Gaetano Irace

2.4k total citations
76 papers, 2.1k citations indexed

About

Gaetano Irace is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Gaetano Irace has authored 76 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 36 papers in Cell Biology and 28 papers in Physiology. Recurrent topics in Gaetano Irace's work include Hemoglobin structure and function (34 papers), Protein Structure and Dynamics (26 papers) and Alzheimer's disease research and treatments (22 papers). Gaetano Irace is often cited by papers focused on Hemoglobin structure and function (34 papers), Protein Structure and Dynamics (26 papers) and Alzheimer's disease research and treatments (22 papers). Gaetano Irace collaborates with scholars based in Italy, Spain and United States. Gaetano Irace's co-authors include Ivana Sirangelo, Giovanni Colonna, Ettore Bismuto, Clara Iannuzzi, Ciro Balestrieri, Luigi Servillo, Raffaele Ragone, Alfonso Giovane, Silvia Vilasi and Margherita Borriello and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Gaetano Irace

76 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gaetano Irace Italy 25 1.4k 620 552 295 205 76 2.1k
Ivana Sirangelo Italy 24 837 0.6× 622 1.0× 231 0.4× 157 0.5× 69 0.3× 63 1.5k
Carmelo La Rosa Italy 29 1.8k 1.3× 1.3k 2.1× 296 0.5× 304 1.0× 120 0.6× 96 2.6k
Danilo Milardi Italy 35 2.1k 1.5× 1.5k 2.4× 391 0.7× 372 1.3× 130 0.6× 126 3.4k
R. Khurana United States 20 2.5k 1.8× 1.8k 2.9× 208 0.4× 522 1.8× 180 0.9× 31 3.8k
Vasanthy Narayanaswami United States 33 1.8k 1.3× 854 1.4× 158 0.3× 298 1.0× 219 1.1× 85 3.4k
Subramanian Vivekanandan United States 25 1.5k 1.1× 1.6k 2.6× 183 0.3× 319 1.1× 319 1.6× 69 2.9k
Andisheh Abedini United States 27 1.8k 1.3× 2.1k 3.4× 498 0.9× 201 0.7× 120 0.6× 35 3.1k
Parvez Alam India 37 2.2k 1.6× 1.0k 1.6× 175 0.3× 401 1.4× 148 0.7× 63 3.4k
Mario Bouchard United Kingdom 12 1.6k 1.2× 840 1.4× 105 0.2× 273 0.9× 202 1.0× 16 2.1k
Peter N. Lowe United Kingdom 30 1.9k 1.4× 313 0.5× 607 1.1× 343 1.2× 112 0.5× 73 2.6k

Countries citing papers authored by Gaetano Irace

Since Specialization
Citations

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

Fields of papers citing papers by Gaetano Irace

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gaetano Irace

This figure shows the co-authorship network connecting the top 25 collaborators of Gaetano Irace. A scholar is included among the top collaborators of Gaetano Irace 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 Gaetano Irace. Gaetano Irace 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.
Iannuzzi, Clara, Margherita Borriello, Vincenzo Carafa, et al.. (2015). D-ribose-glycation of insulin prevents amyloid aggregation and produces cytotoxic adducts. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1862(1). 93–104. 39 indexed citations
2.
Iannuzzi, Clara, Gaetano Irace, & Ivana Sirangelo. (2014). Differential effects of glycation on protein aggregation and amyloid formation. Frontiers in Molecular Biosciences. 1. 9–9. 106 indexed citations
3.
Infusini, Giuseppe, Clara Iannuzzi, Silvia Vilasi, et al.. (2012). Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F. European Biophysics Journal. 41(7). 615–627. 11 indexed citations
4.
Sirangelo, Ivana & Gaetano Irace. (2010). Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose. Expert Opinion on Therapeutic Targets. 14(12). 1311–1321. 23 indexed citations
5.
Sirangelo, Ivana, Clara Iannuzzi, Silvia Vilasi, et al.. (2009). W7FW14F apomyoglobin amyloid aggregates‐mediated apoptosis is due to oxidative stress and AKT inactivation caused by Ras and Rac. Journal of Cellular Physiology. 221(2). 412–423. 20 indexed citations
6.
Vilasi, Silvia, et al.. (2006). Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences. FEBS Letters. 580(6). 1681–1684. 13 indexed citations
7.
Sirangelo, Ivana, et al.. (2002). Tryptophanyl Substitutions in Apomyoglobin Determine Protein Aggregation and Amyloid-like Fibril Formation at Physiological pH. Journal of Biological Chemistry. 277(48). 45887–45891. 38 indexed citations
8.
Sirangelo, Ivana, et al.. (2002). Resolution of Tryptophan-ANS Fluorescence Energy Transfer in Apomyoglobin by Site-directed Mutagenesis¶. Photochemistry and Photobiology. 76(4). 381–381. 12 indexed citations
9.
D’Auria, Sabato, Mosé Rossi, Roberto Nucci, Gaetano Irace, & Ettore Bismuto. (1997). Perturbation of conformational dynamics, enzymatic activity, and thermostability of β-glycosidase from archaeonSulfolobus solfataricus by pH and sodium dodecyl sulfate detergent. Proteins Structure Function and Bioinformatics. 27(1). 71–79. 23 indexed citations
10.
Bismuto, Ettore & Gaetano Irace. (1994). Unfolding Pathway of Apomyoglobin. Journal of Molecular Biology. 241(1). 103–109. 19 indexed citations
11.
Sirangelo, Ivana, Ettore Bismuto, & Gaetano Irace. (1994). Solvent and thermal denaturation of the acidic compact state of apomyoglobin. FEBS Letters. 338(1). 11–15. 19 indexed citations
12.
Sirangelo, Ivana, Gaetano Irace, & Ettore Bismuto. (1994). RESOLUTION OF THE INDIVIDUAL TRYPTOPHANYL CONTRIBUTIONS TO THE NEAR‐ULTRAVIOLET DICHROIC ACTIVITY OF APOMYOGLOBIN. Photochemistry and Photobiology. 59(6). 611–614. 7 indexed citations
13.
Bismuto, Ettore, Ivana Sirangelo, & Gaetano Irace. (1992). Salt-induced refolding of myoglobin at acidic pH: Molecular properties of a partly folded intermediate. Archives of Biochemistry and Biophysics. 298(2). 624–629. 22 indexed citations
14.
Bismuto, Ettore, Ivana Sirangelo, & Gaetano Irace. (1989). Conformational substates of myoglobin detected by extrinsic dynamic fluorescence studies. Biochemistry. 28(19). 7542–7545. 19 indexed citations
15.
Bismuto, Ettore, Gaetano Irace, & Enrico Gratton. (1989). Multiple conformational states in myoglobin revealed by frequency domain fluorometry. Biochemistry. 28(4). 1508–1512. 24 indexed citations
16.
Bismuto, Ettore & Gaetano Irace. (1989). DYNAMIC FLUORESCENCE OF TRYPTOPHANYL RESIDUES IN LOW MOLECULAR WEIGHT MODEL COMPOUNDS AND PROTEINS. Photochemistry and Photobiology. 50(2). 165–168. 15 indexed citations
17.
Bismuto, Ettore, Giovanni Colonna, & Gaetano Irace. (1983). Unfolding pathway of myoglobin. Evidence for a multistate process. Biochemistry. 22(18). 4165–4170. 53 indexed citations
18.
Servillo, Luigi, Giovanni Colonna, Ciro Balestrieri, Raffaele Ragone, & Gaetano Irace. (1982). Simultaneous determination of tyrosine and tryptophan residues in proteins by second-derivative spectroscopy. Analytical Biochemistry. 126(2). 251–257. 78 indexed citations
19.
Colonna, Giovanni, Gaetano Irace, Giuseppe Parlato, Salvatore M. Aloj, & Ciro Balestrieri. (1978). The effect of evolution on homologous proteins: a comparison between the chromophore microenvironments of Italian water buffalo (Bos bubalus, L.) and sperm whale apomyoglobin.. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 532(2). 354–67. 23 indexed citations
20.
Balestrieri, Ciro, Giovanni Colonna, & Gaetano Irace. (1975). Amino acid sequence around a reactive cysteine of yeast alcohol dehydrogenase. Biochemical and Biophysical Research Communications. 66(3). 900–906. 4 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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