David Bienvenue
About
David Bienvenue is a scholar working on Oncology, Molecular Biology and Radiology, Nuclear Medicine and Imaging.
According to data from OpenAlex, David Bienvenue has authored 23 papers receiving a total of 406 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Oncology, 11 papers in Molecular Biology and 7 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in David Bienvenue's work include Peptidase Inhibition and Analysis (10 papers), Monoclonal and Polyclonal Antibodies Research (7 papers) and CAR-T cell therapy research (5 papers). David Bienvenue is often cited by papers focused on Peptidase Inhibition and Analysis (10 papers), Monoclonal and Polyclonal Antibodies Research (7 papers) and CAR-T cell therapy research (5 papers). David Bienvenue collaborates with scholars based in United States and Poland. David Bienvenue's co-authors include Richard C. Holz, Brian Bennett, Dagmar Ringe, Gregory A. Petsko, K.P. Bzymek, William Desmarais, A. Joachimiak, B. Nocek, Robert E. Miller and Jane A. Gross and has published in prestigious journals such as Journal of the American Chemical Society, SHILAP Revista de lepidopterología and The Journal of Immunology.
In The Last Decade
David Bienvenue
23 papers receiving 388 citations
Peers
David Bienvenue
Elisabeth O. Hochleitner Germany
Daniel McMullan United States
Annika Groß Germany
Selvambigai Manivannan United Kingdom
Marco Cavaco Portugal
Charuta C. Palsuledesai United States
Séverine Wack France
Ksenia Matlawska‐Wasowska United States
Patrick Gizzi France
Citations per year, relative to David Bienvenue David Bienvenue (= 1×)
peers
Elisabeth O. Hochleitner
Countries citing papers authored by David Bienvenue
Since
Specialization
Citations
This map shows the geographic impact of David Bienvenue'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 David Bienvenue with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites David Bienvenue more than expected).
Fields of papers citing papers by David Bienvenue
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by David Bienvenue. 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 David Bienvenue. The network helps show where David Bienvenue may publish in the future.
Co-authorship network of co-authors of David Bienvenue
This figure shows the co-authorship network connecting the top 25 collaborators of David Bienvenue. A scholar is included among the top collaborators of David Bienvenue 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 David Bienvenue. David Bienvenue is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Killebrew, Justin R, Shannon Okada, Lynn M. Amon, et al.. (2024). Abstract 4062: A novel method for generating regulated cytokine therapeutics: Safety and activity of a conditionally active cLAG3-IL2 capable of delivering IL2 to LAG3+ cells while remaining inert on LAG3- cells. Cancer Research. 84(6_Supplement). 4062–4062.
2.
Nelson, Michelle H., Robert E. Miller, Anneli Nilsson, et al.. (2020). 851 Potent tumor-directed T cell activation and in vivo tumor inhibition induced by a 4–1BB x 5T4 ADAPTIR™ bispecific antibody. SHILAP Revista de lepidopterología. A507.1–A507.
3.
Comeau, Michael R., Rebecca Gottschalk, Lynda Misher, et al.. (2019). Abstract LB-199: APVO436, a bispecific anti-CD123 x anti-CD3 ADAPTIR™ molecule for redirected T-cell cytotoxicity with limited cytokine release, is well tolerated in repeat dose toxicology studies in cynomolgus macaques. Cancer Research. 79(13_Supplement). LB–199.
4.
Comeau, Michael R., Robert E. Miller, Rebecca Gottschalk, et al.. (2018). Abstract B111: Characterization of APVO436, a bispecific anti-CD123 x anti-CD3 ADAPTIR™ molecule for redirected T-cell cytotoxicity, in preclinical models of AML and nonhuman primates. Molecular Cancer Therapeutics. 17(1_Supplement). B111–B111.
5.
Misher, Lynda, David Bienvenue, Sara Fritzell, et al.. (2018). Activation of the CD137 Pathway in T cells by a CD137 × 5T4 bispecific ADAPTIR Molecule Requires Co-engagement of CD137 and 5T4. The Journal of Immunology. 200(Supplement_1). 58.21–58.21.
6.
Comeau, Michael R., Robert E. Miller, Rebecca Gottschalk, et al.. (2018). Abstract 1786: APVO436, a bispecific anti-CD123 x anti-CD3 ADAPTIR™ molecule for redirected T-cell cytotoxicity, induces potent T-cell activation, proliferation and cytotoxicity with limited cytokine release. Cancer Research. 78(13_Supplement). 1786–1786.
7.
Hernández‐Hoyos, Gabriela, Maria Dasovich, Hang Fang, et al.. (2016). MOR209/ES414, a Novel Bispecific Antibody Targeting PSMA for the Treatment of Metastatic Castration-Resistant Prostate Cancer. Molecular Cancer Therapeutics. 15(9). 2155–2165.
8.
Blankenship, John W., Lynda Misher, Nicole Zhang, et al.. (2016). Abstract 4995: anti-ROR1 x anti-CD3 ADAPTIR™ molecule, ES425, redirects T-cell cytotoxicity and inhibits tumor growth in preclinical models of triple-negative breast cancer. Cancer Research. 76(14_Supplement). 4995–4995.
9.
Scalley‐Kim, Michelle, Bruce W. Hess, Ryan L. Kelly, et al.. (2012). A Novel Highly Potent Therapeutic Antibody Neutralizes Multiple Human Chemokines and Mimics Viral Immune Modulation. PLoS ONE. 7(8). e43332–e43332.
10.
Bienvenue, David, et al.. (2012). ProteinTracker: an application for managing protein production and purification. BMC Research Notes. 5(1). 224–224.
11.
Gillner, Danuta, David Bienvenue, B. Nocek, et al.. (2008). The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues. JBIC Journal of Biological Inorganic Chemistry. 14(1). 1–10.
12.
Desmarais, William, David Bienvenue, K.P. Bzymek, et al.. (2006). The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. JBIC Journal of Biological Inorganic Chemistry. 11(4). 398–408.
13.
Bienvenue, David, et al.. (2006). Kinetic and spectroscopic characterization of the E134A- and E134D-altered dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae. JBIC Journal of Biological Inorganic Chemistry. 11(2). 206–216.
14.
Bienvenue, David, et al.. (2004). Spectroscopic and X-ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase from Aeromonas (Vibrio) proteolytica,. Biochemistry. 43(30). 9620–9628.
15.
Bienvenue, David, et al.. (2003). Substrate Specificity, Metal Binding Properties, and Spectroscopic Characterization of the DapE-Encoded N-Succinyl-l ,l -Diaminopimelic Acid Desuccinylase from Haemophilus influenzae. Biochemistry. 42(36). 10756–10763.
16.
Desmarais, William, David Bienvenue, K.P. Bzymek, et al.. (2002). The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris. Structure. 10(8). 1063–1072.
17.
Bienvenue, David, et al.. (2002). Hydrolysis of Thionopeptides by the Aminopeptidase from Aeromonas proteolytica: Insight into Substrate Binding. Biochemistry. 41(11). 3712–3719.
18.
Bienvenue, David, Rebecca Mathew, Dagmar Ringe, & Richard C. Holz. (2001). The aminopeptidase from Aeromonas proteolytica can function as an esterase. JBIC Journal of Biological Inorganic Chemistry. 7(1-2). 129–135.
19.
Bienvenue, David, Brian Bennett, & Richard C. Holz. (2000). Inhibition of the aminopeptidase from Aeromonas proteolytica by l-leucinethiol: kinetic and spectroscopic characterization of a slow, tight-binding inhibitor–enzyme complex. Journal of Inorganic Biochemistry. 78(1). 43–54.
20.
Bienvenue, David, et al.. (1999). Slow-Binding Inhibition of the Aminopeptidase from Aeromonas proteolytica by Peptide Thiols: Synthesis and Spectroscopic Characterization. Biochemistry. 38(47). 15587–15596.
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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