Barbara Giabbai

899 total citations
17 papers, 407 citations indexed

About

Barbara Giabbai is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Barbara Giabbai has authored 17 papers receiving a total of 407 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Materials Chemistry and 3 papers in Infectious Diseases. Recurrent topics in Barbara Giabbai's work include Biochemical and Molecular Research (6 papers), Enzyme Structure and Function (4 papers) and Protein Structure and Dynamics (3 papers). Barbara Giabbai is often cited by papers focused on Biochemical and Molecular Research (6 papers), Enzyme Structure and Function (4 papers) and Protein Structure and Dynamics (3 papers). Barbara Giabbai collaborates with scholars based in Italy, United States and Austria. Barbara Giabbai's co-authors include Massimo Degano, Ian A. Wilson, Max Crispin, Mitchell Kronenberg, Paola Storici, Angela Bachi, Stéphane Sidobre, Nicola Demitri, Barbara Skerlavaj and Arianna Fornili and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

Barbara Giabbai

16 papers receiving 399 citations

Peers

Barbara Giabbai
Frank Zucker United States
Natascha Mueller United States
Melanie N. Hug Switzerland
Theodora U. J. Bruun United States
Matthew R. Birck United States
Bowen Jin China
Barbara Giabbai
Citations per year, relative to Barbara Giabbai Barbara Giabbai (= 1×) peers Anne Bonhoure

Countries citing papers authored by Barbara Giabbai

Since Specialization
Citations

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

Fields of papers citing papers by Barbara Giabbai

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Barbara Giabbai

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

All Works

17 of 17 papers shown
1.
Tripathi, Shailesh, Marina Veronesi, Debora Russo, et al.. (2022). Identification of Novel GSK-3β Hits Using Competitive Biophysical Assays. International Journal of Molecular Sciences. 23(7). 3856–3856. 4 indexed citations
2.
Battista, Theo, Gianni Colotti, Jessica Rosati, et al.. (2021). Known Drugs Identified by Structure-Based Virtual Screening Are Able to Bind Sigma-1 Receptor and Increase Growth of Huntington Disease Patient-Derived Cells. International Journal of Molecular Sciences. 22(3). 1293–1293. 5 indexed citations
3.
Tripathi, Shailesh, Rita Maria Concetta Di Martino, Da Shi, et al.. (2021). ARN25068, a versatile starting point towards triple GSK-3β/FYN/DYRK1A inhibitors to tackle tau-related neurological disorders. European Journal of Medicinal Chemistry. 229. 114054–114054. 13 indexed citations
4.
Costanzi, Elisa, Maria Kuzikov, Francesca Esposito, et al.. (2021). Structural and Biochemical Analysis of the Dual Inhibition of MG-132 against SARS-CoV-2 Main Protease (Mpro/3CLpro) and Human Cathepsin-L. International Journal of Molecular Sciences. 22(21). 11779–11779. 49 indexed citations
5.
Veggiani, Gianluca, Barbara Giabbai, Marta S. Semrau, et al.. (2019). Comparative analysis of fusion tags used to functionalize recombinant antibodies. Protein Expression and Purification. 166. 105505–105505. 17 indexed citations
6.
Martino, Rita Maria Concetta Di, Shailesh Tripathi, Barbara Giabbai, et al.. (2019). Investigating Drug–Target Residence Time in Kinases through Enhanced Sampling Simulations. Journal of Chemical Theory and Computation. 15(8). 4646–4659. 36 indexed citations
7.
Marchetti, Marialaura, Gianluca Paredi, Heinz Amenitsch, et al.. (2019). Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. International Journal of Molecular Sciences. 20(20). 5219–5219. 10 indexed citations
8.
Raboni, Samanta, Svetlana V. Revtovich, Nicola Demitri, et al.. (2018). Engineering methionine γ-lyase from Citrobacter freundii for anticancer activity. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866(12). 1260–1270. 13 indexed citations
9.
Fornili, Arianna, Barbara Giabbai, G. Garau, & Massimo Degano. (2010). Energy Landscapes Associated with Macromolecular Conformational Changes from Endpoint Structures. Journal of the American Chemical Society. 132(49). 17570–17577. 15 indexed citations
10.
Giabbai, Barbara, Laura Muzzolini, Vittoria Matafora, et al.. (2008). Structural Basis for Substrate Specificity in Group I Nucleoside Hydrolases,. Biochemistry. 47(15). 4418–4426. 33 indexed citations
11.
Giabbai, Barbara, Stéphane Sidobre, Max Crispin, et al.. (2005). Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation. The Journal of Immunology. 175(2). 977–984. 103 indexed citations
12.
Moro, Monica, Virginia Cecconi, Chiara Martinoli, et al.. (2005). Generation of functional HLA-DR*1101 tetramers receptive for loading with pathogen or tumour derived synthetic peptides. BMC Immunology. 6(1). 24–24. 17 indexed citations
13.
Tomasinsig, Linda, Barbara Skerlavaj, Niv Papo, et al.. (2005). Mechanistic and Functional Studies of the Interaction of a Proline-rich Antimicrobial Peptide with Mammalian Cells. Journal of Biological Chemistry. 281(1). 383–391. 49 indexed citations
14.
Giabbai, Barbara & Massimo Degano. (2004). Cloning, purification, crystallization and X-ray analysis of theEscherichia colipyrimidine nucleoside hydrolase YeiK. Acta Crystallographica Section D Biological Crystallography. 60(3). 524–527. 3 indexed citations
15.
Giabbai, Barbara & Massimo Degano. (2004). Crystal Structure to 1.7 Å of the Escherichia coli Pyrimidine Nucleoside Hydrolase YeiK, a Novel Candidate for Cancer Gene Therapy. Structure. 12(5). 739–749. 37 indexed citations
16.
Degano, Massimo, et al.. (2004). Crystal structure of mouse CD1d with a phospholipid self ligand: insights in the molecular basis of regulatory NKT cell activation. Acta Crystallographica Section A Foundations of Crystallography. 60(a1). s146–s146. 2 indexed citations
17.
Giabbai, Barbara, et al.. (2004). Structural and functional characterization of bacterial YeiK nucleoside hydrolase fromE. coli: catalytic mechanism and possible role in cancer gene therapy. Acta Crystallographica Section A Foundations of Crystallography. 60(a1). s148–s148. 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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