Carl G. Kolvenbach

571 total citations
15 papers, 436 citations indexed

About

Carl G. Kolvenbach is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Cell Biology. According to data from OpenAlex, Carl G. Kolvenbach has authored 15 papers receiving a total of 436 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 3 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Cell Biology. Recurrent topics in Carl G. Kolvenbach's work include Protein purification and stability (6 papers), Viral Infectious Diseases and Gene Expression in Insects (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). Carl G. Kolvenbach is often cited by papers focused on Protein purification and stability (6 papers), Viral Infectious Diseases and Gene Expression in Insects (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). Carl G. Kolvenbach collaborates with scholars based in United States and Greece. Carl G. Kolvenbach's co-authors include Michael J. Benecky, Michael W. Mosesson, Stephen R. Brych, Tsutomu Arakawa, Linda O. Narhi, Rahul S. Rajan, David L. Amrani, David N. Brems, Gerd R. Kleemann and Arnold McAuley and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

Carl G. Kolvenbach

15 papers receiving 429 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Carl G. Kolvenbach United States 11 300 138 57 50 42 15 436
Detlef Grunow Germany 11 575 1.9× 116 0.8× 73 1.3× 95 1.9× 23 0.5× 18 667
Susan Hochschwender United States 13 475 1.6× 232 1.7× 81 1.4× 42 0.8× 16 0.4× 15 812
Jerry M. Anchin United States 11 355 1.2× 182 1.3× 72 1.3× 77 1.5× 20 0.5× 21 472
Jason R. Porter United States 12 457 1.5× 111 0.8× 40 0.7× 55 1.1× 90 2.1× 13 662
Karl Proba Switzerland 8 537 1.8× 328 2.4× 96 1.7× 90 1.8× 41 1.0× 9 701
Vanita D. Sood United States 11 372 1.2× 111 0.8× 30 0.5× 64 1.3× 10 0.2× 15 488
Yoshitake Maeda Japan 11 362 1.2× 105 0.8× 38 0.7× 146 2.9× 19 0.5× 20 575
Kaori Esaki Japan 8 626 2.1× 399 2.9× 18 0.3× 48 1.0× 29 0.7× 8 736
Ankit Gupta United States 9 241 0.8× 86 0.6× 24 0.4× 64 1.3× 22 0.5× 22 370
Kathrin Zuberbühler United States 5 289 1.0× 136 1.0× 24 0.4× 62 1.2× 19 0.5× 5 468

Countries citing papers authored by Carl G. Kolvenbach

Since Specialization
Citations

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

Fields of papers citing papers by Carl G. Kolvenbach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Carl G. Kolvenbach. 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 Carl G. Kolvenbach. The network helps show where Carl G. Kolvenbach may publish in the future.

Co-authorship network of co-authors of Carl G. Kolvenbach

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

All Works

15 of 15 papers shown
1.
Agrawal, Neeraj J., et al.. (2018). Prediction of the Hydrogen Peroxide–Induced Methionine Oxidation Propensity in Monoclonal Antibodies. Journal of Pharmaceutical Sciences. 107(5). 1282–1289. 25 indexed citations
2.
Brych, Stephen R., et al.. (2010). Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates. Protein Science. 19(9). 1601–1615. 54 indexed citations
3.
McAuley, Arnold, Jaby Jacob, Carl G. Kolvenbach, et al.. (2007). Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain. Protein Science. 17(1). 95–106. 85 indexed citations
4.
Hoyte, Lennox, et al.. (2002). Variations in levator ani volume and geometry in women: the application of MR based 3D reconstruction in evaluating pelvic floor dysfunction.. PubMed. 54(6). 532–9. 10 indexed citations
5.
Kolvenbach, Carl G., et al.. (2000). Metal-Catalyzed Oxidation of Brain-Derived Neurotrophic Factor (BDNF): Analytical Challenges for the Identification of Modified Sites. Pharmaceutical Research. 17(2). 190–196. 8 indexed citations
6.
Kolvenbach, Carl G., Linda O. Narhi, John S. Philo, et al.. (1997). Granulocyte‐colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH 2. Journal of Peptide Research. 50(4). 310–318. 37 indexed citations
7.
Kolvenbach, Carl G., Steven Elliott, Raj Sachdev, Tsutomu Arakawa, & Linda O. Narhi. (1993). Characterization of two fluorescent tryptophans in recombinant human granulocyte-colony stimulating factor: Comparison of native sequence protein and tryptophan-deficient mutants. Journal of Protein Chemistry. 12(2). 229–236. 17 indexed citations
8.
Arakawa, Tsutomu, et al.. (1993). Analysis of the Heat-Induced Denaturation of Proteins Using Temperature Gradient Gel Electrophoresis. Analytical Biochemistry. 208(2). 255–259. 9 indexed citations
9.
Narhi, Linda O., Robert Rosenfeld, Jane Talvenheimo, et al.. (1993). Comparison of the biophysical characteristics of human brain-derived neurotrophic factor, neurotrophin-3, and nerve growth factor. Journal of Biological Chemistry. 268(18). 13309–13317. 55 indexed citations
10.
Benecky, Michael J., et al.. (1991). Ionic-strength- and pH-dependent conformational states of human plasma fibronectin. Biochemistry. 30(17). 4298–4306. 23 indexed citations
11.
Stabinsky, Y., Michael Levitt, Linda Miller, et al.. (1991). Enhanced stability of subtilisin by three point mutations. Biotechnology and Applied Biochemistry. 13(1). 12–24. 27 indexed citations
12.
Kolvenbach, Carl G., et al.. (1991). Densimetric determination of carbohydrate content in glycoproteins. Journal of Biochemical and Biophysical Methods. 23(4). 295–300. 7 indexed citations
13.
Benecky, Michael J., et al.. (1990). Human plasma fibronectin structure probed by steady-state fluorescence polarization: evidence for a rigid oblate structure. Biochemistry. 29(12). 3082–3091. 33 indexed citations
14.
Kolvenbach, Carl G., et al.. (1990). Comparative study on proteinase R, T, and K from Tritirachiam album limber. International journal of peptide & protein research. 36(4). 387–391. 7 indexed citations
15.
Benecky, Michael J., Carl G. Kolvenbach, David L. Amrani, & Michael W. Mosesson. (1988). Evidence that binding to the carboxyl-terminal heparin-binding domain (Hep II) dominates the interaction between plasma fibronectin and heparin. Biochemistry. 27(19). 7565–7571. 39 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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