IN MEMORIAM
https://doi.org/10.1083/jcb.201803048
1
J. Cell Biol. 2018
Rockefeller University Press
Günter Blobel was a scientific colossus who dedicated his career to understanding the mechanisms for protein sorting to
membrane organelles. His monumental contributions established research paradigms for major arenas of molecular cell
biology. For this work, he received many accolades, including the Nobel Prize in Medicine or Physiology in 1999. He was a
scientist of extreme passion and a nurturing mentor for generations of researchers, imbuing them with his deep love of cell
biology and galvanizing them to continue his scientific legacy. Günter passed away on February 18, 2018, at the age of 81.
Rockefeller University Press
Günter was a
Lebenskünstler—a master of the art of living. He
had a tremendous presence; when he walked into a room, he
couldn’t help but command attention. A towering man, with a
flock of white hair and a jovial nature, he loved to tell stories: of
experiences in the laboratory, of life in New York, and of his time
growing up in Germany. Günter was born in 1936, as the son of
a veterinarian. He considered his early childhood to be idyllic,
raised with his seven siblings in a rural and remote part of Silesia,
then in the eastern part of Germany. There, largely isolated from
the horrific developments overtaking Europe, Günter recalled
long afternoons in beautiful manor houses adorned with hunting
trophies, winter days of sleighing, and summer days in horse-
drawn carriages. However, this life was shattered during the final
months of the Second World War, when he and his family were
forced to flee the advancing Soviet army. Passing through Dres-
den at this chaotic time, Günter experienced two life-changing
events: seeing for the first time the magnificent baroque splen-
dor of this “great jewel of a city,” and days later, witnessing its
leveling by Allied firebombing. The family picked up the threads
of their former lives in Freiberg, a medieval town located to the
west of Dresden. Again, Günter has fond recollections of his time
there. He immersed himself in the town’s rich cultural legacy,
centered around baroque and classical music performances in its
Gothic cathedral. Unfortunately, the new communist regime of
East Germany was inhospitable to the Blobel family, who were
seen as part of the bourgeois class and were therefore denied
access to higher education. Forced to leave Freiberg by these
circumstances, Günter moved to Tübingen in West Germany to
study medicine. Though he completed an MD degree, he was not
inspired to become a practicing physician. Instead, he decided to
try a career in research science.
Accordingly, Günter joined the laboratory of Van Potter at the
University of Wisconsin to obtain a PhD. As a graduate student, he
developed an interest in cell structure and function, and became
engaged with a problem that subsequently became an obsession:
how the cell sorts secretory proteins to the rough ER. To pursue
these interests, he moved to the laboratory of George Palade at
the Rockefeller University for postdoctoral studies. Günter’s time
with Palade was a critical and formative experience, as the Palade
laboratory was an intellectual epicenter for study of the ER. Pal-
ade and coworkers had described the secretory pathway during
the 1960s in an exquisite series of studies that combined cell
fractionation, biochemistry, and electron microscopy. Indeed,
this and related work on the functions of membrane organelles
earned Palade, Christian De Duve, and Albert Claude the Nobel
Günter Blobel: Pioneer of molecular cell biology
(1936–2018)
Blobel Laboratory Trainees
© 2018 Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months
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). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike
4.0 International license, as described at
https:// creativecommons .org/ licenses/ by -nc -sa/ 4 .0/
).
Correspondence to John D. Aitchison:
jaitchison@ systemsbiology .org
; Larry Gerace:
lgerace@ scripps .edu
; Michael P. Rout:
rout@ rockefeller .edu
.
Günter Blobel.
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Günter Blobel: 1936–2018
Journal of Cell Biology
https://doi.org/10.1083/jcb.201803048
2
Prize in Medicine or Physiology in 1974. Günter revered Palade,
and used his mentor’s work and conceptualization of cell func-
tion as a touchstone throughout his career.
As a newly promoted faculty member at the Rockefeller Uni-
versity, Günter set out to address the question of how mRNAs that
encode secretory proteins are selected for synthesis on the rough
ER. Despite a lack of experimental evidence, in 1971, Günter and
David Sabatini proposed an amazingly prescient hypothesis (
1
).
They suggested that ER targeting of secretory proteins is spec-
ified by the presence of a signal peptide on the N terminus of
proteins destined to be translocated into the ER. This concept was
subsequently termed the “signal hypothesis” (
2
). ‘‘At first it was
just a wonderful idea,” Günter remembered; “It was quite a bold
thing to say because nothing hinted at a signal sequence. But it
was by far the best thing we could come up with.”
Inspired by his work with Palade, Günter knew that only a
complete in vitro reconstitution of the ER translocation process
with purified components—a Herculean challenge at the time—
could validate this hypothesis. Encouraged by studies from sev-
eral laboratories suggesting that the IgG light chain might be
synthesized as a precursor polypeptide larger than the secreted
form (1972–1975), he worked intensively to develop methods to
biochemically dissect the process of ER secretory protein trans-
location. He provided the first strong experimental support for
the signal hypothesis in two landmark papers in 1975 (
2
,
3
). As
with many of his most remarkable discoveries, these were pub-
lished in the
Journal of Cell Biology. By analyzing IgG light chain
synthesis using in vitro assays with isolated ER membranes, he
obtained striking evidence for the presence of an N-terminal sig-
nal sequence on the nascent chains that was involved in cotrans-
lational translocation across the ER membrane, and that was
cotranslationally removed (
Fig. 1
). He predicted that the signal
sequence communicated with specific receptor proteins to medi-
ate ER attachment of ribosomes and induce transient assembly
of a proteinaceous channel to conduct the nascent polypeptide
across the ER membrane. He also proposed that the mechanisms
and components involved in secretory protein translocation
could be used for the insertion of membrane proteins into the
ER. These ideas were controversial, particularly the notion that
a proteinaceous channel was involved in signal sequence–medi-
ated membrane translocation, and became the focus of heated
scientific debates for the subsequent two decades. But, as was
typical of Günter’s outlook on science, he was unfazed: “I thought
my ideas were reasonable. So why not propose them?”
Indeed, the controversies surrounding the signal hypothesis
were laid to rest, one by one, by a series of elegant papers from the
Blobel laboratory and from others over the next two decades. This
work identified a cytosolic ribonucleoprotein particle (termed
the SRP) that interacts with the signal sequence, a specific SRP
receptor in the ER membrane involved in ribosome targeting, a
signal peptidase that cotranslationally removes the signal pep-
tide, and, finally, the proteinaceous channel (Sec61 complex) that
mediates movement of the nascent chain across the membrane
(
4
). The evolutionary significance of signal-mediated protein
translocation across the ER was resoundingly underscored by
the identification of conserved systems in diverse organisms
including yeast and bacteria. The experimental approach used by
Günter and associates for these studies, involving the use of an in
vitro assay with a quantitative functional output for mechanistic
analysis by fractionation and reconstitution, helped usher in the
era of modern molecular cell biology.
With the first experimental evidence for the signal hypothesis
in hand, Günter prophetically speculated that systems analogous
to those for ER translocation also might be deployed for targeting
proteins to other membrane organelles (
2
). These speculations
were decisively borne out in subsequent studies on protein trans-
port into the mitochondrion, the chloroplast, the peroxisome,
and the nucleus (
Fig. 2
), providing the ultimate vindication for
these bold conjectures. This was a major element of Günter’s
principle of “protein topogenesis”: that information for sorting
Figure 1. The original signal hypothesis
(adapted from reference
2
). (A) Illustration of
the essential features of the signal hypothesis for
the transfer of proteins across membranes. Sig-
nal codons after the initiation codon AUG are indi-
cated by a zigzag region in the mRNA. The signal
sequence region of the nascent chain is indicated
by a dashed line. Endoproteolytic removal of the
signal sequence is indicated by the presence of
signal peptides (indicated by short dashed lines).
(B) Model for the formation of a transient pro-
teinaceous tunnel in the membrane through
which the nascent chain is transferred.
Günter Blobel: 1936–2018
Journal of Cell Biology
https://doi.org/10.1083/jcb.201803048
3
of proteins to different membrane compartments, as well as for
integration into membranes, is encoded in discrete classes of
“topogenic” sequences recognized by various receptor systems,
membrane-spanning protein conduits, and other effectors (
5
).
Propelled by his polymathic character, Günter brought his
enthusiasm and brilliance to bear on several other areas, particu-
larly nucleocytoplasmic transport and the nuclear lamina. In the
mid-1970s, Günter and coworkers made the remarkable discov-
ery that nuclear pore complexes (NPCs) remain as intact struc-
tures after detergent extraction of nuclear envelopes, attached to
a proteinaceous “nuclear lamina” derived from the inner surface
of the nuclear envelope (
Fig. 3, A and B
;
6
,
7
). These results sug-
gested that NPCs could be isolated and biochemically analyzed,
a goal that was realized many years later by trainees from his
laboratory. Günter enthusiastically promoted the view that the
nuclear lamina is a widespread nuclear structural component of
fundamental importance, albeit not evident in most cells by elec-
tron microscopy. These results initiated a stream of biochemical
and functional studies that gradually became an experimental
torrent involving numerous laboratories. This effort has firmly
established the importance of the lamina in myriad nuclear
functions in higher eukaryotes, including nuclear mechanics,
signaling, and the dynamic 3D functional organization of chro-
matin. The relatively recent discoveries linking mutations in
nuclear lamina proteins to at least 15 human genetic disorders
speak to Günter’s visionary intuition on the importance of the
nuclear lamina.
In the arena of nucleocytoplasmic transport. Günter’s group
was a frontrunner in the identification of nuclear transport fac-
tor proteins and NPC components, his competitive fervor help-
ing to propel the field forward at an astounding rate during the
1990s. More recently, in keeping with his desire to understand
the mechanistic principles of cells and fascinated by the molec-
ular architecture of these players, he retailored his laboratory
to solve the atomic structures for some of the proteins compris-
ing these assemblies (
Fig. 3 C
). He drew great joy from solving
molecular structures, seeing in them an elegance akin to that
found in great architectural masterpieces, and he was adept in
Figure 3. The nuclear envelope, and associated structures. (A and B) Transmission electron micrographs of a thin section through an NPC–lamina frac-
tion isolated from rodent liver, showing NPCs in lateral (single arrow) and frontal (double arrow) views, and the associated nuclear lamina (lA). Bars, 100 nm
(adapted from reference
7
). (C) An example of one of the most recent structures from the Blobel laboratory (PDB:
5SUP
): the messenger ribonucleoprotein
particles remodeling complex of Sub2 associated with an ATP analogue, RNA, and a C-terminal fragment of Yra1, required to process and package messenger
ribonucleoprotein particles before export through the NPC.
Figure 2. The principles of protein targeting
directed by signal sequences. A schematic of
a cell is shown, with different membrane-bound
organelles illustrated and labeled. Newly synthe-
sized proteins carry signal sequences, often but
not always at one end of the protein, which can
direct that protein to the correct organelle within
the cell and allow them to cross the organellar
membranes. The lower right inset depicts how
additional classes of topogenic sequences (
5
)
can specify the membrane integration of proteins
(brown shading) instead of simple membrane
translocation with signal sequence cleavage
(orange shading).
Günter Blobel: 1936–2018
Journal of Cell Biology
https://doi.org/10.1083/jcb.201803048
4
interpreting them in the context of cellular functions. Often he
would retreat to his office for days, poring over stacks of litera-
ture and drawing on his experiences, to interpret their mecha-
nisms and dynamics, ultimately explaining them with flamboy-
ant imagery that reflected his love of cell biology.
Günter felt that doing science is a privilege and that it unifies
humanity. He espoused da Vinci’s belief that “the noblest plea-
sure is the joy of understanding.” His enthusiasm was infectious
and his laboratory was a hotbed of exciting ideas and around-
the-clock activity. Sometimes the exciting ideas did not survive
rigorous experimental scrutiny. But Günter was not afraid to
miss the mark. Those who knew him well also knew how passion-
ate he could become when a concept seemed particularly appeal-
ing. However, as he himself acknowledged, it sometimes became
clear that (paraphrasing Thomas Huxley) “there are beautiful
hypotheses killed by ugly facts.” He fully embraced this facet of
scientific research, further stating that “one must not be wed to
one’s fantasies.”
As trainees, it was a pleasure and privilege for us to be part of
his life and to have been influenced by this extraordinary man.
We started our careers on the fertile ground tilled by our time in
Günter’s laboratory. He inspired us to think big and to ask the
questions in biology that really mattered. Günter viewed his lab-
oratory as the greatest of master artists viewed their studios, just
as these studios apprenticed new artists while the paintings were
produced, Günter sought both to produce new scientific discov-
eries and to train new scientific researchers. Only last year, five
of Günter’s postdoctoral researchers and senior fellows gained
assistant professor tenure track positions. His office door was
always open to his trainees, past and present. They knew they
could go in, even if defeated and distraught after long strings of
failures, thrash through the issues, work with him on new ways
of tackling them, and emerge reinvigorated.
Günter’s passions extended beyond the scientific. The sim-
plest of things could ignite an exuberant outpouring. A walk
with his dogs through Central Park, the flowers in the garden at
the Rockefeller University, or an evening at his favorite haunt,
Barbetta Restaurant. This sentiment and joie de vivre belied
an intensely competitive spirit, but at heart Günter was a kind
gentleman who was enormously generous. Spurred by his child-
hood experiences, he became the founder and president of the
nonprofit organization Friends of Dresden. Indeed, he donated
his Nobel Prize money to Dresden, devoted to the rebuilding of
the Frauenkirche—a Lutheran church and baroque architectural
masterpiece—and the New Synagogue, to replace the synagogue
destroyed by the Nazis.
With deep sadness, we accept that eventually Günter grace-
fully succumbed to the self-described “noble injuries of time,”
maintaining his enthusiasm until the end. There is so much
more we could say about this incredibly inspiring man; we feel
we got to know him well (
Fig. 4
). But, as Günter himself often
liked to say, “less is more.” For his memorial, one can view the
architectural splendors in Dresden reborn through his efforts,
his towering masterpieces of scientific insight that underlie
countless medical therapies and treatments being pioneered
today, and the generations of researchers inspired by him who
are continuing his work and who are passing on his baton to the
next generations.
Figure 4. Blobel laboratory trainees were polled
for up to five one-word descriptors they have used
to describe Günter to their friends, family, and col-
leagues. Responses are shown in word cloud format
produced using software from WordArt.com. The size of
each word reflects its frequency of usage.
Günter Blobel: 1936–2018
Journal of Cell Biology
https://doi.org/10.1083/jcb.201803048
5
Submitted: 9 March 2018
Accepted: 9 March 2018
References
1. Blobel, G., and D.D. Sabatini. 1971. Ribosome-membrane interaction in
eukaryotic cells.
In Biomembranes. L.A. Manson, editor. Springer, Bos-
ton, MA. 193–195.
https:// doi .org/ 10 .1007/ 978 -1 -4684 -3330 -2 _16
2. Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes.
I. Presence of proteolytically processed and unprocessed nascent immu-
noglobulin light chains on membrane-bound ribosomes of murine
myeloma. J. Cell Biol. 67:835–851.
https:// doi .org/ 10 .1083/ jcb .67 .3 .835
3. Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes.
II. Reconstitution of functional rough microsomes from heterologous
components. J. Cell Biol. 67:852–862.
https:// doi .org/ 10 .1083/ jcb .67 .3 .852
4. Blobel, G. 2000. Protein targeting (Nobel lecture). ChemBioChem. 1:86–102.
https:// doi .org/ 10 .1002/ 1439 -7633(20000818)1: 2 %3C86:: AID -CBIC86
%3E3 .0 .CO;2 -A
5. Blobel, G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA.
77:1496–1500.
https:// doi .org/ 10 .1073/ pnas .77 .3 .1496
6. Aaronson, R.P., and G. Blobel. 1975. Isolation of nuclear pore complexes
in association with a lamina. Proc. Natl. Acad. Sci. USA. 72:1007–1011.
https:// doi .org/ 10 .1073/ pnas .72 .3 .1007
7. Dwyer, N., and G. Blobel. 1976. A modified procedure for the isolation of a
pore complex–lamina fraction from rat liver nuclei. J. Cell Biol. 70:581–
591.
https:// doi .org/ 10 .1083/ jcb .70 .3 .581
Blobel Laboratory Trainees contributing to this article : John D. Aitchison (Center for Infectious Disease Research): john.aitchison@cidresearch.org; Markus Albertini (Boehringer
Ingelheim Pharma GmbH & Co. KG): markus.albertini@gmx.de; David J. Anderson (California Institute of Technology): wuwei@caltech.edu; Bruce Aronow (Cincinnati Children’s
Hospital Research Foundation): bruce.aronow@cchmc.org; Roland Beckmann (Ludwig-Maximilians Universität München): beckmann@genzentrum.lmu.de; Manindra Bera (The
Rockefeller University): mbera@rockefeller.edu; Elisa Bergamin (Institute of Genetics and Molecular and Cellular Biology): bergamin.elisa@gmail.com; Doris Berman (Wake Forest
School of Medicine): dberman@wakehealth.edu; Miguel Berrios (State University of New York, Stony Brook): miguel.berrios@stonybrook.edu; Bartlomiej Blus (The Rockefeller
University): bblus@rockefeller.edu; Stefano Bonatti (University of Naples Federico II): bonatti@unina.it; Neris Bonifaci (Santen Italy Srl): neris.bonifaci@santen.com; Nica Borgese
(CNR Neuroscience Institute): n.borgese@in.cnr.it; Nilabh Chaudhary (Hopewell Global Health Initiative): nilabh.chaudhary@hopewellglobal.org; Radha Chauhan (National Centre for
Cell Science): radha.chauhan@nccs.res.in; Susana Chaves (University of Minho): suchaves@bio.uminho.pt; William J. Chirico (SUNY Downstate Medical Center): william.chirico@
downstate.edu; YuhMin Chook (University of Texas Southwestern): yuhmin.chook@utsouthwestern.edu; Greg Conner (University of Miami): gconner@miami.edu; Jean-Claude
Courvalin (Paris University): jccourvalin37@icloud.com; Elias Coutavas (The Rockefeller University): coutavas@mac.com; Erik Debler (Thomas Jefferson University): erik.debler@
jefferson.edu; Natalia Denisenko (Massachusetts Institute of Technology): ndenisen@mit.edu; Anne Devillers-Thiery (Pasteur Institute): anne.devill@laposte.net; Maryann Dickey
Fletcher: mdfletch217@gmail.com; Karima Djabali (Technical University of Munich): djabali@tum.de; Bernhard Dobberstein (ZMBH University Heidelberg): dobberstein@zmbh.
uni-heidelberg.de; Nancy Dwyer (LCCB, NIDDK, National Institutes of Health, retired): dwyer15@yahoo.com; Cordula Enenkel (University of Toronto): cordula.enenkel@utoronto.
ca; Jost Enninga (Institut Pasteur): jostenn@pasteur.fr; Ralf Erdmann (Ruhr-University Bochum): ralf.erdmann@rub.de; Ann Erickson (University of North Carolina at Chapel Hill):
annherickson@gmail.com; Jie Fan (Accutar Biotechnology): Jiefan@accutarbio.com; Irene (Fecycz) Bridger (Bennett Jones LLP): bridgeri@bennettjones.com; Adele Filson: adelefil@
gmail.com; Daniel Fisher (University of Massachusetts Medical School): daniel.fisher@umassmemorial.org; David Fisher (Massachusetts General Hospital): dfisher3@partners.
org; Robert P. Fisher (Icahn School of Medicine at Mount Sinai): robert.fisher@mssm.edu; Paul Fletcher (Brody School of Medicine, East Carolina University): fletcherpa@ecu.
edu; Monique Floer (Michigan State University): floer@msu.edu; Beatriz Fontoura (University of Texas Southwestern Medical Center): beatriz.fontoura@utsouthwestern.
edu; Martin Friedlander (The Scripps Research Institute): friedlan@scripps.edu; Larry Gerace (The Scripps Research Institute): lgerace@scripps.edu; Reid Gilmore (University of
Massachusetts Medical School): reid.gilmore@umassmed.edu; Linda Giudice (University of California, San Francisco): Linda.Giudice@ucsf.edu; Mara Gnädig (The Rockefeller
University): mgnadig@rockefeller.edu; Logan Gray: Logangray3.14@gmail.com; Gary Greenburg (Gordon and Betty Moore Foundation): gary.greenburg@Moore.org; Einar Hallberg
(Stockholm University): einar.hallberg@dbb.su.se; Qi Hao (Calico): hellohaoqi@gmail.com; Jürgen Helmers (Wayfair): juergen.helmers@gmail.com; Makoto Hijikata (Institute for
Frontier Life and Medical Sciences, Kyoto University): mhijikat@infront.kyoto-u.ac.jp; Andre Hoelz (California Institute of Technology): hoelz@caltech.edu; Egbert Hoiczyk (University
of Sheffield): e.hoiczyk@Sheffield.ac.uk; Kuo-Chiang Hsia (Academia Sinica): khsia@gate.sinica.edu.tw; John Hunt (Columbia University): jfh21@columbia.edu; Michael Hurwitz
(Yale Cancer Center): michael.hurwitz@yale.edu; Tita Isberto (The Rockefeller University): isbertt@rockefeller.edu; Erica Johnson (Thomas Jefferson University): erica.johnson@
jefferson.edu; Martin Kampmann (University of California, San Francisco): martin.kampmann@ucsf.edu; Jim Kaput (Vydiant Inc): jkaput@gmail.com; Elaine Katz: elainekatz@
college.harvard.edu; Felix Kessler (University of Neuchâtel): felix.kessler@unine.ch; Hyung Bum Kim (The Rockefeller University): hkim02@rockefeller.edu; Megan King (Yale
University): megan.king@yale.edu; Claudia Koch-Brandt (Gutenberg-University Mainz): koch@uni-Mainz.de; Junseock Koh (Seoul National University): junseockkoh@snu.
ac.kr; Doris Kraemer (University Hospital Oldenburg): kraemer.doris@klinikum-oldenburg.de; Aleksandra Krolak (The Rockefeller University): akrolak@rockefeller.edu; Xiaochun Li
(University of Texas Southwestern Medical Center): xiaochun.li@utsouthwestern.edu; Vishwanath R. Lingappa (Prosetta Biosciences, Inc): vlingappa@prosetta.com; Jairam Lingappa
(University of Washington): lingappa@uw.edu; Jaisri Lingappa (University of Washington): jais@uw.edu; Patrick Lusk (Yale University): patrick.lusk@yale.edu; Yingli Ma (Amgen
Inc.): yingli.ma@gmail.com; Michael J. Matunis (Johns Hopkins University): mmatuni1@jhu.edu; Mike McCune (University of California San Francisco): mike.mccune@ucsf.edu; Tom
Meier (Albert Einstein College of Medicine): tom.meier@einstein.yu.edu; Ivo Melcak (The Rockefeller University): melcaki@rockefeller.edu; Carl Mitchell (The Rockefeller University):
carl.abbate.mitchell@gmail.com; Mary Moore (Ross School of Medicine): mmoore@rossu.edu; Junona Moroianu (Boston College): moroianu@bc.edu; Matthias Muller (University of
Freiburg, Germany): matthias.mueller@biochemie.uni-freiburg.de; Vivien Nagy (German Center for Infection Research): vivien.nagy@dzif.de; Johanna Napetschnig (Regeneron
Pharmaceuticals): johanna.napetschnig@gmail.com; Ulf Nerhbass (Luxembourg Institute of Health): ulf.nehrbass@lih.lu; Chris Nicchitta (Duke University School of Medicine):
christopher.nicchitta@duke.edu; Sanjay K. Nigam (University of California San Diego): snigam@ucsd.edu; Gisele Nimic (The Rockefeller University): gmnimic@aol.com; Debkumar
Pain (New Jersey Medical School, Rutgers University): painde@njms.rutgers.edu; Lourdes R. Quirolgico (The Rockefeller University): quiroll@rockefeller.edu; Mahmudur Rahman
(Cornell University): mr558@cornell.edu; Yi Ren (Vanderbilt University): yi.ren@vanderbilt.edu; Michèle Roa (Institut Pasteur): michele.roa@pasteur.fr; Michael P. Rout (The
Rockefeller University): rout@rockefeller.edu; Daniel Schmidt (University of Minnesota): schmida@umn.edu; Danny Schnell (Michigan State University): schnelld@msu.
edu; Norbert Schuelke (Takeda Pharmaceuticals International Inc.): norbert.schuelke@takeda.com; Thomas Schwartz (Massachusetts Insitute of Technology): tus@mit.edu; Hyuk-
Soo Seo (Dana-Farber Cancer Institute): hux@crystal.harvard.edu; Alok Sharma (The Rockefeller University): asharma@rockefeller.edu; Greg Shelness (NIH Center for Scientific
Review): gshelness@gmail.com; Sandy Simon (The Rockefeller University): simon@rockefeller.edu; Nimisha Singh (The Rockefeller University): nsingh01@rockefeller.edu; Susan
Smith (NYU School of Medicine): susan.smith@med.nyu.edu; Sozanne R. Solmaz (State University of New York at Binghamton): ssolmaz@binghamton.edu; Caterina Strambio De
Castillia (UMass Medical School): caterina.strambio@umassmed.edu; Jianfeng Sun (The Rockefeller University): jsun01@rockefeller.edu; Anton Titov (DiagnosticDetectives.com):
anton.titov@diagnosticdetectives.com; Linas Urnavicius (The Rockefeller University): lurnaviciu@rockefeller.edu; Daniel Wacker (Icahn School of Medicine): daniel.wacker@mssm.
edu; Peter Walter (University of California, San Francisco): peter@walterlab.ucsf.edu; Gerry Waters (Novartis): gerrywaters57@gmail.com; Susan R. Wente (Vanderbilt University):
susan.wente@vanderbilt.edu; Richard A. Wing (Phosplatin Therapeutics): rwing@phosplatin.com; Richard Wong (Kanazawa University): rwong@staff.kanazawa-u.ac.jp; Howard
Worman (Columbia University): hjw14@columbia.edu; Richard W. Wozniak (University of Alberta): rick.wozniak@ualberta.ca; Jacques YaDeau (Hospital for Special Surgery yadeauj@
hss.edu; Nabeel Yaseen (Northwestern University): nyaseen@nm.org; Kimihisa Yoshida (Kobe Rosai Hospital): kimihisayoshida@icloud.com; Xiaolan Zhao (Memorial Sloan-
Kettering Cancer Center): zhaox1@mskcc.org; Hualin Zhong (Hunter College, CUNY): zhong@genectr.hunter.cuny.edu.
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