

Citations per year, relative to H. Van Dael H. Van Dael (= 1×) peers Ignace Hanssens

Countries citing papers authored by H. Van Dael

Since Specialization

Citations

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

Fields of papers citing papers by H. Van Dael

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of H. Van Dael

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

All Works

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20 of 20 papers shown

Farkas, Viktor, et al.. (2005). Tryptophan to phenylalanine substitutions allow differentiation of short‐ and long‐range conformational changes during denaturation of goat α‐lactalbumin. Proteins Structure Function and Bioinformatics. 60(1). 118–130. 10 indexed citations

Dael, H. Van, et al.. (2003). Equilibrium and kinetic studies on folding of canine milk lysozyme. Protein Science. 12(3). 609–619. 9 indexed citations

Laureto, Patrizia Polverino de, Erica Frare, Rossella Gottardo, H. Van Dael, & Angelo Fontana. (2002). Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Science. 11(12). 2932–2946. 88 indexed citations

Dael, H. Van, et al.. (2002). Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. Journal of Inorganic Biochemistry. 88(1). 69–76. 36 indexed citations

Joniau, Marcel, et al.. (2001). Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and α‐lactalbumin. Proteins Structure Function and Bioinformatics. 44(1). 1–11. 5 indexed citations

Hanssens, Ignace, et al.. (1998). The Perturbations of the Native State of Goat α-Lactalbumin Induced by 1,1′-Bis(4-Anilino-5-Naphthalenesulfonate) Are Ca2+-Dependent. Biophysical Journal. 75(5). 2195–2204. 16 indexed citations

Dael, H. Van. (1998). Chimeras of human lysozyme and ? -lactalbumin: an interesting tool for studying partially folded states during protein folding. Cellular and Molecular Life Sciences. 54(11). 1217–1230. 13 indexed citations

Aerts, Tony, et al.. (1997). Interaction of detergents with bovine lens α-crystallin: evidence for an oligomeric structure based on amphiphilic interactions. European Biophysics Journal. 25(5-6). 445–454. 15 indexed citations

Dael, H. Van, et al.. (1997). Conformational stability of LYLA1, a synthetic chimera of human lysozyme and bovine α-lactalbumin. European Biophysics Journal. 25(3). 171–179. 7 indexed citations

10.

Morozova‐Roche, Ludmilla A., et al.. (1997). Structural characterisation and comparison of the native and A-states of equine lysozyme. Journal of Molecular Biology. 268(5). 903–921. 58 indexed citations

11.

Haynie, Donald T., et al.. (1995). Structural basis of the stability of a lysozyme molten globule. Nature Structural Biology. 2(10). 871–875. 109 indexed citations

12.

Joniau, Marcel, et al.. (1995). An Equilibrium Partially Folded State of Human Lysozyme at Low pH. Journal of Molecular Biology. 246(3). 382–387. 62 indexed citations

13.

Dael, H. Van, et al.. (1993). Partially folded states of equine lysozyme. Structural characterization and significance for protein folding. Biochemistry. 32(44). 11886–11894. 70 indexed citations

14.

Joniau, Marcel, et al.. (1993). Stability effects associated with the introduction of a partial and a complete Ca²⁺-binding site into human lysozyme. Protein Engineering Design and Selection. 6(6). 643–649. 15 indexed citations

15.

Dael, H. Van, et al.. (1992). Conformational aspects of the Cu2+ binding to α-lactalbumin. Characterization and stability of the Cu-bound state. Biophysical Chemistry. 42(3). 235–242. 7 indexed citations

16.

Noppe, Wim, et al.. (1992). Hydrophobic interaction of lysozyme and α-lactalbumin from equine milk whey. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1122(3). 305–310. 13 indexed citations

17.

Desmet, Jan, et al.. (1991). Thermodynamics of Mn2+-binding to goat α-lactalbumin. European Biophysics Journal. 20(5). 263–268. 5 indexed citations

18.

Dael, H. Van, et al.. (1989). Molecular structure of carrageenans and kappa oligomers: a Raman spectroscopic study. International Journal of Biological Macromolecules. 11(5). 259–264. 26 indexed citations

19.

Desmet, Johan, H. Van Dael, Frans Van Cauwelaert, Katsutoshi Nitta, & Shintaro Sugai. (1989). Comparison of the binding of Ca2+ and Mn2+ to bovine α-lactalbumin and equine lysozyme. Journal of Inorganic Biochemistry. 37(3). 185–191. 26 indexed citations

20.

Dael, H. Van & Frans Van Cauwelaert. (1988). The effect of α-lactalbumin on the thermotropic phase behaviour of phosphatidylcholine bilayers, studied by fluorescence polarization, differential scanning calorimetry and Raman spectroscopy. Biochimica et Biophysica Acta (BBA) - Biomembranes. 943(2). 126–136. 5 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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