M.J. Levine

2.2k total citations
37 papers, 1.9k citations indexed

About

M.J. Levine is a scholar working on Molecular Biology, Physiology and Organic Chemistry. According to data from OpenAlex, M.J. Levine has authored 37 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 14 papers in Physiology and 8 papers in Organic Chemistry. Recurrent topics in M.J. Levine's work include Glycosylation and Glycoproteins Research (25 papers), Salivary Gland Disorders and Functions (14 papers) and Carbohydrate Chemistry and Synthesis (8 papers). M.J. Levine is often cited by papers focused on Glycosylation and Glycoproteins Research (25 papers), Salivary Gland Disorders and Functions (14 papers) and Carbohydrate Chemistry and Synthesis (8 papers). M.J. Levine collaborates with scholars based in United States, Canada and Taiwan. M.J. Levine's co-authors include Libuse A. Bobek, M. Srinivasulu Reddy, Aaron R Biesbrock, Lawrence A. Tabak, Hsin‐Yue Tsai, Mira Edgerton, Patricia Murray, Prateek Raj, M W Stinson and Earl J. Bergey and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Immunology and Biochemical Journal.

In The Last Decade

M.J. Levine

37 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.J. Levine United States 20 1.0k 629 573 268 260 37 1.9k
Janet R. Kimball United States 15 506 0.5× 529 0.8× 141 0.2× 176 0.7× 103 0.4× 16 1.8k
Hakimuddin T. Sojar United States 27 810 0.8× 1.5k 2.4× 200 0.3× 827 3.1× 23 0.1× 58 2.4k
Martin A. Imboden Switzerland 18 391 0.4× 327 0.5× 100 0.2× 186 0.7× 36 0.1× 27 1.2k
Naoya Ohara Japan 27 1.0k 1.0× 717 1.1× 94 0.2× 363 1.4× 12 0.0× 90 2.4k
I Carlstedt Sweden 34 1.8k 1.7× 32 0.1× 269 0.5× 125 0.5× 655 2.5× 51 2.9k
RI Lehrer United States 16 840 0.8× 37 0.1× 227 0.4× 92 0.3× 147 0.6× 22 2.1k
Andrew Levin United States 16 373 0.4× 522 0.8× 133 0.2× 444 1.7× 11 0.0× 35 1.6k
Bernhard B. Singer Germany 34 972 0.9× 44 0.1× 83 0.1× 111 0.4× 94 0.4× 92 2.9k
Michael D.P. Boyle United States 28 699 0.7× 49 0.1× 200 0.3× 984 3.7× 15 0.1× 103 2.4k
Wim van't Hof Netherlands 8 427 0.4× 72 0.1× 91 0.2× 66 0.2× 90 0.3× 8 882

Countries citing papers authored by M.J. Levine

Since Specialization
Citations

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

Fields of papers citing papers by M.J. Levine

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.J. Levine. 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 M.J. Levine. The network helps show where M.J. Levine may publish in the future.

Co-authorship network of co-authors of M.J. Levine

This figure shows the co-authorship network connecting the top 25 collaborators of M.J. Levine. A scholar is included among the top collaborators of M.J. Levine 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 M.J. Levine. M.J. Levine 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.
Tseng, Ching‐Chung, et al.. (2000). Differential Effect toward Inhibition of Papain and Cathepsin C by Recombinant Human Salivary Cystatin SN and Its Variants Produced by a Baculovirus System. Archives of Biochemistry and Biophysics. 380(1). 133–140. 15 indexed citations
2.
Miyamoto, Michael M., et al.. (1999). The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase. Archives of Oral Biology. 44(2). 119–127. 20 indexed citations
3.
Bobek, Libuse A., et al.. (1998). Tissue-specific expression of human salivary mucin gene, MUC7, in transgenic mice. Transgenic Research. 7(3). 195–204. 7 indexed citations
4.
Bobek, Libuse A., et al.. (1996). Structure and Chromosomal Localization of the Human Salivary Mucin Gene, MUC7. Genomics. 31(3). 277–282. 58 indexed citations
5.
Schifferle, Robert E., Mark E. Wilson, M.J. Levine, & Robert J. Genco. (1993). Activation of serum complement by polysaccharide‐containing antigens of Porphyromonas gingivalis. Journal of Periodontal Research. 28(4). 248–254. 19 indexed citations
6.
Bobek, Libuse A., et al.. (1993). Efficient production of biologically active human salivary cystatins in Escherichia coli. Gene. 123(2). 203–210. 16 indexed citations
7.
Schifferle, Robert E., et al.. (1993). Modification of experimental Porphyromonas gingivalis murine infection by immunization with a polysaccharide‐protein conjugate. Oral Microbiology and Immunology. 8(5). 266–271. 18 indexed citations
8.
Reddy, Molakala S., M.J. Levine, & W Paranchych. (1993). Low-Molecular-Mass Human Salivary Mucin, MG2: Structure and Binding of Pseudomonas aeruginosa. Critical Reviews in Oral Biology & Medicine. 4(3). 315–323. 25 indexed citations
9.
Ramasubbu, N., Leonard M. Thomas, Krishna K. Bhandary, & M.J. Levine. (1993). Structural Characteristics of Human Salivary Statherin: A Model for Boundary Lubrication at the Enamel Surface. Critical Reviews in Oral Biology & Medicine. 4(3). 363–370. 35 indexed citations
10.
Bobek, Libuse A., Hsin‐Yue Tsai, Aaron R Biesbrock, & M.J. Levine. (1993). Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7).. Journal of Biological Chemistry. 268(27). 20563–20569. 402 indexed citations
11.
Edgerton, Mira & M.J. Levine. (1992). Characterization of acquired denture pellicle from healthy and stomatitis patients. Journal of Prosthetic Dentistry. 68(4). 683–691. 64 indexed citations
12.
Cohen, Robert E., Alfredo Aguirre, Mirdza E. Neiders, et al.. (1991). Immunochemistry and immunogenicity of low molecular weight human salivary mucin. Archives of Oral Biology. 36(5). 347–356. 37 indexed citations
13.
Ramasubbu, N., Krishna K. Bhandary, Frank A. Scannapieco, & M.J. Levine. (1991). Crystallization and preliminary X‐ray diffraction studies of human salivary α‐amylase. Proteins Structure Function and Bioinformatics. 11(3). 230–232. 14 indexed citations
14.
Johnsson, Mats, Carl Richardson, Earl J. Bergey, M.J. Levine, & George H. Nancollas. (1991). The effects of human salivary cystatins and statherin on hydroxyapatite crystallization. Archives of Oral Biology. 36(9). 631–636. 71 indexed citations
15.
Schifferle, Robert E., M. Srinivasulu Reddy, Joseph J. Zambon, R. J. Genco, & M.J. Levine. (1989). Characterization of a polysaccharide antigen from Bacteroides gingivalis .. The Journal of Immunology. 143(9). 3035–3042. 70 indexed citations
16.
Linzer, R, M. Srinivasulu Reddy, & M.J. Levine. (1987). Structural studies of the serotype-f polysaccharide antigen from Streptococcus mutans OMZ175. Infection and Immunity. 55(12). 3006–3010. 11 indexed citations
17.
Tabak, Lawrence A., et al.. (1982). Structures of the O-glycosidic Units of a Mucin-gycoprotein from Rat Submandibular Glands. Journal of Dental Research. 61. 240. 3 indexed citations
18.
Levine, M.J. & Robert G. Spiro. (1979). Isolation from glomerular basement membrane of a glycopeptide containing both asparagine-linked and hydroxylysine-linked carbohydrate units.. Journal of Biological Chemistry. 254(17). 8121–8124. 36 indexed citations
19.
20.
Levine, M.J., Mark C. Herzberg, Melvin Levine, et al.. (1978). Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans. Infection and Immunity. 19(1). 107–115. 209 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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