J. Chaloupka

998 total citations
74 papers, 779 citations indexed

About

J. Chaloupka is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, J. Chaloupka has authored 74 papers receiving a total of 779 indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 34 papers in Biotechnology and 21 papers in Plant Science. Recurrent topics in J. Chaloupka's work include Enzyme Production and Characterization (32 papers), Phytase and its Applications (19 papers) and Enzyme Structure and Function (15 papers). J. Chaloupka is often cited by papers focused on Enzyme Production and Characterization (32 papers), Phytase and its Applications (19 papers) and Enzyme Structure and Function (15 papers). J. Chaloupka collaborates with scholars based in Czechia, Belarus and Slovakia. J. Chaloupka's co-authors include V. Vinter, M. Höfer, Nadina Stadler, Karel Sigler, Jela Brozmanová, Helena Kučerová, Libuše Váchová, L. Říhová, R.J. Doyle and Jana Čechová and has published in prestigious journals such as Nature, Biochemical and Biophysical Research Communications and Applied Microbiology and Biotechnology.

In The Last Decade

J. Chaloupka

71 papers receiving 709 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. Chaloupka Czechia 15 431 308 178 130 118 74 779
S E Mainzer United States 10 573 1.3× 127 0.4× 95 0.5× 218 1.7× 116 1.0× 13 842
Mitsuo Takano Japan 16 500 1.2× 145 0.5× 346 1.9× 61 0.5× 61 0.5× 28 791
Suk‐Tae Kwon South Korea 18 743 1.7× 263 0.9× 146 0.8× 175 1.3× 105 0.9× 64 1.0k
Marie‐Francoise Hullo France 12 591 1.4× 209 0.7× 282 1.6× 282 2.2× 126 1.1× 12 1.1k
Clive F. Roberts United Kingdom 23 1.1k 2.5× 131 0.4× 305 1.7× 192 1.5× 140 1.2× 47 1.3k
Charles L. Wittenberger United States 17 551 1.3× 155 0.5× 75 0.4× 114 0.9× 171 1.4× 30 1.0k
V. Vinter Czechia 18 471 1.1× 144 0.5× 258 1.4× 214 1.6× 48 0.4× 48 892
Shannon B. Conners United States 17 654 1.5× 194 0.6× 138 0.8× 153 1.2× 135 1.1× 21 1.0k
Thomas B. May United States 11 615 1.4× 158 0.5× 173 1.0× 171 1.3× 41 0.3× 15 897
J. A. Garibaldi United States 20 309 0.7× 378 1.2× 207 1.2× 74 0.6× 51 0.4× 39 1.3k

Countries citing papers authored by J. Chaloupka

Since Specialization
Citations

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

Fields of papers citing papers by J. Chaloupka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of J. Chaloupka. A scholar is included among the top collaborators of J. Chaloupka 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. Chaloupka. J. Chaloupka 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.
Horáček, J, S Sulková, František Lopot, et al.. (2007). Resting energy expenditure and thermal balance during isothermic and thermoneutral haemodialysis heat production does not explain increased body temperature during haemodialysis. Nephrology Dialysis Transplantation. 22(12). 3553–3560. 10 indexed citations
2.
Kučerová, Helena, et al.. (2001). Differences in the Regulation of the Intracellular Ca2+-Dependent Serine Proteinase Activity Between Bacillus subtilis and B. megaterium. Current Microbiology. 42(3). 178–183. 3 indexed citations
3.
Sigler, Karel, J. Chaloupka, Jela Brozmanová, Nadina Stadler, & M. Höfer. (1999). Oxidative stress in microorganisms—I. Folia Microbiologica. 44(6). 587–624. 129 indexed citations
4.
Kučerová, Helena & J. Chaloupka. (1995). Intracellular serine proteinase behaves as a heat-stress protein in nongrowing but as a cold-stress protein in growing populations of Bacillus megaterium. Current Microbiology. 31(1). 39–43. 9 indexed citations
5.
Chaloupka, J., et al.. (1993). Sporulation and synthesis of extracellular proteinases inBacillus subtilis are more temperature-sensitive than growth. Folia Microbiologica. 38(1). 22–24. 14 indexed citations
6.
Pazlarová, J., et al.. (1993). Turnover of canavanine-containing proteins inSaccharomyces cerevisiae. Folia Microbiologica. 38(3). 225–228. 2 indexed citations
7.
Kučerová, Helena & J. Chaloupka. (1993). Netropsin inhibits the increase of intracellular Ca2+-dependent serine proteinase activity in sporulatingBacillus megaterium. Folia Microbiologica. 38(1). 10–14. 2 indexed citations
8.
Váchová, Libuše, et al.. (1990). Effect of actinomycin D on viability, sporulation and nucleotide pool ofBacillus megaterium. Folia Microbiologica. 35(3). 190–199. 2 indexed citations
9.
Moravcová, Jana & J. Chaloupka. (1990). Characteristics of intracellular proteolytic activities ofBacillus megaterium. Folia Microbiologica. 35(5). 402–412. 2 indexed citations
10.
Hao, Jin-Ping, et al.. (1989). Regulation of extracellular proteins and α-amylase secretion by temperature inBacillus subtilis. Folia Microbiologica. 34(3). 179–184. 2 indexed citations
11.
Chaloupka, J. & Helena Kučerová. (1988). Netropsin increases formation of mRNA coding for a neutral metalloproteinase in Bacillus megaterium. Journal of Basic Microbiology. 28(1-2). 11–16. 5 indexed citations
12.
Kučerová, Helena, et al.. (1986). Effect of temperature on growth and protein turnover in Bacillus megaterium. Journal of Basic Microbiology. 26(5). 289–298. 9 indexed citations
13.
Chaloupka, J., et al.. (1985). Temperature shiftup suppresses synthesis of extracellular proteins inBacillus megaterium. Current Microbiology. 12(1). 9–11. 1 indexed citations
14.
Chaloupka, J., et al.. (1983). Combined effect of temperature and nutrients on protein turnover inBacillus megaterium. Folia Microbiologica. 28(1). 46–50. 2 indexed citations
15.
Chaloupka, J., et al.. (1983). Initial kinetics of Protein turnover in growing yeast. Folia Microbiologica. 28(4). 274–281. 1 indexed citations
16.
Chaloupka, J., et al.. (1982). Kinetics of Protein Turnover in Growing Cells of Bacillus megaterium. Microbiology. 128(5). 1003–1008. 24 indexed citations
17.
Chaloupka, J., et al.. (1980). The complex effect of temperature on protein degradation in sporulatingBacillus megaterium. FEMS Microbiology Letters. 9(2). 107–110. 8 indexed citations
18.
Čechová, Jana & J. Chaloupka. (1978). Functional half-life of the exocellular protease mRNA ofBacillus megaterium. Folia Microbiologica. 23(5). 329–336. 7 indexed citations
19.
Chaloupka, J., et al.. (1975). Protease activity in cells ofBacillus megaterium during derepression. Folia Microbiologica. 20(4). 277–288. 21 indexed citations
20.
Chaloupka, J.. (1969). Dual control of megateriopeptidase synthesis.. PubMed. 117(5). 631–6. 14 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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