K. E. T. Kerling

493 total citations
38 papers, 366 citations indexed

About

K. E. T. Kerling is a scholar working on Molecular Biology, Organic Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, K. E. T. Kerling has authored 38 papers receiving a total of 366 indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 12 papers in Organic Chemistry and 6 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in K. E. T. Kerling's work include Chemical Synthesis and Analysis (30 papers), RNA and protein synthesis mechanisms (12 papers) and Protein Structure and Dynamics (9 papers). K. E. T. Kerling is often cited by papers focused on Chemical Synthesis and Analysis (30 papers), RNA and protein synthesis mechanisms (12 papers) and Protein Structure and Dynamics (9 papers). K. E. T. Kerling collaborates with scholars based in Netherlands and Germany. K. E. T. Kerling's co-authors include E. Havinga, Servaas Visser, W. Bloemhoff, Jan Raap, Peter Hoogerhout, Henk J. Vreeman, A. C. A. Jansen, H.J. Geerligs, Wicher J. Weijer and Jan W. Drijfhout and has published in prestigious journals such as Journal of Virology, Biochemical Journal and Biochemical and Biophysical Research Communications.

In The Last Decade

K. E. T. Kerling

36 papers receiving 319 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
K. E. T. Kerling Netherlands	12	299	96	49	37	31	38	366
J. Watson Canada	5	346 1.2×	54 0.6×	17 0.3×	13 0.4×	31 1.0×	9	492
Claus‐W. von der Lieth Germany	11	453 1.5×	235 2.4×	37 0.8×	8 0.2×	58 1.9×	14	535
Natesa Muthukumaraswamy United States	11	368 1.2×	79 0.8×	23 0.5×	13 0.4×	17 0.5×	22	519
Manuel H. Jimenez United States	8	309 1.0×	98 1.0×	35 0.7×	8 0.2×	11 0.4×	12	371
Dirk Kramer Germany	9	176 0.6×	91 0.9×	21 0.4×	12 0.3×	30 1.0×	13	351
Alexander S. McColl United States	6	256 0.9×	92 1.0×	44 0.9×	3 0.1×	42 1.4×	8	378
Mollie N. Pflumm United States	8	320 1.1×	72 0.8×	64 1.3×	11 0.3×	56 1.8×	9	420
John W. Jensen United States	13	469 1.6×	229 2.4×	6 0.1×	22 0.6×	13 0.4×	17	551
Hiroko Hama-Inaba Japan	12	311 1.0×	23 0.2×	34 0.7×	11 0.3×	14 0.5×	28	399
Roopa Kenoth India	13	318 1.1×	104 1.1×	20 0.4×	15 0.4×	39 1.3×	22	402

Countries citing papers authored by K. E. T. Kerling

Since Specialization

Citations

This map shows the geographic impact of K. E. T. Kerling'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 K. E. T. Kerling with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites K. E. T. Kerling more than expected).

Fields of papers citing papers by K. E. T. Kerling

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by K. E. T. Kerling. 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 K. E. T. Kerling. The network helps show where K. E. T. Kerling may publish in the future.

Co-authorship network of co-authors of K. E. T. Kerling

This figure shows the co-authorship network connecting the top 25 collaborators of K. E. T. Kerling. A scholar is included among the top collaborators of K. E. T. Kerling 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 K. E. T. Kerling. K. E. T. Kerling 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

Rüterjans, Heinz, et al.. (1988). ¹⁵N‐ and ¹H‐NMR investigations of the active‐site amino acids in semisynthetic RNase S′ and RNase A. European Journal of Biochemistry. 172(2). 485–497. 5 indexed citations

Weijer, Wicher J., Jan W. Drijfhout, H.J. Geerligs, et al.. (1988). Antibodies against synthetic peptides of herpes simplex virus type 1 glycoprotein D and their capability to neutralize viral infectivity in vitro. Journal of Virology. 62(2). 501–510. 42 indexed citations

Hoogerhout, Peter, et al.. (1985). Synthesis of the glycotripeptide alanyl‐(O‐β‐D‐galactopyranosylseryl)‐alanine using (9‐fluorenylmethoxy)carbonyl and esters of 2‐(hydroxymethyl)‐9,10‐anthraquinone as temporary protecting groups. Recueil des Travaux Chimiques des Pays-Bas. 104(2). 54–59. 13 indexed citations

Bloemhoff, W., et al.. (1984). Studies on polypeptides XL. The role of histidine‐119 in non‐covalent semisynthetic ribonuclease; its replacement by 3‐(3‐pyrazolyl)‐L‐alanine, N^π‐methyl‐L‐histidine and N^τ‐methyl‐L‐histidine. Recueil des Travaux Chimiques des Pays-Bas. 103(2). 50–54. 2 indexed citations

Kerling, K. E. T., et al.. (1983). Studies on polypeptides XXXIX. The role of the imidazole tele‐nitrogen atom of histidine‐12 in the catalytic action of RNase S′. Recueil des Travaux Chimiques des Pays-Bas. 102(3). 140–147. 5 indexed citations

Raap, Jan, K. E. T. Kerling, Henk J. Vreeman, & Servaas Visser. (1983). Peptide substrates for chymosin (rennin): Conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction. Archives of Biochemistry and Biophysics. 221(1). 117–124. 28 indexed citations

Kerling, K. E. T., et al.. (1981). Studies on polypeptides XXXVI. Chemical semisynthesis of a ribonuclease A analogue ([13‐isoleucine, 20‐homoserine] ‐ ribonuclease A). Recueil des Travaux Chimiques des Pays-Bas. 100(5). 215–216. 2 indexed citations

Raap, Jan, et al.. (1980). Studies on polypeptides XXXIII: Semisynthetic Ribonuclease analogues. The role of histidine‐119. Recueil des Travaux Chimiques des Pays-Bas. 99(11). 349–352. 4 indexed citations

Visser, Servaas, et al.. (1977). Peptide substrates for chymosin (Rennin) Kinetic studies with bovine κ-casein-(103–108)-hexapeptide analogues. Biochimica et Biophysica Acta (BBA) - Enzymology. 481(1). 171–176. 27 indexed citations

10.

Raap, Jan, et al.. (1976). Studies on polypeptides XVIII Solid‐phase synthesis of RNase S‐peptide analogues with high S‐protein activating ability; replacement of histidine‐12 by L‐homohistidine. Recueil des Travaux Chimiques des Pays-Bas. 95(11). 278–281. 8 indexed citations

11.

Kerling, K. E. T., et al.. (1976). Synthesis and enzymatic activity of an RNase S′ analogue in which the 4‐imidazolylglycyl residue takes the position and the role of histidine‐12. FEBS Letters. 68(2). 228–230. 7 indexed citations

12.

Kerling, K. E. T., et al.. (1976). AN IMPROVED SYNTHESIS OF tert‐ BUTYLOXYCARBONYL‐L‐HISTIDINE. International journal of peptide & protein research. 8(1). 1–2. 14 indexed citations

13.

Bloemhoff, W. & K. E. T. Kerling. (1975). Studies on polypeptides XV Synthesis of L‐ and D‐homohistidine. Recueil des Travaux Chimiques des Pays-Bas. 94(8). 182–185. 14 indexed citations

14.

Raap, Jan, et al.. (1975). A partially synthetic highly active ribonuclease S analogue in which L-homohistidine replaces histidine-12 as the operative component. Tetrahedron Letters. 16(51). 4591–4594. 3 indexed citations

15.

Hessing, J. G. M., et al.. (1971). Studies on polypeptides. XIII: Relation between structure and capacity to function as rennin substrate: (Short communication). Recueil des Travaux Chimiques des Pays-Bas. 90(12). 1320–1322. 13 indexed citations

16.

Visser, Servaas, Jan Raap, K. E. T. Kerling, & E. Havinga. (1970). Studies on polypeptides. Part IX: Combination of solid‐phase and classical methods of peptide synthesis in the preparation of 1‐13[13‐Leucine] bovine pancreatic ribonuclease. Recueil des Travaux Chimiques des Pays-Bas. 89(8). 865–875. 10 indexed citations

17.

Visser, Servaas & K. E. T. Kerling. (1970). Studies on polypeptides. Part XI: Fragment condensation by azide coupling with a polymer‐bound peptide. The synthesis of 1‐13[10‐Citrulline, 13‐Leucine] bovine pancreatic ribonuclease. Recueil des Travaux Chimiques des Pays-Bas. 89(8). 880–884. 4 indexed citations

18.

Visser, Servaas, et al.. (1968). Studies on polypeptides VI: Synthesis of protected hexa‐ and octa‐peptide hydrazides related to the N‐terminal part of bovine pancreatic ribonuclease a using the solid‐phase method. Recueil des Travaux Chimiques des Pays-Bas. 87(5). 559–571. 15 indexed citations

19.

Havinga, E., et al.. (1964). Studies on polypeptides I: Synthesis and activity of angiotensin analogues (mostly heptapeptides) in which the arginine moiety is replaced by similar residues of varied structure and configuration. Recueil des Travaux Chimiques des Pays-Bas. 83(7). 672–676. 10 indexed citations

20.

Kerling, K. E. T., et al.. (1964). Studies on polypeptides III: Synthesis of the heptapeptides (des‐Asp¹)‐Arg²‐Ile⁵‐Angiotensin II, (des‐Asp¹)‐D Arg²‐Ile⁵‐Angiotensin II, (des‐Asp¹)‐ Har²‐Ile⁵‐Angiotensin II, (des‐Asp¹)‐D Har²‐Ile⁵‐Angiotensin II and the octapeptides Asp¹ (NH₂)‐Ile⁵‐Angiotensin II, Asp¹ (NH₂)‐D Arg²‐Ile⁵‐Angiotensin II and Gly¹‐Ile⁵‐Angiotensin II. Recueil des Travaux Chimiques des Pays-Bas. 83(7). 684–688. 2 indexed citations

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