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Joohong Ahnn

Hanyang University · Biochemistry, Genetics and Molecular Biology

About the Lab

Professor Joohong Ahnn's research lab focuses on molecular and genetic mechanisms underlying cellular physiology and development in model organisms, particularly *C. elegans* and *E. coli*. The lab investigates conserved signaling pathways, including Ras-like GTPases, calcineurin phosphatase, and redox systems such as thioredoxin, with an emphasis on their roles in aging, autophagy, and cellular homeostasis. Additional research explores enzymes critical for metabolism and development, such as inorganic pyrophosphatase, and the therapeutic mechanisms of botulinum toxins in pain regulation. The lab integrates molecular genetics, cell biology, and biochemistry to uncover fundamental biological processes with implications for human health and disease.

agingautophagysignaling pathwaysredox regulationmodel organisms

Research Overview

Papers
115
Total Citations
3,605
Papers (5y)
11
Primary Field
Biochemistry, Genetics and Molecular Biology

Research Output Trend

Figures are computed from collected data and may differ slightly.

Publications per year (5y)
11total
2020
2021
2022
2023
2024
Citations per year (5y)
128total
20202021202220232024

Selected Papers

15
1
Article|146 citations·1986
A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins.
Joohong Ahnn, Paul E. March, Howard Takiff, Masayori Inouye
SJR Q1Proceedings of the National Academy of Sciences

The DNA sequence of a gene (era) located immediately downstream of the gene (rnc) encoding ribonuclease III of Escherichia coli was determined and found to encode a protein of 316 amino acid residues. The amino acid sequence of this protein, Era, has significant similarity to the yeast RAS proteins. Overexpression of the Era protein was achieved and GTP cross-linking experiments demonstrated that the protein was indeed capable of binding GTP, as are the yeast and mammalian ras gene products. The

Molecular BiologyBiochemistry, Genetics and Molecular Biology
2
Article|99 citations·2009
C. elegans Behavior of Preference Choice on Bacterial Food
Emad Abd-elmoniem Abada, Hyun Sung, Meenakshi Dwivedi, Byung-Jae Park, Sun-Kyung Lee, Joohong Ahnn
SJR Q1Molecules and Cells
AgingBiochemistry, Genetics and Molecular Biology
3
Article|63 citations·2004
Transcriptional Regulation and Life-span Modulation of Cytosolic Aconitase and Ferritin Genes in C.elegans
Young‐Il Kim, Jeong Hoon Cho, Ook Joon Yoo, Joohong Ahnn
SJR Q1Journal of Molecular Biology
AgingBiochemistry, Genetics and Molecular Biology
4
Review|57 citations·2010
Vacuolar (H+)-ATPases in Caenorhabditis elegans: What can we learn about giant H+ pumps from tiny worms?
Sun‐Kyung Lee, Weixun Li, Seong-Eon Ryu, Taiyoun Rhim, Joohong Ahnn
SJR Q1Biochimica et Biophysica Acta (BBA) - Bioenergetics
Molecular BiologyBiochemistry, Genetics and Molecular Biology
5
Article|56 citations·2009
Autophagy genes mediate the effect of calcineurin on life span inC. elegans
Meenakshi Dwivedi, Hyun‐Ok Song, Joohong Ahnn
SJR Q1AutophagyOA

Calcineurin (CaN) is a serine/threonine phosphatase, activated by Ca2+/calmodulin (Ca2+/CaM). CaN is known to regulate various cellular responses in different organisms. A recent study showed an extended life span in the calcineurin mutants of C. elegans. In this study, we report that calcineurin defective strains exhibit enhanced autophagy. In addition, we found two essential autophagy genes (bec-1 and atg-7) are required for the life-span extension in calcineurin null mutants [cnb-1(jh103)]. T

AgingBiochemistry, Genetics and Molecular Biology
6
Review|55 citations·2015
Botulinum Toxin as a Pain Killer: Players and Actions in Antinociception
Dong-Wan Kim, Sun-Kyung Lee, Joohong Ahnn
SJR Q1ToxinsOA

Botulinum neurotoxins (BoNTs) have been widely used to treat a variety of clinical ailments associated with pain. The inhibitory action of BoNTs on synaptic vesicle fusion blocks the releases of various pain-modulating neurotransmitters, including glutamate, substance P (SP), and calcitonin gene-related peptide (CGRP), as well as the addition of pain-sensing transmembrane receptors such as transient receptor potential (TRP) to neuronal plasma membrane. In addition, growing evidence suggests that

NeurologyMedicine
7
Article|51 citations·2009
C. elegans STI-1, the Homolog of Sti1/Hop, Is Involved in Aging and Stress Response
Hyun‐Ok Song, Wonhae Lee, Kiyoung An, Hye-suk Lee, Jeong Hoon Cho, Zee‐Yong Park, Joohong Ahnn
SJR Q1Journal of Molecular Biology
AgingBiochemistry, Genetics and Molecular Biology
8
Article|51 citations·1994
A screen for genetic loci required for body-wall muscle development during embryogenesis in Caenorhabditis elegans.
Joohong Ahnn, Andrew Fire
SJR Q1GeneticsOA

We have used available chromosomal deficiencies to screen for genetic loci whose zygotic expression is required for formation of body-wall muscle cells during embryogenesis in Caenorhabditis elegans. To test for muscle cell differentiation we have assayed for both contractile function and the expression of muscle-specific structural proteins. Monoclonal antibodies directed against two myosin heavy chain isoforms, the products of the unc-54 and myo-3 genes, were used to detect body-wall muscle di

AgingBiochemistry, Genetics and Molecular Biology
9
Article|50 citations·2005
Thioredoxin is related to life span regulation and oxidative stress response inCaenorhabditis elegans
Changhoon Jee, Liviu Vanoaica, Jungsoo Lee, Byung Jae Park, Joohong Ahnn
SJR Q2Genes to CellsOA

Thioredoxin, an oxidoreductase, is a multifunction protein. The thioredoxin system is composed of NADPH, thioredoxin reductase and thioredoxin. This enzyme is highly conserved from bacteria to humans. We have characterized TRX-1, a thioredoxin homolog in C. elegans, which has about 36% identity in amino acid sequence with human thioredoxin. By gfp reporter system, trx-1 has been shown to be restrictedly expressed in ASI and ASJ neurons and in intestine. Immunostaining confirmed the intestinal ex

AgingBiochemistry, Genetics and Molecular Biology
10
Article|49 citations·2007
PYP‐1, inorganic pyrophosphatase, is required for larval development and intestinal function in C. elegans
Kyung Min Ko, Wonhae Lee, Jae-Ran Yu, Joohong Ahnn
SJR Q1FEBS LettersOA

Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into phosphate (Pi), which provides a thermodynamic driving force for important biosynthetic reactions. The nematode Caenorhabditis elegans gene C47E12.4 encodes a PPase (PYP-1) which shows 54% amino acid identity with human PPase. PYP-1 exhibits specific enzyme activity and is mainly expressed in the intestinal and nervous system. A null mutant of pyp-1 reveals a developmental arrest at early larval stag

AgingBiochemistry, Genetics and Molecular Biology
11
Article|47 citations·2003
The Caenorhabditis elegans Homologue of Down Syndrome Critical Region 1, RCN-1, Inhibits Multiple Functions of the Phosphatase Calcineurin
Jin Il Lee, Bijaya K. Dhakal, Jungsoo Lee, Jaya Bandyopadhyay, Sang Young Jeong, Soo Hyun Eom, Do Han Kim, Joohong Ahnn
SJR Q1Journal of Molecular Biology
Molecular BiologyBiochemistry, Genetics and Molecular Biology
12
Article|44 citations·2000
Two isoforms of sarco/endoplasmic reticulum calcium ATPase (SERCA) are essential in Caenorhabditis elegans
Jeong Hoon Cho, Jaya Bandyopadhyay, Jiyeon Lee, Chul‐Seung Park, Joohong Ahnn
SJR Q2Gene
AgingBiochemistry, Genetics and Molecular Biology
13
Article|37 citations·2004
Opposing Functions of Calcineurin and CaMKII Regulate G-protein Signaling in Egg-laying Behavior of C.elegans
Jungsoo Lee, Changhoon Jee, Hyun‐Ok Song, Jaya Bandyopadhyay, Jin I. Lee, Jae-Ran Yu, Jiyeon Lee, Byung-Jae Park, Joohong Ahnn
SJR Q1Journal of Molecular Biology
AgingBiochemistry, Genetics and Molecular Biology
14
Article|36 citations·2012
Two Thioredoxin Reductases, trxr-1 and trxr-2, Have Differential Physiological Roles in Caenorhabditis elegans
Weixun Li, Jaya Bandyopadhyay, Hyun Sook Hwaang, Byung-Jae Park, Jeong Hoon Cho, Jin II Lee, Joohong Ahnn, Sun-Kyung Lee
SJR Q1Molecules and CellsOA

Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide reductase family, which mainly functions in the thioredoxin system. TrxR is found in all living organisms and exists in two major ubiquitous isoenzymes in higher eukaryotic cells; One is cytosolic and the other mitochondrial. Mitochondrial TrxR functions to protect mitochondria from oxidative stress, where reactive oxidative species are mainly generated, while cytosolic TrxR plays a role to maintain optimal oxido-reduc

Nutrition and DieteticsNursing
15
Article|30 citations·2007
Differential Requirement of Unfolded Protein Response Pathway for Calreticulin Expression in Caenorhabditis elegans
Dukgyu Lee, Gunasekaran Singaravelu, Byung-Jae Park, Joohong Ahnn
SJR Q1Journal of Molecular Biology
Cell BiologyBiochemistry, Genetics and Molecular Biology

Research Areas

AgingMolecular BiologyCell BiologyImmunology and AllergyPlant ScienceCellular and Molecular Neuroscience

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