Hivatalos program | Kémia Koordinációs Intézet

Kedd

2025. június 10.

Szerda

2025. június 11.

Csütörtök

2025. június 12.

SFRR-E Young Investigator Satellite Day

Péntek

2025. június 13.

Szombat

2025. június 14.

Délelőtti szekció

Délelőtti szekció

Délelőtti szekció

Délelőtti szekció

Délelőtti szekció

8:30-9

Köszöntők

(PN, EA, OK, DT, KT)

9-10

Redox cycling and basic principles of redox biochemistry (EA)

10-10:15

Kávészünet

10:15-11:15 Oxidative stress, introduction to the concept (OK)

11:15-12

The thioredoxin system (ES)

8:30 – 9:15

Mitochondria-borne reactive oxygen species (OK)

9:15-10:00

Redox Regulation & Protein Folding: A Dynamic Interface (DT)

10-10:15

Kávészünet

10:15-11:00

Poly-ADP-ribosylation in oxidative stress signaling (LV)

11:00-11:45

Exercise and epigenetics (ZR)

7 - Indulás busszal Mádra

9 - 9:15 Kávészünet

9:15-10

Glutathione homeostasis and GST (KT)

10-10:45

Metals and redox stress (JL)

10:45-11:30

Trace elements and redox signaling (AK)

8:30-9:15

Nitric Oxide signaling (DT)

9:15-10

Iron-sulfur cluster proteins and redox regulation (LZ)

10-10:15

Kávészünet

10:15-11:00 Oxidative stress-inducing bacterial metabolites regulating breast cancer behavior (PB)

11-11:45

Using stable sulfur isotopes for tracking redox metabolism (CM)

8:30-12

Tanulási idő - lehetőség van konzultálni a tanárokkal

Ebéd 12:00 - 13:00 

Ebéd 12:00 - 13:00

Ebéd 12:00 - 13:00

Ebéd 12:00 - 13:00

Ebéd 12:00 - 13:00

Délutáni szekció

Délutáni szekció

Délutáni szekció

Délutáni szekció

Délutáni szekció

1-2

Selenium and selenoproteins in human health and disease (EA)

Nyilvános előadás a Learning Center 0.14. teremben

2-2:45 Glutaredoxins

(LC)

2:45-3

Kávészünet

3-3:45

Oxygen and blindness of premature newborns (GyB)

3:45 – 4:30

Reductive stress (KT)

4:30 – 5

Persulfidation in redox biology (ÉD)

1-2
Mitochondria and their quality control (OK)

2-3

Mouse models for redox studies (ES)

3-3:15

Kávészünet

3:15-4

Realigned transsulfuration in cancer models (PN)

4-4:45

Application and limitations of tools for redox analysis in live cells (KS)

4:45-5:30

Recent developments in recombinant selenoprotein studies (QC)

1-1:45

 Vascular calcification - What the clinician sees and does (BJ)

1:45-2:30

Integration of Signaling Pathways: Free Radical, Protein Phosphorylation and Steroids in Carcinogenesis (MFL)

2:30-2:45 Kávészünet

2:45 – ca. 5:15

Hallgatói előadások

1-2

Peroxidasin: a link between reactive oxygen species and extracellular matrix (MG)

2-2:30

Kávészünet

2:30 – 3:30

Career discussion (PN, EA, OK, DT, KT)

3:30 – 5

Tanulási idő - lehetőség van konzultálni a tanárokkal

1-3 Vizsga

7:00 –

Üdvözlő vacsora

5-8

Poszterszekció

6:30 –

Díjátadó és koccintás

1. csoport - Thiol redox systems

Keresztnév

Vezetéknév

Intézmény

Témakörök

Rachelle

Nelson

UNL

1. What is the function of thioredoxin? How many thioredoxin isoforms are in humans and where are they localized in the cell? Describe the structure of thioredoxin. Name at least three protein targets of thioredoxin.
2. What is the function of glutaredoxin? How many glutaredoxin isoforms are in humans and where are they localized in the cell? Describe the structure of glutaredoxin. Name at least three protein targets of glutaredoxin.
3. Describe the enzyme systems responsible for recycling thioredoxin and glutaredoxin by showing the structures and catalytic mechanisms. Where are these recycling enzymes localized in mammalian cells? In plants?
4. Describe the biosynthesis pathway for glutathione and the system for maintainining the intracelullar GSH/GSSG ratio. What are the concentrations of glutathione in different intracellular compartments (e.g., cytosol, mitochondria, endoplasmic reticulum). How is glutathione imported into cells?

Katalin Fruzsina

Magi

UD

Daniella

Dörgő

NIO

Bohdana

Sokolova

KI

Thomas

Dempster

MUSC

Balázs

Gombos

UVMB

2. csoport - Metals and Trace Elements in Redox Biology

Keresztnév

Vezetéknév

Intézmény

Témakörök

Emma

Bergmeyer

UNL

1. Which metals are the major contributors to hydroxyl radical formation in cells? What are the intracellular concentrations of these metals in mammals? Show the reaction by which these metals catalyze the formation of hydroxyl radicals. Provide an example of how mammalian cells import/export metals?
2. How do mammalian cells import/export metals? How are import/export systems used to protect against stress? Provide specific examples.
3. Give an example of a metalloprotein that is involved in oxygen or redox sensing? Describe the mechanism of response.
4. Give some examples on how Zinc, Copper and Iron are linked to different redox processes in cells.
5. Give four examples each of selenoproteins from bacteria, archaea and eukaryotes, as well as cysteine orthologues of each of these selenoproteins from other organisms. Provide some hypotheses on why or how selenoproteins have evolved, and why not all organisms have them.

Yuchao

Ding

UD

Martina

Serrano Álvarez

US

Andrea Cecília

Badari

UVMB

Mattia

Pantalone

KI

3. csoport – Redox regulation

Keresztnév

Vezetéknév

Intézmény

Témakörök

Brett

Hilbers

UNL

1. Describe the mechanism by which OxyR responds to hydrogen peroxide and regulates gene expression. Include structures if available. Describe at least five genes regulated by OxyR.
2. Describe the mechanism by which Yap1p is involved in the response to oxidative stress in S. cerevisiae. What target genes are activated by Yap1p?
3. Describe the Keap1-Nrf2-ARE signaling pathway. How does it help cells respond to oxidative stress? What genes are regulated by this system?
4. Give at least four levels of redox control that affect cellular responses to insulin.

Njomza

Gashi

UD

Viola

Varga

SU

Alexander

van Deventer

KI

Kathleen

Klinzing

MUSC

4. csoport – Oxidative Stress and Antioxidant Enzymes

Keresztnév

Vezetéknév

Intézmény

Témakörök

Adedotun

Adenofalu

UNL

1. How many superoxide dismutase (SOD) genes are in E. coli, B. subtilis, S. cerevisiae, and humans? What metal cofactors are utilized by the different SODs and where are the SODs localized? Describe the overall reaction catalyzed by SOD. Does SOD have a role in redox signaling? If so, how?
2. How many catalase genes are in E. coli, B. subtilis, S. cerevisiae, and humans? What cofactor does catalase require? Where are the different catalase enzymes localized? Are there any diseases or phenotype associated with lack of catalase?
3. How do peroxiredoxins protect cells against oxidative stress? Describe the reaction catalyzed by peroxidredoxin. Where are peroxiredoxins localized in mammalian cells? Do peroxiredoxins have a role in redox signaling? If so, how?
4. What are the biochemical functions of glutathione peroxidases? Describe the reaction catalyzed by glutathione peroxidase. Where are glutathione peroxidases localized in mammalian cells?
5. Describe DNA and lipid modifications that are found in cells exposed to oxidative stress agents? How do these modifications affect cell viability and contribute to disease progression?
6. What are some of the most common protein modifications that occur under oxidative stress? Describe how oxidative modification of SOD is associated with a disease.
7. How do cells repair oxidatively damaged DNA and proteins? Describe a specific example of one DNA and one protein repair enzyme.

Kristóf

Gui

UD

Maja

Mikolás

UD

Krisztina

Veszelyi

SU

Kia

Liermann-Wooldrik

UNMC

Linglong

Huang

KI

5. csoport – Reactive sulfur species in redox biology

Keresztnév

Vezetéknév

Intézmény

Témakörök

David

Obe

UNL

1. Describe sources of biological sulfur. Briefly present metabolic routes of amino acids cysteine and methionine.
2. Mention some pathophysiological roles of transsulfuration enzymes in cancer models and metabolic diseases (i.e. homocystinuria)
3. Reactive sulfur species arising from cysteine metabolism. Give 3 examples for the biological roles of H₂S and/or cysteine persulfidation. What is the role of selenoproteins in the metabolism of persulfide species.
4. How RSS may contribute to mitochondrial bioenergetics?

Katalin

Sikura

UD

Zoe

Seaford

MSU

Xueping

Jiang

KI

Kathryn

Glorioso

MUSC

Avia

Simmons

MSU