Hosts accepting graduate students and postdocs – by research area

The following researchers/laboratories are open to host an IUBMB research fellowship holder. Note that fellows can also choose to go to laboratories not listed on this page.

If you are a researcher interested in becoming a host, please use the following form:


No Entries Found
No Entries Found
</p><p>Reichmann, Dana</p><p>

Researcher Name: Reichmann, Dana

Research Area(s): Computational Biology, Microbiology, Protein Structure and Folding, Protein Synthesis and Degradation

Affiliation: The Hebrew University of Jerusalem

Country: Israel

Website 

Scientific Interests:

We are interested in molecular structures and dynamic protein assemblies formed during physiological stress conditions and aging.

One of the major focuses in the lab is understanding how cells maintain their “healthy”  and complex protein structures during stress conditions ( mainly increased oxidation) which is one of the main hallmarks of aging and age-related diseases (e.g., Alzheimer, Parkinson and others). Our overarching goal is to develop a novel technology that will enable us to unravel the mystery of the cellular “redox code” and the way it defines cells and their aging process.

To achieve this goal, we utilize and develop an extensive toolbox of technologies which able to quantify changes on cellular and molecular levels.  For example, we have developed fluorescence-based sensors, expressed inside cells at different organelles to monitor and quantify precise changes in intracellular oxidation. This allows us to study redox-dependent heterogeneity on a single cell level as well as isolate a subset of cells with pre-defined cellular oxidation for investigation of its proteome and redox-dependent regulation. 

Moreover, to identify redox switch proteins we are developing different proteomic platforms enabling mapping and quantifying mild changes in protein oxidation associated with a wide range of physiological conditions, aging and diseases.

On a protein level, we have established a toolbox of cutting-edge mass spectrometry technology to map conformational changes in proteins upon interactions and/or oxidation, specifically focusing on structurally challenging proteins, such as large and dynamic protein complexes.  These technologies include an automatized, high-resolution platform for conducting Hydrogen/Deuterium exchange coupled with mass spectrometry (HDX-MS), as well as in-vivo and in-vitro crosslinking (XL-MS).

 

This offer applies to trainees/researchers eligible for the following fellowships

Everyone (not restricted to fellowship holders)

Contact:

danare@mail.huji.ac.il

Close this page to return to list of all hosts

No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
No Entries Found
</p><p>Reichmann, Dana</p><p>

Researcher Name: Reichmann, Dana

Research Area(s): Computational Biology, Microbiology, Protein Structure and Folding, Protein Synthesis and Degradation

Affiliation: The Hebrew University of Jerusalem

Country: Israel

Website 

Scientific Interests:

We are interested in molecular structures and dynamic protein assemblies formed during physiological stress conditions and aging.

One of the major focuses in the lab is understanding how cells maintain their “healthy”  and complex protein structures during stress conditions ( mainly increased oxidation) which is one of the main hallmarks of aging and age-related diseases (e.g., Alzheimer, Parkinson and others). Our overarching goal is to develop a novel technology that will enable us to unravel the mystery of the cellular “redox code” and the way it defines cells and their aging process.

To achieve this goal, we utilize and develop an extensive toolbox of technologies which able to quantify changes on cellular and molecular levels.  For example, we have developed fluorescence-based sensors, expressed inside cells at different organelles to monitor and quantify precise changes in intracellular oxidation. This allows us to study redox-dependent heterogeneity on a single cell level as well as isolate a subset of cells with pre-defined cellular oxidation for investigation of its proteome and redox-dependent regulation. 

Moreover, to identify redox switch proteins we are developing different proteomic platforms enabling mapping and quantifying mild changes in protein oxidation associated with a wide range of physiological conditions, aging and diseases.

On a protein level, we have established a toolbox of cutting-edge mass spectrometry technology to map conformational changes in proteins upon interactions and/or oxidation, specifically focusing on structurally challenging proteins, such as large and dynamic protein complexes.  These technologies include an automatized, high-resolution platform for conducting Hydrogen/Deuterium exchange coupled with mass spectrometry (HDX-MS), as well as in-vivo and in-vitro crosslinking (XL-MS).

 

This offer applies to trainees/researchers eligible for the following fellowships

Everyone (not restricted to fellowship holders)

Contact:

danare@mail.huji.ac.il

Close this page to return to list of all hosts

No Entries Found
No Entries Found
No Entries Found
No Entries Found
</p><p>Reichmann, Dana</p><p>

Researcher Name: Reichmann, Dana

Research Area(s): Computational Biology, Microbiology, Protein Structure and Folding, Protein Synthesis and Degradation

Affiliation: The Hebrew University of Jerusalem

Country: Israel

Website 

Scientific Interests:

We are interested in molecular structures and dynamic protein assemblies formed during physiological stress conditions and aging.

One of the major focuses in the lab is understanding how cells maintain their “healthy”  and complex protein structures during stress conditions ( mainly increased oxidation) which is one of the main hallmarks of aging and age-related diseases (e.g., Alzheimer, Parkinson and others). Our overarching goal is to develop a novel technology that will enable us to unravel the mystery of the cellular “redox code” and the way it defines cells and their aging process.

To achieve this goal, we utilize and develop an extensive toolbox of technologies which able to quantify changes on cellular and molecular levels.  For example, we have developed fluorescence-based sensors, expressed inside cells at different organelles to monitor and quantify precise changes in intracellular oxidation. This allows us to study redox-dependent heterogeneity on a single cell level as well as isolate a subset of cells with pre-defined cellular oxidation for investigation of its proteome and redox-dependent regulation. 

Moreover, to identify redox switch proteins we are developing different proteomic platforms enabling mapping and quantifying mild changes in protein oxidation associated with a wide range of physiological conditions, aging and diseases.

On a protein level, we have established a toolbox of cutting-edge mass spectrometry technology to map conformational changes in proteins upon interactions and/or oxidation, specifically focusing on structurally challenging proteins, such as large and dynamic protein complexes.  These technologies include an automatized, high-resolution platform for conducting Hydrogen/Deuterium exchange coupled with mass spectrometry (HDX-MS), as well as in-vivo and in-vitro crosslinking (XL-MS).

 

This offer applies to trainees/researchers eligible for the following fellowships

Everyone (not restricted to fellowship holders)

Contact:

danare@mail.huji.ac.il

Close this page to return to list of all hosts

</p><p>Reichmann, Dana</p><p>

Researcher Name: Reichmann, Dana

Research Area(s): Computational Biology, Microbiology, Protein Structure and Folding, Protein Synthesis and Degradation

Affiliation: The Hebrew University of Jerusalem

Country: Israel

Website 

Scientific Interests:

We are interested in molecular structures and dynamic protein assemblies formed during physiological stress conditions and aging.

One of the major focuses in the lab is understanding how cells maintain their “healthy”  and complex protein structures during stress conditions ( mainly increased oxidation) which is one of the main hallmarks of aging and age-related diseases (e.g., Alzheimer, Parkinson and others). Our overarching goal is to develop a novel technology that will enable us to unravel the mystery of the cellular “redox code” and the way it defines cells and their aging process.

To achieve this goal, we utilize and develop an extensive toolbox of technologies which able to quantify changes on cellular and molecular levels.  For example, we have developed fluorescence-based sensors, expressed inside cells at different organelles to monitor and quantify precise changes in intracellular oxidation. This allows us to study redox-dependent heterogeneity on a single cell level as well as isolate a subset of cells with pre-defined cellular oxidation for investigation of its proteome and redox-dependent regulation. 

Moreover, to identify redox switch proteins we are developing different proteomic platforms enabling mapping and quantifying mild changes in protein oxidation associated with a wide range of physiological conditions, aging and diseases.

On a protein level, we have established a toolbox of cutting-edge mass spectrometry technology to map conformational changes in proteins upon interactions and/or oxidation, specifically focusing on structurally challenging proteins, such as large and dynamic protein complexes.  These technologies include an automatized, high-resolution platform for conducting Hydrogen/Deuterium exchange coupled with mass spectrometry (HDX-MS), as well as in-vivo and in-vitro crosslinking (XL-MS).

 

This offer applies to trainees/researchers eligible for the following fellowships

Everyone (not restricted to fellowship holders)

Contact:

danare@mail.huji.ac.il

Close this page to return to list of all hosts

No Entries Found