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In Memoriam: In Remembrance of Cancer Researchers who passed in 2026

Posted in Cancer Prevention: Research & Programs, Drug Discovery Chemistry, Gene Regulation, Li-fraumeni syndrome., Mourning the Loss of a Scientific Leader, Patents, TP53 - Germline mutations, tagged AACR, breast cancer, cancer risk, Li-fraumeni syndrome., novartis, nuclear receptors, Purdue University, retinol binding protein, steroid receptor, TP53 on July 13, 2026| Leave a Comment »

In Memoriam: In Remembrance of Cancer Researchers who passed in 2026

Reporter: Stephen J. Williams, Ph.D.

Source: https://www.aacr.org/professionals/membership/in-memoriam/

The following remembrances of American Association of Cancer Research (AACR) prominent member who have recently passed in 2026 is given below.  Each have contributed seminal research and discovery in the field of cancer biology and cancer risk.  In many cases, their discoveries transformed the way  we understand and treat cancer.  A separate In Memoriam for Nobel Leaureatte Dr. J. Michael Bishop will be given in a separate post.

Joseph F. Fraumeni, Jr., MD, FAACR (04/01/1933 – 06/22/2026)

Joseph F. Fraumeni, Jr., MD, FAACR, a renowned cancer epidemiologist, a Fellow of the AACR Academy, and a former member of the AACR Board of Directors, died June 22, 2026, at the age of 93. A career researcher and leader at the National Cancer Institute, Fraumeni was a co-discoverer of the genetic condition now known as the Li-Fraumeni syndrome and launched the U.S. Atlas of Cancer Mortality, which mapped geographic variations in cancer.Born April 1, 1933, in Boston, Fraumeni earned a bachelor’s degree from Harvard College, a medical degree from Duke University School of Medicine, and a master of science in epidemiology from the Harvard University School of Public Health. He completed medical residencies at Johns Hopkins Hospital and the Memorial Sloan-Kettering Cancer Center. A member of the AACR since 1968, Fraumeni served on the AACR’s Board of Directors from 1983 to 1986. He also served the AACR as an assistant editor, senior editor, and editorial board member for Cancer Epidemiology, Biomarkers & Prevention and an assistant editor for Cancer Research. The AACR recognized him with the AACR-American Cancer Society Award for Research Excellence in Epidemiology and Prevention in 1993 and the AACR Award for Lifetime Achievement in Cancer Research in 2009. He was inducted as a member of the inaugural class of Fellows of the AACR Academy in 2013. Fraumeni was a fellow of the American College of Physicians, the American Association for the Advancement of Science, and the American Academy of Arts and Sciences, and a member of the Institute of Medicine, the Association of American Physicians, and the National Academy of Sciences.

In 1962, Fraumeni joined the Epidemiology Branch of the National Cancer Institute (NCI) as a commissioned officer in the U.S. Public Health Service (USPHS). He went on to hold several leadership positions at the NCI, including posts as head of the Ecology Studies Section, chief of the Environmental Epidemiology Branch, director of the Epidemiology and Biostatistics Program, and founding director of the Division of Cancer Epidemiology and GeneticsHe retired from the USPHS in 1999 with the rank of rear admiral and assistant surgeon general. When he retired from NCI in 2017, he was named Scientist Emeritus. He authored or co-authored more than 900 scientific publications.

His research focused the epidemiology of high cancer risk populations and, in 1969, led him to discover a familial syndrome of early-onset cancers of the breast, brain, and other malignancies known as Li-Fraumeni Syndrome.  Li-Fraumeni Sydrome is characterized by inherited mutations in the p53 tumor suppressor gene.

Li-Fraumeni Syndrome

from Cleveland Clinic: Li-Fraumeni syndrome is a rare genetic disorder that increases the risk you and your family members will develop cancer. Everyone with this condition has a 90% chance of developing one or more types of cancer by age 60. About half develop cancer before they turn 40. Females with Li-Fraumeni syndrome almost always develop breast cancer.

Below is the original reference published with his colleague the late Dr, Federick Li.  Thier work together over the years helped develop the discovery of cancer susceptiblitiy genes and the importance of mutations of these genes linked to increased risk of developing cancer.

Li FP, Fraumeni JF Jr. 1969. Soft-tissue sarcomas, breast cancer, and other neoplasms. A familial syndrome? Ann Intern Med 71: 747–752.

Four families were identified in which a pair of children had soft-tissue sarcomas: three sets of sibs and one set of cousins. One parent of each affected child developed cancer; carcinoma of the breast occurred in three mothers under 30 years of age. Other young adults in these families had a high frequency of cancer, with no evidence of underlying genetic disorders known to carry a high risk of neoplasia. The increased familial susceptibility to cancer was manifested not only by the large number of members affected but by a seeming excess of multiple primary neoplasms.

It wasn’t until the 1990’s that Malkin et al. that germline mutations in TP53 were associated with this disease

Malkin D, Li FP, Strong LC, Fraumeni JF Jr, Nelson CE, Kim DH, Kassel J, Gryka MA, Bischoff FZ, Tainsky MA, et al. 1990. Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasms. Science 250: 1233–1238.

A similar syndrome named Lynch syndrome also  gave rise to early increased risk of multiple cancers but due to germline mutations in mismatch repair genes like MLH1, MSH2, MSH6, or PMS2.

Lynch HT, Mulcahy GM, Harris RE, Guirgis HA, Lynch JF. 1978. Genetic and pathologic findings in a kindred with hereditary sarcoma, breast cancer, brain tumors, leukemia, lung, laryngeal, and adrenal cortical carcinoma. Cancer 41: 2055–2064.

 

Pierre Chambon, MD, FAACR, (02/07/1931 – 05/05/2026)

Pierre Chambon, MD, FAACR, a Fellow of the AACR Academy who was a pioneer in the structure and expression of genes, died May 5, 2026, at the age of 95. Chambon’s early work contributed to the discovery of PolyADPribose, the discovery of multiple RNA polymerases, major contributions to the elucidation of chromatin structure, and the discovery of animal split genes. Later work included the discovery of multiple promoter elements and their cognate factors. His research on nuclear receptors has had a marked influence on the understanding of signal transduction and endocrinology in vertebrates.

Born February 7, 1931, in Mulhouse, France, Chambon received his medical degree from the University of Strasbourg in 1958. He joined the university as a research associate, becoming an associate professor in 1962 and professor of biochemistry in 1968. He founded the Institute for Genetics and Cellular and Molecular Biology in 1994 and served as its director until 2002. He then founded the Mouse Clinical Institute and served as director until 2006. He held the chair of molecular genetics at the Collège de France from 1993 to 2003 and served as chair of molecular genetics and biology at the University of Strasbourg Institute for Advanced Study from 2012 to 2021. Chambon was elected to the French Academy of Sciences in1985, the same year in which he was elected a foreign member of both the U.S. National Academy of Sciences and the American Academy of Arts and Sciences.

Juliet M. Daniel, PhD

Juliet M. Daniel, PhD, a cell biologist who was a distinguished university professor at McMaster University in Hamilton, Ontario, and member of AACR since 2002, died April 28, 2026. She was 61 years of age. Noted for her work on genetic risk factors for breast cancer, Daniel discovered and gave the name “Kaiso” to a gene associated with triple negative breast cancer in women of African descent. Born in Barbados in 1964, Daniel obtained a bachelor’s degree in life sciences from Queen’s University in Kingston, Ontario, in 1987 and a doctorate in microbiology from University of British Columbia in Vancouver in 1993. She conducted postdoctoral research at St. Jude Children’s Research Hospital in Memphis and Vanderbilt University in Nashville. She joined McMaster as an assistant professor in 1999, the first black woman to become a member of the Faculty of Science. She was promoted to associate professor in 2005 and professor in 2012. Daniel was appointed associate dean of research and external relations for the Faculty of Science on an acting basis in 2020 and permanently in 2021. She was named strategic advisor to the university president for the Canada-Caribbean Institute (CCI) at McMaster in 2024. She was named a distinguished university professor, the highest faculty honor, in 2025. Among many other honors, she was elected a fellow of the Canadian Academy of Health Sciences in 2025, received the inaugural Canadian Cancer Society Inclusive Excellence Prize in Cancer Research in 2020, and was awarded an honorary doctorate in science by the University of the West Indies in 2021.

Philip S. Low, PhD

Philip S. Low, PhD, the Ralph C. Corley distinguished professor of chemistry at Purdue University, an inventor and entrepreneur with more than 100 patents to his credit, and an emeritus member of AACR, died March 4, 2026, at the age of 78. He also served as Purdue’s Presidential Scholar for Drug Discovery and was for a time as director of the university’s Center for Drug Discovery. Low held more than 100 U.S.-issued patents through Purdue Innovates and is listed on 600 U.S. and international patents and 145 invention disclosures. He founded seven companies based on based on work conducted at Purdue, one of which, Endocyte Inc., was sold to Novartis in 2018. Born in Ames, Iowa, in 1947, Low earned a bachelor’s degree in chemistry from Brigham Young University in 1971 and a doctorate in biochemistry from the University of California, San Diego, in 1975. He joined the Purdue University faculty in 1976. An AACR member since 2005, Low received the AACR Award for Outstanding Achievement in Chemistry in Cancer Research in 2015 in recognition of his research on low molecular weight ligand-targeted therapeutic and imaging agents. In the same year, he also received the American Chemical Society (ACS) George & Christine Sosnovsky Award for Cancer Research and was elected to the National Academy of Inventors. In August 2025, Low was named the recipient of the ACS Alfred Burger Award in Medicinal Chemistry for 2026. He also received the Order of the Griffin and the Morrill Award from Purdue.

For more remebrances of past AACR members please visit: https://www.aacr.org/professionals/membership/in-memoriam/

Other recent In Memoriam on this Open Access Scientific Journal Include:

News from AACR; In Memoriam: Nobel Leaureate David Baltimore, Ph.D

In Memoriam: Professor Yitzhak Apeloig, President and Distinguised Professor of the Technion

 

 

 

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Accelerating PROTAC drug discovery: Establishing a relationship between ubiquitination and target protein degradation

Posted in Apoptosis, Bio Instrumentation in Experimental Life Sciences Research, Biological Networks, Biomedical Measurement Science, Cancer - General, Cancer and Current Therapeutics, CANCER BIOLOGY & Innovations in Cancer Therapy, Cell Biology, Signaling & Cell Circuits, Childhood cancer, Enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP), KRAS Mutation, Li-fraumeni syndrome., Proteosome, TP53 - Germline mutations, Ubiquitin, tagged breast cancer, Cancer - General, E3 Ligase, high throughput, MDM2, PROTAC, TUBEs, Ubiquitin ligase, ubiquitin-proteosome, VHL on October 4, 2022| Leave a Comment »

Accelerating PROTAC drug discovery: Establishing a relationship between ubiquitination and target protein degradation

Curator: Stephen J. Williams, Ph.D.

PROTACs have been explored in multiple disease fields with focus on only few ligases like cereblon (CRBN), Von Hippel-Lindau (VHL), IAP and MDM2. Cancer targets like androgen receptor, estrogen receptor, BTK, BCL2, CDK8 and c-MET [[6], [7], [8], [9], [10], [11]] have been successfully targeted using PROTACs. A variety of BET family (BRD2, BRD3, and BRD4)- PROTACs were designed using multiple ligases; MDM2-based BRD4 PROTAC [12], CRBN based dBET1 [13] and BETd-24-6 [14] for triple-negative breast cancer, enhanced membrane permeable dBET6 [15], and dBET57 PROTAC [16]. PROTACs for Hepatitis c virus (HCV) protease, IRAK4 and Tau [[17], [18], [19]] have been explored for viral, immune and neurodegenerative diseases, respectively. Currently, the PROTAC field expansion to vast undruggable proteome is hindered due to narrow focus on select E3 ligases. Lack of reliable tools to rapidly evaluate PROTACs based on new ligases is hindering the progress. Screening platforms designed must be physiologically relevant and represent true PROTAC cellular function, i.e., PROTAC-mediated target ubiquitination and degradation.

In the current study, we employ TUBEs as affinity capture reagents to monitor PROTAC-induced poly-ubiquitination and degradation as a measure of potency. We established and validated proof-of-concept cell-based assays in a 96-well format using PROTACS for three therapeutic targets BET family proteins, kinases, and KRAS. To our knowledge, the proposed PROTAC assays are first of its kind that can simultaneously 1) detect ubiquitination of endogenous, native protein targets, 2) evaluate the potency of PROTACs, and 3) establish a link between the UPS and protein degradation. Using these TUBE assays, we established rank order potencies between four BET family PROTACs dBET1, dBET6, BETd246 and dBET57 based on peak ubiquitination signals (“Ub_Max”) of the target protein. TUBE assay was successful in demonstrating promiscuous kinase PROTACs efficiency to degrade Aurora Kinase A at sub-nanomolar concentrations within 1 h. A comparative study to identify changes in the ubiquitination and degradation profile of KRAS G12C PROTACs recruiting two E3 ligases (CRBN and VHL). All of the ubiquitination and degradation profiles obtained from TUBE based assays correlate well with traditional low throughput immunoblotting. Significant correlation between DC₅₀ obtained from protein degradation in western blotting and Ub_Max values demonstrates our proposed assays can aid in high-throughput screening and drastically eliminate artifacts to overcome bottlenecks in PROTAC drug discovery.

To successfully set up HTS screening with novel PROTACs without pre-existing knowledge, we recommend the following steps. 1. Identify a model PROTAC that can potentially demonstrate activity based on knowledge in PROTAC design or in vitro binding studies. 2. Perform a time course study with 2–3 doses of the model PROTAC based on affinities of the ligands selected. 3. Monitor ubiquitination and degradation profiles using plate-based assay and identify time point that demonstrates Ub_Max. 4. Perform a dose response at selected time point with a library of PROTACs to establish rank order potency.

INTRODUCTION

Ubiquitination is a major regulatory mechanism to maintain cellular protein homeostasis by marking proteins for proteasomal-mediated degradation [1]. Given ubiquitin’s role in a variety of pathologies, the idea of targeting the Ubiquitin Proteasome System (UPS) is at the forefront of drug discovery [2]. “Event-driven” protein degradation using the cell’s own UPS is a promising technology for addressing the “undruggable” proteome [3]. Targeted protein degradation (TPD) has emerged as a new paradigm and promising therapeutic option to selectively attack previously intractable drug targets using PROteolytic TArgeting Chimeras (PROTACs) [4]. PROTACs are heterobifunctional molecules with a distinct ligand that targets a specific E3 ligase which is tethered to another ligand specific for the target protein using an optimized chemical linker. A functional PROTAC induces a ternary E3-PROTAC-target complex, resulting in poly-ubiquitination and subsequent controlled protein degradation [5]. Ability to function at sub-stoichiometric levels for efficient degradation, a significant advantage over traditional small molecules.

PROTACs have been explored in multiple disease fields with focus on only few ligases like cereblon (CRBN), Von Hippel-Lindau (VHL), IAP and MDM2. Cancer targets like androgen receptor, estrogen receptor, BTK, BCL2, CDK8 and c-MET [[6], [7], [8], [9], [10], [11]] have been successfully targeted using PROTACs. A variety of BET family (BRD2, BRD3, and BRD4)- PROTACs were designed using multiple ligases; MDM2-based BRD4 PROTAC [12], CRBN based dBET1 [13] and BETd-24-6 [14] for triple-negative breast cancer, enhanced membrane permeable dBET6 [15], and dBET57 PROTAC [16]. PROTACs for Hepatitis c virus (HCV) protease, IRAK4 and Tau [[17], [18], [19]] have been explored for viral, immune and neurodegenerative diseases, respectively. Currently, the PROTAC field expansion to vast undruggable proteome is hindered due to narrow focus on select E3 ligases. Lack of reliable tools to rapidly evaluate PROTACs based on new ligases is hindering the progress. Screening platforms designed must be physiologically relevant and represent true PROTAC cellular function, i.e., PROTAC-mediated target ubiquitination and degradation.

Cellular PROTAC screening is traditionally performed using cell lines harboring reporter genes and/or Western blotting. While Western blotting is easy to perform, they are low throughput, semi-quantitative and lack sensitivity. While reporter gene assays address some of the issues, they are challenged by reporter tags having internal lysines leading to artifacts. Currently, no approaches are available that can identify true PROTAC effects such as target ubiquitination and proteasome-mediated degradation simultaneously. High affinity ubiquitin capture reagents like TUBEs [20] (tandem ubiquitin binding entities), are engineered ubiquitin binding domains (UBDs) that allow for detection of ultralow levels of polyubiquitinated proteins under native conditions with affinities as low as 1 nM. The versatility and selectivity of TUBEs makes them superior to antibodies, and they also offer chain-selectivity (-K48, -K63, or linear) [21]. High throughput assays that can report the efficacy of multiple PROTACs simultaneously by monitoring PROTAC mediated ubiquitination can help establish rank order potency and guide chemists in developing meaningful structure activity relationships (SAR) rapidly.

In the current study, we employ TUBEs as affinity capture reagents to monitor PROTAC-induced poly-ubiquitination and degradation as a measure of potency. We established and validated proof-of-concept cell-based assays in a 96-well format using PROTACS for three therapeutic targets BET family proteins, kinases, and KRAS. To our knowledge, the proposed PROTAC assays are first of its kind that can simultaneously 1) detect ubiquitination of endogenous, native protein targets, 2) evaluate the potency of PROTACs, and 3) establish a link between the UPS and protein degradation. Using these TUBE assays, we established rank order potencies between four BET family PROTACs dBET1, dBET6, BETd246 and dBET57 based on peak ubiquitination signals (“Ub_Max”) of the target protein. TUBE assay was successful in demonstrating promiscuous kinase PROTACs efficiency to degrade Aurora Kinase A at sub-nanomolar concentrations within 1 h. A comparative study to identify changes in the ubiquitination and degradation profile of KRAS G12C PROTACs recruiting two E3 ligases (CRBN and VHL). All of the ubiquitination and degradation profiles obtained from TUBE based assays correlate well with traditional low throughput immunoblotting. Significant correlation between DC₅₀ obtained from protein degradation in western blotting and Ub_Max values demonstrates our proposed assays can aid in high-throughput screening and drastically eliminate artifacts to overcome bottlenecks in PROTAC drug discovery.

 

 

 

 

 

 

 

 

 

SOURCE

https://www.sciencedirect.com/science/article/abs/pii/S0006291X22011792

Other articles of PROTACs in this Open Access Journal Include

The Vibrant Philly Biotech Scene: Proteovant Therapeutics Using Artificial Intelligence and Machine Learning to Develop PROTACs

The Map of human proteins drawn by artificial intelligence and PROTAC (proteolysis targeting chimeras) Technology for Drug Discovery

Live Conference Coverage AACR 2020 in Real Time: Monday June 22, 2020 Late Day Sessions

From High-Throughput Assay to Systems Biology: New Tools for Drug Discovery

 

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