Matthew Newman

1.2k total citations
16 papers, 959 citations indexed

About

Matthew Newman is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Matthew Newman has authored 16 papers receiving a total of 959 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 5 papers in Materials Chemistry and 4 papers in Biotechnology. Recurrent topics in Matthew Newman's work include RNA and protein synthesis mechanisms (5 papers), Enzyme Structure and Function (5 papers) and DNA and Nucleic Acid Chemistry (4 papers). Matthew Newman is often cited by papers focused on RNA and protein synthesis mechanisms (5 papers), Enzyme Structure and Function (5 papers) and DNA and Nucleic Acid Chemistry (4 papers). Matthew Newman collaborates with scholars based in United Kingdom, United States and Denmark. Matthew Newman's co-authors include Ira Schildkraut, Teresa E. Strzelecka, Lydia F. Dorner, Aneel K. Aggarwal, Tom L. Blundell, Keith D. Lunnen, Simon E. V. Phillips, Geoffrey G. Wilson, Ian J. Tickle and Carlos Frazão and has published in prestigious journals such as Nature, Science and The EMBO Journal.

In The Last Decade

Matthew Newman

16 papers receiving 939 citations

Peers

Matthew Newman

GENET

BIOTE

ECOLO

Guy Dodson United Kingdom

Kay Diederichs Germany

С.В. Никонов Russia

P McPhie United States

Mark Safro Israel

A.N. Lebedev Russia

Kin‐ichiro Miura Japan

Sue Ellen Gerchman United States

Arnthór Aevarsson Iceland

Christoph Scheich Germany

Guy Dodson United Kingdom

Matthew Newman

656 ×0.8

163 ×0.7

GENET

128 ×0.8

62 ×0.7

BIOTE

86 ×1.3

ECOLO

Citations per year, relative to Matthew Newman Matthew Newman (= 1×) peers Guy Dodson

Countries citing papers authored by Matthew Newman

Since Specialization

Citations

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

Fields of papers citing papers by Matthew Newman

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Matthew Newman

This figure shows the co-authorship network connecting the top 25 collaborators of Matthew Newman. A scholar is included among the top collaborators of Matthew Newman 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 Matthew Newman. Matthew Newman 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

Newman, Matthew, et al.. (2020). Design and synthesis of 4-[4-formyl-3-(2-naphthyl)pyrazol-1-yl]benzoic acid derivatives as potent growth inhibitors of drug-resistant Staphylococcus aureus. The Journal of Antibiotics. 73(12). 818–827. 18 indexed citations

Ali, Mohamad Akbar, et al.. (2018). Hexafluoroisopropanol-Mediated Domino Reaction for the Synthesis of Thiazolo-androstenones: Potent Anticancer Agents. ACS Omega. 3(12). 17991–18001. 12 indexed citations

Newman, Matthew, Judith Murray‐Rust, John Lally, et al.. (2005). Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition. The EMBO Journal. 24(5). 895–905. 87 indexed citations

Lally, John, Matthew Newman, Judith Murray‐Rust, et al.. (2004). Crystallization of the xeroderma pigmentosum group F endonuclease fromAeropyrum pernix. Acta Crystallographica Section D Biological Crystallography. 60(9). 1658–1661. 1 indexed citations

Newman, Matthew, et al.. (1998). Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence. The EMBO Journal. 17(18). 5466–5476. 125 indexed citations

Aguilar, C. F., Nora Cronin, M. Badasso, et al.. (1997). The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae. Journal of Molecular Biology. 267(4). 899–915. 29 indexed citations

Newman, Matthew, Teresa E. Strzelecka, Lydia F. Dorner, Ira Schildkraut, & Aneel K. Aggarwal. (1995). Structure of Bam HI Endonuclease Bound to DNA: Partial Folding and Unfolding on DNA Binding. Science. 269(5224). 656–663. 252 indexed citations

Strzelecka, Teresa E., et al.. (1994). Crystallization and Preliminary X-ray Analysis of Restriction Endonuclease BamHI-DNA Complex. Journal of Molecular Biology. 239(3). 430–432. 6 indexed citations

Newman, Matthew, Teresa E. Strzelecka, Lydia F. Dorner, Ira Schildkraut, & Aneel K. Aggarwal. (1994). Structure of restriction endonuclease BamHI and its relationship to EcoRI. Nature. 368(6472). 660–664. 143 indexed citations

10.

Newman, Matthew, et al.. (1994). Structure of restriction endonuclease BamHI phased at 1.95 å resolution by MAD analysis. Structure. 2(5). 439–452. 51 indexed citations

11.

Aguilar, C. F., Matthew Newman, J. Sanz‐Aparicio, et al.. (1993). The use of protein homologues in the rotation function. Acta Crystallographica Section A Foundations of Crystallography. 49(2). 306–315. 3 indexed citations

12.

Newman, Matthew, P. Roychowdhury, M. Badasso, et al.. (1993). X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus.. PubMed. 230(1). 260–83. 37 indexed citations

13.

Dhanaraj, V., Chris Dealwis, Carlos Frazão, et al.. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature. 357(6378). 466–472. 102 indexed citations

14.

Pitts, Jim E., V. Dhanaraj, Chris Dealwis, et al.. (1992). Multidisciplinary cycles for protein engineering: Site-directed mutagenesis and X-ray structural studies of aspartic proteinases. Scandinavian Journal of Clinical and Laboratory Investigation. 52(sup210). 39–50. 18 indexed citations

15.

Cooper, J.B. & Matthew Newman. (1991). X-Ray Structural Studies of Mammalian Aspartic Proteinases. Advances in experimental medicine and biology. 306. 47–61. 2 indexed citations

16.

Newman, Matthew, Mark Safro, Carlos Frazão, et al.. (1991). X-ray analyses of aspartic proteinases IV. Journal of Molecular Biology. 221(4). 1295–1309. 73 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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