Gaetano Speciale

1.2k total citations
16 papers, 474 citations indexed

About

Gaetano Speciale is a scholar working on Molecular Biology, Organic Chemistry and Biotechnology. According to data from OpenAlex, Gaetano Speciale has authored 16 papers receiving a total of 474 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 11 papers in Organic Chemistry and 6 papers in Biotechnology. Recurrent topics in Gaetano Speciale's work include Carbohydrate Chemistry and Synthesis (10 papers), Enzyme Production and Characterization (6 papers) and Glycosylation and Glycoproteins Research (5 papers). Gaetano Speciale is often cited by papers focused on Carbohydrate Chemistry and Synthesis (10 papers), Enzyme Production and Characterization (6 papers) and Glycosylation and Glycoproteins Research (5 papers). Gaetano Speciale collaborates with scholars based in Australia, United Kingdom and United States. Gaetano Speciale's co-authors include Spencer J. Williams, G.J. Davies, Andrew J. Thompson, Anna Bernardi, Filippo Nisic, Ethan D. Goddard‐Borger, Yi Jin, Max J. Temple, Harry J. Gilbert and Z. Hakki and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Gaetano Speciale

16 papers receiving 469 citations

Peers

Countries citing papers authored by Gaetano Speciale

Since Specialization

Citations

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

Fields of papers citing papers by Gaetano Speciale

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gaetano Speciale

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

All Works

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16 of 16 papers shown

#	Work	Indexed citations
1	Reengineering the specificity of the highly selective Clostridium botulinum protease via directed evolution 2022 ·Scientific Reports ·(unknown), (unknown), (unknown), Gaetano Speciale, Madison H. Fletcher, (unknown), Yi Liu, Karen Brami‐Cherrier, (unknown), (unknown), (unknown), (unknown), (unknown), (unknown), Benjamin B. Katz, Lance E. Steward, Sudipta Majumdar, Amy Brideau-Andersen, Gregory A. Weiss	6
2	An Epoxide Intermediate in Glycosidase Catalysis 2020 ·ACS Central Science ·L.F. Sobala, Gaetano Speciale, Sha Zhu, Lluı́s Raich, (unknown), Andrew J. Thompson, Z. Hakki, Dan Lu, (unknown), Andrew R. Lewis, (unknown), Ganeko Bernardo‐Seisdedos, Yongmin Zhang, Óscar Millet, Jesús Jiménez‐Barbero, Andrew J. Bennet, Matthieu Sollogoub, Carme Rovira, G.J. Davies, Spencer J. Williams	40
3	Photostable and Proteolysis-Resistant Förster Resonance Energy Transfer-Based Calcium Biosensor 2020 ·Analytical Chemistry ·(unknown), (unknown), (unknown), (unknown), (unknown), Gaetano Speciale, (unknown), Sudipta Majumdar, Gregory A. Weiss, Elliot L. Botvinick	6
4	Distortion of mannoimidazole supports a B_2,5 boat transition state for the family GH125 α-1,6-mannosidase from Clostridium perfringens 2019 ·Organic & Biomolecular Chemistry ·(unknown), Gaetano Speciale, Spencer J. Williams, G.J. Davies	9
5	Electrochemical Quantification of Glycated and Non-glycated Human Serum Albumin in Synthetic Urine 2019 ·ACS Applied Materials & Interfaces ·(unknown), (unknown), Gaetano Speciale, Sudipta Majumdar, (unknown), Emily C. Sanders, Reginald M. Penner, Gregory A. Weiss	22
6	A Bacteroidetes locus dedicated to fungal 1,6-β-glucan degradation: Unique substrate conformation drives specificity of the key endo-1,6-β-glucanase 2017 ·Journal of Biological Chemistry ·Max J. Temple, Fiona Cuskin, Arnaud Baslé, (unknown), Gaetano Speciale, Spencer J. Williams, Harry J. Gilbert, Elisabeth C. Lowe	66
7	Selective Manipulation of Discrete Mannosidase Activities in the Endoplasmic Reticulum by Using Reciprocally Selective Inhibitors 2017 ·ChemBioChem ·(unknown), Makoto Hirano, Gaetano Speciale, Spencer J. Williams, Yukishige Ito, Kiichiro Totani	15
8	YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids 2016 ·Nature Chemical Biology ·Gaetano Speciale, Yi Jin, G.J. Davies, Spencer J. Williams, Ethan D. Goddard‐Borger	62
9	C2-Oxyanion Neighboring Group Participation: Transition State Structure for the Hydroxide-Promoted Hydrolysis of 4-Nitrophenyl α-d-Mannopyranoside 2016 ·Journal of the American Chemical Society ·Gaetano Speciale, (unknown), (unknown), Spencer J. Williams, Andrew J. Bennet	24
10	Evidence for a Boat Conformation at the Transition State of GH76 α‐1,6‐Mannanases—Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism 2015 ·Angewandte Chemie International Edition ·Andrew J. Thompson, Gaetano Speciale, Javier Iglesias‐Fernández, Z. Hakki, (unknown), Alan Cartmell, Richard J. Spears, (unknown), Max J. Temple, Judith Stepper, Harry J. Gilbert, Carme Rovira, Spencer J. Williams, G.J. Davies	43
11	Evidence for a Boat Conformation at the Transition State of GH76 α‐1,6‐Mannanases—Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism 2015 ·Angewandte Chemie ·Andrew J. Thompson, Gaetano Speciale, Javier Iglesias‐Fernández, Z. Hakki, (unknown), Alan Cartmell, Richard J. Spears, (unknown), Max J. Temple, Judith Stepper, Harry J. Gilbert, Carme Rovira, Spencer J. Williams, G.J. Davies	1
12	Dissecting conformational contributions to glycosidase catalysis and inhibition 2014 ·Current Opinion in Structural Biology ·Gaetano Speciale, Andrew J. Thompson, G.J. Davies, Spencer J. Williams	114
13	Structural and Kinetic Dissection of the endo‐α‐1,2‐Mannanase Activity of Bacterial GH99 Glycoside Hydrolases from Bacteroides spp. 2014 ·Chemistry - A European Journal ·Z. Hakki, Andrew J. Thompson, (unknown), Gaetano Speciale, G.J. Davies, Spencer J. Williams	18
14	9‐Fluorenone‐2‐Carboxylic Acid as a Scaffold for Tubulin Interacting Compounds 2013 ·ChemPlusChem ·Francesco Calogero, (unknown), Gaetano Speciale, Michael S. Christodoulou, Daniele Cartelli, Dario Ballinari, Francesco Sola, Clara Albanese, Antonella Ciavolella, Daniele Passarella, Graziella Cappelletti, Stefano Pieraccini, Maurizio Sironi	8
15	A Facile Synthesis of α-N-Ribosyl-Asparagine and α-N-Ribosyl-Glutamine Building Blocks 2013 ·Molecules ·Gaetano Speciale, Anna Bernardi, Filippo Nisic	10
16	Stereoselective Synthesis of α‐ and β‐Glycofuranosyl Amides by Traceless Ligation of Glycofuranosyl Azides 2012 ·Chemistry - A European Journal ·Filippo Nisic, Gaetano Speciale, Anna Bernardi	30

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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