Skip to main content

이형호 교수

Hyung Ho Lee

서울대학교 · 생화학·유전·분자생물학

연구실 소개

이형호 교수의 연구실은 세포 내 막 분리 및 세포 분열 과정에서 핵심적인 역할을 하는 ESCRT 시스템과 관련된 단백질 복합체의 구조와 기능을 중심으로 연구를 진행하고 있습니다. 특히, HIV-1의 탈출, 세포 분열의 마지막 단계인 cytokinesis, 그리고 림프계관련 소기관 형성 등 생리적 과정에서의 단백질 상호작용 메커니즘을 고해상도 구조 생물학적 접근을 통해 규명하고 있습니다. 또한, 핵내 단백질의 기능적 다양성과 전사 인자 간의 상호작용 메커니즘에 대해서도 깊이 있는 연구를 수행하고 있습니다.

ESCRT 시스템단백질 상호작용고해상도 구조세포 분열전사 조절

연구 현황

논문 수
142
총 인용 수
2,005
최근 5년 논문
39
주요 분야
생화학·유전·분자생물학

연구 성과 추이

표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.

5개년 연도별 논문 게재 수
39총합
2022
2023
2024
2025
2026
5개년 연도별 피인용 수
233총합
20222023202420252026

주요 논문

15
1
논문|인용수 257·2008
Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55
Hyung Ho Lee, Natalie Elia, Rodolfo Ghirlando, Jennifer Lippincott‐Schwartz, James H. Hurley
SJR Q1FWCI 6.4ScienceOA

The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT and ALIX-b

Cell BiologyBiochemistry, Genetics and Molecular Biology
2
논문|인용수 109·2007
Crystal structure of human nucleophosmin‐core reveals plasticity of the pentamer–pentamer interface
Hyung Ho Lee, Hyoun Sook Kim, Ji Yong Kang, Byung Il Lee, Jun Yong Ha, Hye Jin Yoon, Seung Oe Lim, Guhung Jung, Se Won Suh
SJR Q1FWCI 0.7Proteins Structure Function and Bioinformatics

Human nucleophosmin (NPM; also known as B23, NO38, or numatrin), encoded by the NPM1 gene, is an abundant phosphoprotein in nucleoli.1-3 It is primarily localized to nucleolus but has been shown to shuttle between the cytoplasm and nucleus.4 Two isoforms of NPM, designated B23.1 and B23.2,5 consist of 294 and 259 amino acid residues, respectively, with B23.1 being the prevalent form in all tissues.5, 6 The C-terminal 35 amino acids of B23.1 are missing from B23.2 and the N-terminal 257 residues

Molecular BiologyBiochemistry, Genetics and Molecular Biology
3
논문|인용수 99·2007
Structural and Functional Insights into Dom34, a Key Component of No-Go mRNA Decay
Hyung Ho Lee, Youn-Sung Kim, Kyoung Hoon Kim, Inha Heo, Sang Kyu Kim, Olesya Kim, Hye Kyung Kim, Ji Yoon, Hyoun Sook Kim, Dojin Kim, Sang Jae Lee, Hye Jin Yoon
SJR Q1FWCI 3.6Molecular CellOA
Molecular BiologyBiochemistry, Genetics and Molecular Biology
4
논문|인용수 71·2011
Assembly and Architecture of Biogenesis of Lysosome-related Organelles Complex-1 (BLOC-1)
Hyung Ho Lee, Daniel Němeček, Christina Schindler, William J. Smith, Rodolfo Ghirlando, Alasdair C. Steven, Juan S. Bonifacino, James H. Hurley
SJR Q1FWCI 2.0Journal of Biological ChemistryOA

BLOC-1 (biogenesis of lysosome-related organelles complex-1) is critical for melanosome biogenesis and has also been implicated in neurological function and disease. We show that BLOC-1 is an elongated complex that contains one copy each of the eight subunits pallidin, Cappuccino, dysbindin, Snapin, Muted, BLOS1, BLOS2, and BLOS3. The complex appears as a linear chain of eight globular domains, ∼300 Å long and ∼30 Å in diameter. The individual domains are flexibly connected such that the linear

Cell BiologyBiochemistry, Genetics and Molecular Biology
5
논문|인용수 61·2020
Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide
Kyung-Jin Min, Hye‐Jin Yoon, Ji Young Park, Mithu Baidya, Hemlata Dwivedi‐Agnihotri, Jagannath Maharana, Madhu Chaturvedi, Ka Young Chung, Arun K. Shukla, Hyung Ho Lee
SJR Q1FWCI 3.1StructureOA
Molecular BiologyBiochemistry, Genetics and Molecular Biology
6
논문|인용수 35·2004
Crystal Structure of T-protein of the Glycine Cleavage System
Hyung Ho Lee, Dojin Kim, Hyung Jun Ahn, Jun Yong Ha, Se Won Suh
SJR Q1FWCI 1.1Journal of Biological ChemistryOA

The glycine cleavage system catalyzes the oxidative decarboxylation of glycine in bacteria and in mitochondria of animals and plants. Its deficiency in human causes nonketotic hyperglycinemia, an inborn error of glycine metabolism. T-protein, one of the four components of the glycine cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It catalyzes the transfer of the methylene carbon unit to tetrahydrofolate from the methylamine group covalently attached to the lipoamide arm

BiochemistryBiochemistry, Genetics and Molecular Biology
7
논문|인용수 22·2007
Crystal structure of the <i>Helicobacter pylori</i> enoyl‐acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan
Hyung Ho Lee, Jinho Moon, Se Won Suh
SJR Q1FWCI 1.3Proteins Structure Function and BioinformaticsOA

Enoyl-ACP reductase (ENR; EC 1.3.1.9), encoded by the fabI gene, is a key enzyme of the Type II fatty-acid biosynthetic system in prokaryotes and plants. It uses NADH or NADPH as the cofactor to reduce the double bond between C2 and C3 positions of a fatty acyl chain bound to the acyl carrier protein in the terminal rate-limiting step of the fatty acid chain elongation cycle.1 Because it shows low overall sequence homology with mammalian enzymes, it is a potential target for antibacterial discov

Organic ChemistryChemistry
8
논문|인용수 17·2022
FOXL2 and FOXA1 cooperatively assemble on the <i>TP53</i> promoter in alternative dimer configurations
Yuri Choi, Yongyang Luo, Seung Hwa Lee, Hanyong Jin, Hye‐Jin Yoon, Yoonsoo Hahn, Jeehyeon Bae, Hyung Ho Lee
SJR Q1FWCI 1.4Nucleic Acids ResearchOA

Although both the p53 and forkhead box (FOX) family proteins are key transcription factors associated with cancer progression, their direct relationship is unknown. Here, we found that FOX family proteins bind to the non-canonical homotypic cluster of the p53 promoter region (TP53). Analysis of crystal structures of FOX proteins (FOXL2 and FOXA1) bound to the p53 homotypic cluster indicated that they interact with a 2:1 stoichiometry accommodated by FOX-induced DNA allostery. In particular, FOX

Molecular BiologyBiochemistry, Genetics and Molecular Biology
9
논문|인용수 17·2016
Structural and Biochemical Studies Reveal a Putative FtsZ Recognition Site on the Z-ring Stabilizer ZapD
HwaJung Choi, Kyung-Jin Min, Bunzo Mikami, Hye‐Jin Yoon, Hyung Ho Lee
SJR Q1FWCI 1.5Molecules and CellsOA

FtsZ, a tubulin homologue, is an essential protein of the Z-ring assembly in bacterial cell division. It consists of two domains, the N-terminal and C-terminal core domains, and has a conserved C-terminal tail region. Lateral interactions between FtsZ protofilaments and several Z-ring associated proteins (Zaps) are necessary for modulating Z-ring formation. ZapD, one of the positive regulators of Z-ring assembly, directly binds to the C-terminal tail of FtsZ and promotes stable Z-ring formation

GeneticsBiochemistry, Genetics and Molecular Biology
10
논문|인용수 16·2011
Crystal Structure of Phosphopantetheine Adenylyltransferase from Enterococcus faecalis in the Ligand-Unbound State and in Complex with ATP and Pantetheine
Hye‐Jin Yoon, Ji Yong Kang, Bunzo Mikami, Hyung Ho Lee, Se Won Suh
SJR Q1FWCI 0.9Molecules and CellsOA
NeurologyNeuroscience
11
논문|인용수 14·2007
Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: Scuticociliatida)
Sang Jung Ahn, Jung Soo Seo, Moo‐Sang Kim, Soo Jin Jeon, Na Young Kim, Jae Ho Jang, Ki Hong Kim, Yong‐Ki Hong, Joon Ki Chung, Hyung Ho Lee
SJR Q3FWCI 0.4Molecular and Biochemical Parasitology
Molecular BiologyBiochemistry, Genetics and Molecular Biology
12
논문|인용수 14·2009
The structure of<i>Staphylococcus aureus</i>phosphopantetheine adenylyltransferase in complex with 3′-phosphoadenosine 5′-phosphosulfate reveals a new ligand-binding mode
Hyung Ho Lee, H.J. Yoon, Ji Yong Kang, Ji Hyeon Park, Dojin Kim, Kwang-Hyun Choi, Seungkyu Lee, Jin Su Song, Hie‐Joon Kim, Se Won Suh
FWCI 1.1Acta Crystallographica Section F Structural Biology and Crystallization CommunicationsOA

Bacterial phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway. It catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate. Previous structural studies have revealed how several ligands are recognized by bacterial PPATs. ATP, ADP, Ppant and dPCoA bind to the same binding site in a highly similar manner, while CoA binds to a partially overla

NeurologyNeuroscience
13
논문|인용수 13·2005
Crystal Structure of a Metal Ion-bound IS200 Transposase
Hyung Ho Lee, Ji Yoon, Hyoun Sook Kim, Ji Yong Kang, Kyoung Hoon Kim, Dojin Kim, Jun Yong Ha, Bunzo Mikami, Hye Jin Yoon, Se Won Suh
SJR Q1FWCI 0.5Journal of Biological ChemistryOA

IS200 transposases, present in many bacteria and Archaea, appear to be distinct from other groups of transposases. To provide a structural basis for understanding the action of IS200 transposases, we have determined the crystal structure of the SSO1474 protein from Sulfolobus solfataricus, a member of the IS200 family, in both Mn(2+)-bound and Mn(2+)-free forms. Its monomer fold is distinct from other classes of structurally characterized transposases. Two monomers form a tight dimer by exchangi

Molecular BiologyBiochemistry, Genetics and Molecular Biology
14
논문|인용수 10·2008
MMTS, a New Subfamily of Tc1-like Transposons
Sang Jung Ahn, Moo‐Sang Kim, Jae Ho Jang, Sang Uk Lim, Hyung Ho Lee
SJR Q1FWCI 1.7Molecules and CellsOA

A novel Tc1-like transposable element has been identified as a new DNA transposon in the mud loach, Misgurnus mizolepis. The M. mizolepis Tc1-like transposon (MMTS) is comprised of inverted terminal repeats and a single gene that codes Tc1-like transposase. The deduced amino acid sequence of the transposase-encoding region of MMTS transposon contains motifs including DDE motif, which was previously recognized in other Tc1-like transposons. However, putative MMTS transposase has only 34-37% ident

Plant ScienceAgricultural and Biological Sciences
15
논문|인용수 9·2020
Molecular dynamics study with mutation shows that N‐terminal domain structural re‐orientation in Niemann‐Pick type C1 is required for proper alignment of cholesterol transport
Hye‐Jin Yoon, Jian Jeong, Hyung Ho Lee, Soonmin Jang
SJR Q1FWCI 1.0Journal of NeurochemistryOA

The lysosomal membrane protein Niemann-Pick type C1 (NPC1) and Niemann-Pick type C2 (NPC2) are main players of cholesterol control in the lysosome and it is known that the mutation on these proteins leads to the cholesterol trafficking-related neurodegenerative disease, which is called the NPC disease. The mutation R518W or R518Q on the NPC1 is one of the type of disease-related mutation that causes cholesterol transports to be cut in half, which results in the accumulation of cholesterol and li

PhysiologyMedicine

대표 연구 분야

Molecular BiologyMaterials ChemistryRenewable Energy, Sustainability and the EnvironmentCell BiologyGeneticsPhysiology

이형호 교수의 연구를 Nubint에서 더 깊이 살펴보세요

이 연구실의 논문을 앱에서 열어 AI와 함께 읽고, 핵심을 요약하고, 내 글에 인용하세요.