Rudolf Gilmanshin

4.0k total citations · 2 hit papers
26 papers, 3.5k citations indexed

About

Rudolf Gilmanshin is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Rudolf Gilmanshin has authored 26 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 9 papers in Materials Chemistry and 6 papers in Cell Biology. Recurrent topics in Rudolf Gilmanshin's work include Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (9 papers) and Hemoglobin structure and function (6 papers). Rudolf Gilmanshin is often cited by papers focused on Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (9 papers) and Hemoglobin structure and function (6 papers). Rudolf Gilmanshin collaborates with scholars based in United States and Russia. Rudolf Gilmanshin's co-authors include Gennady V. Semisotnov, Robert Callender, R. Brian Dyer, William H. Woodruff, Н. А. Родионова, Vladimir N. Uversky, Oleg B. Ptitsyn, Skip Williams, Valentina E. Bychkova and Е. В. Бражников and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Accounts of Chemical Research and The Journal of Physical Chemistry B.

In The Last Decade

Rudolf Gilmanshin

26 papers receiving 3.4k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe

1991 1.1k citations Gennady V. Semisotnov, Н. А. Родионова et al. Biopolymers profile →
α‐lactalbumin: compact state with fluctuating tertiary structure?

1981 548 citations Д. А. Долгих, Rudolf Gilmanshin et al. FEBS Letters profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Rudolf Gilmanshin United States	17	2.6k	1.2k	469	427	390	26	3.5k
Klaus Gast Germany	38	2.3k 0.9×	929 0.8×	568 1.2×	733 1.7×	304 0.8×	115	3.9k
Darwin O. V. Alonso United States	28	2.4k 0.9×	1.0k 0.9×	358 0.8×	327 0.8×	251 0.6×	36	3.1k
Giuliano Siligardi United Kingdom	38	2.8k 1.1×	1.4k 1.1×	568 1.2×	294 0.7×	409 1.0×	165	5.3k
Arturo Muga Spain	34	3.1k 1.2×	634 0.5×	200 0.4×	266 0.6×	329 0.8×	107	3.9k
Katsuhide Yutani Japan	41	3.8k 1.5×	2.1k 1.8×	279 0.6×	143 0.3×	370 0.9×	154	4.5k
William H. Sawyer Australia	42	3.3k 1.3×	442 0.4×	588 1.3×	385 0.9×	355 0.9×	138	5.4k
Guy Duportail France	37	2.7k 1.0×	959 0.8×	686 1.5×	563 1.3×	251 0.6×	101	4.7k
Jochen Balbach Germany	33	2.6k 1.0×	989 0.8×	412 0.9×	169 0.4×	293 0.8×	127	3.4k
Gennady V. Semisotnov Russia	20	3.0k 1.2×	1.6k 1.3×	228 0.5×	128 0.3×	477 1.2×	52	3.7k
Philip A. Evans United Kingdom	28	3.2k 1.2×	2.0k 1.6×	517 1.1×	237 0.6×	382 1.0×	35	3.7k

Countries citing papers authored by Rudolf Gilmanshin

Since Specialization

Citations

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

Fields of papers citing papers by Rudolf Gilmanshin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rudolf Gilmanshin

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

All Works

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20 of 20 papers shown

Meltzer, Robert H., Lisa W. Kwok, R. E. Allen, et al.. (2011). A lab-on-chip for biothreat detection using single-molecule DNA mapping. Lab on a Chip. 11(5). 863–863. 34 indexed citations

Protozanova, Ekaterina, Meng Zhang, Eric J. White, et al.. (2010). Fast high-resolution mapping of long fragments of genomic DNA based on single-molecule detection. Analytical Biochemistry. 402(1). 83–90. 11 indexed citations

Burton, Randall E., Eric J. White, Ted R. Foss, et al.. (2010). A microfluidic chip-compatible bioassay based on single-molecule detection with high sensitivity and multiplexing. Lab on a Chip. 10(7). 843–843. 18 indexed citations

Foss, Ted R., et al.. (2009). A Single-Molecule System for Detection and Quantification of Proteins with Robust Capture Units and Potential for High Multiplexing. Biophysical Journal. 96(3). 25a–25a. 1 indexed citations

Mollova, Emilia T., Vishal Patil, Ekaterina Protozanova, Meng Zhang, & Rudolf Gilmanshin. (2009). An automated sample preparation system with mini-reactor to isolate and process submegabase fragments of bacterial DNA. Analytical Biochemistry. 391(2). 135–143. 7 indexed citations

Kwok, Lisa W., Yi Zhou, Robert H. Meltzer, et al.. (2009). An Integrated Multifunctional Lab-on-a-Chip Platform for High Throughput Optical Mapping of DNA. Biophysical Journal. 96(3). 48a–48a. 1 indexed citations

White, Eric J., et al.. (2009). Staphylococcus aureus Strain Typing by Single-Molecule DNA Mapping in Fluidic Microchips with Fluorescent Tags. Clinical Chemistry. 55(12). 2121–2129. 12 indexed citations

Larson, Jonathan W., Qun Zhong, Lori A. Neely, et al.. (2006). Single DNA molecule stretching in sudden mixed shear and elongational microflows. Lab on a Chip. 6(9). 1187–1199. 76 indexed citations

Chan, Eugene, Rebecca A. Haeusler, Jonathan W. Larson, et al.. (2004). DNA Mapping Using Microfluidic Stretching and Single-Molecule Detection of Fluorescent Site-Specific Tags. Genome Research. 14(6). 1137–1146. 136 indexed citations

10.

Gilmanshin, Rudolf, et al.. (1999). An FTIR Study of the Complex Melting Behavior of α-Lactalbumin. The Journal of Physical Chemistry B. 103(19). 3947–3953. 12 indexed citations

11.

Dyer, R. Brian, Feng Gai, William H. Woodruff, Rudolf Gilmanshin, & Robert Callender. (1998). Infrared Studies of Fast Events in Protein Folding. Accounts of Chemical Research. 31(11). 709–716. 158 indexed citations

12.

Callender, Robert, R. Brian Dyer, Rudolf Gilmanshin, & William H. Woodruff. (1998). FAST EVENTS IN PROTEIN FOLDING: The Time Evolution of Primary Processes. Annual Review of Physical Chemistry. 49(1). 173–202. 178 indexed citations

13.

Callender, Robert, Hua Deng, & Rudolf Gilmanshin. (1998). Raman difference studies of protein structure and folding, enzymatic catalysis and ligand binding. Journal of Raman Spectroscopy. 29(1). 15–21. 16 indexed citations

14.

Gilmanshin, Rudolf, et al.. (1997). Structural heterogeneity of the various forms of apomyoglobin; Implications for protein folding. Protein Science. 6(10). 2134–2142. 40 indexed citations

15.

Gilmanshin, Rudolf, Skip Williams, Robert Callender, William H. Woodruff, & R. Brian Dyer. (1997). Fast Events in Protein Folding: Relaxation Dynamics and Structure of the I Form of Apomyoglobin. Biochemistry. 36(48). 15006–15012. 56 indexed citations

16.

Gilmanshin, Rudolf, Carl E. Creutz, & Lukas K. Tamm. (1994). Annexin IV Reduces the Rate of Lateral Lipid Diffusion and Changes the Fluid Phase Structure of the Lipid Bilayer When It Binds to Negatively Charged Membranes in the Presence of Calcium. Biochemistry. 33(27). 8225–8232. 57 indexed citations

17.

Semisotnov, Gennady V., et al.. (1991). Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31(1). 119–128. 1142 indexed citations breakdown →

18.

Gilmanshin, Rudolf & Oleg B. Ptitsyn. (1987). An early intermediate of refolding α‐lactalbumin forms within 20 ms. FEBS Letters. 223(2). 327–329. 49 indexed citations

19.

Долгих, Д. А., I.A. Bolotina, Е. В. Бражников, et al.. (1985). Compact state of a protein molecule with pronounced small-scale mobility: bovine ?-lactalbumin. European Biophysics Journal. 13(2). 109–21. 228 indexed citations

20.

Долгих, Д. А., Rudolf Gilmanshin, Е. В. Бражников, et al.. (1981). α‐lactalbumin: compact state with fluctuating tertiary structure?. FEBS Letters. 136(2). 311–315. 548 indexed citations breakdown →

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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