The Wolf Prize laureates

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Stephen L. Buchwald

Wolf Prize Laureate in Chemistry

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Moshe Safdie

Wolf Prize Laureate in Architecture 2019

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

John F. Hartwig

Wolf Prize Laureate in Chemistry 2019

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Jeffrey Friedman

Wolf Prize Laureate in Medicine 2019

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Jean Francois le Gall

Wolf Prize Laureate in Mathematics 2019

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Lewis Cantley

Wolf Prize Laureate in Medicine 2016

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

C. Ronald Kahn

Wolf Prize Laureate in Medicine 2016

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Olafur Eliasson

Jean-François Le Gall has made several deep and elegant contributions to the theory of stochastic processes. His work on the fine properties of Brownian motions solved many difficult problems, such as the characterization of sets visited multiple times and the behavior of the volume of its neighborhood – the Brownian sausage. Le Gall made groundbreaking advances in the theory of branching processes, which arise in many applications. In particular, his introduction of the Brownian snake and his studies of its properties revolutionized the theory of super-processes – generalizations of Markov processes to an evolving cloud of dying and splitting particles. He then used some of these tools for achieving a spectacular breakthrough in the mathematical understanding of 2D quantum gravity. Le Gall established the convergence of uniform planar maps to a canonical random metric object, the Brownian map, and showed that it almost surely has Hausdorff dimension 4 and is homeomorphic to the 2-spher

Prizes and scholarships laureates

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Malachi Noked

Winner of Krill Prize 2019
Bar-Ilan University

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Yaron Fuchs

Winner of Krill Prize 2019
Technion

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Dafna Shahaf

Winner of Krill Prize 2019
The Hebrew University
of Jerusalem

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Shahar Kvatinsky

Winner of Krill Prize 2019
Technion

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Ofer Firstenberg

Winner of Krill Prize 2019
Weizmann Institute

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Neta Regev-Rudzki

Winner of Krill Prize 2019
Weizmann Institute

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Noga Ron-Zewi

Winner of Krill Prize 2019
University of Haifa

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Baruch Barzel

Winner of Krill Prize 2019
Bar-Ilan University

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Amnon Bar-Shir

Winner of Krill Prize 2019
Weismann Institute

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Ori Katz

Winner of Krill Prize 2019
The Hebrew University
of Jerusalem

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Charles E. Diesendruck

Winner of Krill Prize 2018
Technion

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Yakov Babichenko

Winner of Krill Prize 2018
Technion

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Elad Gross

Winner of Krill Prize 2018
The Hebrew University
of Jerusalem

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Ayelet Erez

Winner of Krill Prize 2018
Weismann Institute

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Amit Sever

Winner of Krill Prize 2018
Tel-Aviv University

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Adi Salomon

Winner of Krill Prize 2018
Bar-Ilan University

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Meital Landau

Winner of Krill Prize 2018
Technion

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

Itzhak Tamo

Winner of Krill Prize 2018
Tel-Aviv University

Technion
New Structure-activity
Paradigms for Amyloids
from Pathogenic Microbes

 

Microbial functional amyloids form protein fibrils that
serve as key virulence determinants and participate
in aggressive infections. Yet, amyloids are mostly
known for their involvement in fatal neurodegenerative
diseases and their structures have been studied
mostly in eukaryotes.
Our lab pioneered the investigations of bacterial
functional amyloids at the atomic level, and published
the first structure of an amyloid fibril from bacteria
(Tayeb-Fligelman et. al., Science 2017). The structure
revealed a unique cross-α amyloid-like fibril which
presented a paradigm shift in amyloid research,
where it has been believed that β-rich structures are
central. The novel fibril structure is of PSMα3, a
virulent peptide secreted by the pathogenic bacterium
Staphylococcus aureus that is toxic to human cells.
Given this and other results we show that the structural
and functional repertoire of microbial amyloids is far
more diverse than previously anticipated, providing
a rich source of targets for antimicrobial drug discovery.

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