L. Juliano

468 total citations
23 papers, 387 citations indexed

About

L. Juliano is a scholar working on Molecular Biology, Genetics and Oncology. According to data from OpenAlex, L. Juliano has authored 23 papers receiving a total of 387 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 8 papers in Genetics and 5 papers in Oncology. Recurrent topics in L. Juliano's work include Coagulation, Bradykinin, Polyphosphates, and Angioedema (8 papers), Chemical Synthesis and Analysis (5 papers) and Peptidase Inhibition and Analysis (5 papers). L. Juliano is often cited by papers focused on Coagulation, Bradykinin, Polyphosphates, and Angioedema (8 papers), Chemical Synthesis and Analysis (5 papers) and Peptidase Inhibition and Analysis (5 papers). L. Juliano collaborates with scholars based in Brazil, Denmark and United States. L. Juliano's co-authors include Jair R. Chagas, Eline S. Prado, María A. Juliano, Morten Meldal, Elaine Del Nery, Júlio Scharfstein, Ib Svendsen, Eloíza H. Tajara, Eurı́dice Carmona and Gustavo Orlando Bonilla‐Rodriguez and has published in prestigious journals such as Analytical Biochemistry, Biochemical and Biophysical Research Communications and British Journal of Pharmacology.

In The Last Decade

L. Juliano

23 papers receiving 384 citations

Peers

L. Juliano
Tami Ueda Japan
Jeffrey Neumann United States
Thomas S. Fletcher United States
Marieke Lamers United Kingdom
Mandy Cromwell United States
Li-Shan Hsieh United States
L. Juliano
Citations per year, relative to L. Juliano L. Juliano (= 1×) peers Thaysa Paschoalin

Countries citing papers authored by L. Juliano

Since Specialization
Citations

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

Fields of papers citing papers by L. Juliano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L. Juliano

This figure shows the co-authorship network connecting the top 25 collaborators of L. Juliano. A scholar is included among the top collaborators of L. Juliano 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 L. Juliano. L. Juliano 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.
Sato, Paloma Mieko, Adriana Rios Lopes, L. Juliano, María A. Juliano, & Walter R. Terra. (2008). Subsite substrate specificity of midgut insect chymotrypsins. Insect Biochemistry and Molecular Biology. 38(6). 628–633. 16 indexed citations
2.
Murakami, M.T., Hamilton Cabral, Eloíza H. Tajara, et al.. (2008). Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii. Protein and Peptide Letters. 15(7). 724–730. 12 indexed citations
3.
Cabral, Hamilton, Andréia Machado Leopoldino, Eloíza H. Tajara, et al.. (2005). Preliminary Functional Characterization, Cloning and Primary Sequence of Fastuosain, a Cysteine Peptidase Isolated from Fruits of Bromelia fastuosa. Protein and Peptide Letters. 13(1). 83–89. 22 indexed citations
4.
Hilaire, Phaedria M. St., Morten Meldal, Sanya J. Sanderson, et al.. (2001). Identification of peptides inhibitory to recombinant cysteine proteinase, CPB, of Leishmania mexicana. Molecular and Biochemical Parasitology. 114(1). 81–88. 18 indexed citations
5.
Melo, Robson L., Elisa Perissutti, Giuseppe Caliendo, et al.. (2001). Synthesis and hydrolysis by cathepsin B of fluorogenic substrates with the general structure benzoyl-X-ARG-MCA containing non-natural basic amino acids at position X. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1547(1). 82–94. 22 indexed citations
6.
Hilaire, Phaedria M. St., Sanya J. Sanderson, Jeremy C. Mottram, et al.. (2000). The Substrate Specificity of a Recombinant Cysteine Protease from Leishmania mexicana: Application of a Combinatorial Peptide Library Approach. ChemBioChem. 1(2). 115–122. 10 indexed citations
7.
Emim, José Artur da Silva, Caden Souccar, Rosely Oliveira Godinho, et al.. (2000). Evidence for activation of the tissue kallikrein‐kinin system in nociceptive transmission and inflammatory responses of mice using a specific enzyme inhibitor. British Journal of Pharmacology. 130(5). 1099–1107. 19 indexed citations
8.
Juliano, María A., Elaine Del Nery, L. Juliano, et al.. (1999). Chromogenic and fluorogenic glycosylated and acetylglycosylated peptides as substrates for serine, thiol and aspartyl proteases. Journal of Peptide Research. 53(2). 109–119. 4 indexed citations
9.
Nery, Elaine Del, Jair R. Chagas, María A. Juliano, L. Juliano, & Eline S. Prado. (1999). Comparison of human and porcine tissue kallikrein substrate specificities. Immunopharmacology. 45(1-3). 151–157. 6 indexed citations
10.
Meldal, Morten, Ib Svendsen, L. Juliano, et al.. (1998). Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay.D-Amino Acid Inhibitors for cruzipain, cathepsin B and cathepsin L. Journal of Peptide Science. 4(2). 83–91. 41 indexed citations
11.
Gomes, Roseli Aparecida da Silva, L. Juliano, Jair R. Chagas, & Valdemar Hial. (1997). Characterization of kininogenase activity of an acidic proteinase isolated from human kidney.. PubMed. 75(6). 757–61. 2 indexed citations
12.
Vanhoof, Greet, Filip Goossens, María A. Juliano, et al.. (1997). Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P). Cytogenetic and Genome Research. 78(3-4). 275–280. 8 indexed citations
13.
Juliano, L., et al.. (1997). Synthesis of N alpha-protected aminoacyl 7-amino-4-methyl-coumarin amide by phosphorous oxychloride and preparation of specific fluorogenic substrates for papain.. PubMed. 9(2). 92–6. 40 indexed citations
14.
Antunes, Edson, Fernanda Calheta Vieira Portaro, María A. Juliano, et al.. (1996). Pharmacological characterization of novel tissue kallikrein inhibitors in vivo. Immunopharmacology. 32(1-3). 111–114. 3 indexed citations
15.
Juliano, L., et al.. (1996). [Antithrombin III dosage using the chromogenic substrate Tos-Gly-Pro-Arg-NAN, in several pathological situations].. PubMed. 41(6). 373–8. 1 indexed citations
16.
Chao, Julie, et al.. (1992). Comparative Studies on P2 Specificity of Wild-Type Rat Tissue Kallikrein, Y99H:W215G Mutant and Tonin. Birkhäuser Basel eBooks. 38 ( Pt 1). 59–65. 1 indexed citations
17.
Chagas, Jair R., L. Juliano, & Eline S. Prado. (1991). Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Analytical Biochemistry. 192(2). 419–425. 109 indexed citations
18.
Juliano, L., et al.. (1990). The anti-leishmanial activity of dipeptide esters onLeishmania amazonensisamastigotes. Parasitology. 100(2). 201–207. 5 indexed citations
19.
Juliano, L., et al.. (1990). A selective assay for endooligopeptidase a based on the cleavage of fluorogenic substrate structurally related to enkephalin. Biochemical and Biophysical Research Communications. 173(2). 647–652. 34 indexed citations
20.
Juliano, L., et al.. (1989). Rat Submandibular Gland Kallikreins A and B: Isolation, Purification and Properties. Advances in experimental medicine and biology. 247B. 163–168. 1 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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