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  <title>Repository Collection: null</title>
  <link rel="alternate" href="https://scholar.dgist.ac.kr/handle/20.500.11750/9954" />
  <subtitle />
  <id>https://scholar.dgist.ac.kr/handle/20.500.11750/9954</id>
  <updated>2026-09-26T06:06:57Z</updated>
  <dc:date>2026-09-26T06:06:57Z</dc:date>
  <entry>
    <title>S100 Calcium-Binding Protein P Predicts Early Recurrence and Poor Survival in Distal Cholangiocarcinoma: A Proteomics Study</title>
    <link rel="alternate" href="https://scholar.dgist.ac.kr/handle/20.500.11750/60862" />
    <author>
      <name>Kim, Hyemin</name>
    </author>
    <author>
      <name>Huh, Sunghyun</name>
    </author>
    <author>
      <name>Han, In Woong</name>
    </author>
    <author>
      <name>Choi, Young Hoon</name>
    </author>
    <author>
      <name>Choi, Kyu</name>
    </author>
    <author>
      <name>Lee, Seung-Eun</name>
    </author>
    <author>
      <name>Lee, Se-Hoon</name>
    </author>
    <author>
      <name>Jang, Kee-Taek</name>
    </author>
    <author>
      <name>Lee, Jong Kyun</name>
    </author>
    <author>
      <name>Lee, Kyu Taek</name>
    </author>
    <author>
      <name>Park, Joo Kyung</name>
    </author>
    <author>
      <name>Kim, Min-Sik</name>
    </author>
    <author>
      <name>Lee, Kwang Hyuk</name>
    </author>
    <id>https://scholar.dgist.ac.kr/handle/20.500.11750/60862</id>
    <updated>2026-09-23T05:10:14Z</updated>
    <published>2026-05-31T15:00:00Z</published>
    <summary type="text">Title: S100 Calcium-Binding Protein P Predicts Early Recurrence and Poor Survival in Distal Cholangiocarcinoma: A Proteomics Study
Author(s): Kim, Hyemin; Huh, Sunghyun; Han, In Woong; Choi, Young Hoon; Choi, Kyu; Lee, Seung-Eun; Lee, Se-Hoon; Jang, Kee-Taek; Lee, Jong Kyun; Lee, Kyu Taek; Park, Joo Kyung; Kim, Min-Sik; Lee, Kwang Hyuk
Abstract: Distal cholangiocarcinoma (dCCA) is a rare malignancy with a poor prognosis, necessitating novel biomarkers for acute prognosis and optimal treatment selection. This study aimed to elucidate the proteomic landscape of dCCA and identify novel biomarkers associated with improved patient outcomes. Proteomic profiling was conducted on 18 surgical samples from patients with dCCA by using shotgun liquid chromatography with tandem mass spectrometry. Patients were categorized into early recurrence (n = 9) and nonearly recurrence (n = 9) groups. Validation was performed via immunohistochemical (IHC) analysis on an independent dCCA cohort of 26 tissue microarray samples. A total of 6804 proteins were identified, and differential expression and functional enrichment analyses revealed 219 upregulated proteins in the early recurrence group, associated with biological processes of the extracellular matrix and cellular interaction. Among these, S100 calcium-binding protein P (S100P) correlated with EZR, and LGALS3BP was significantly overexpressed in the early recurrence group. Furthermore, high S100P expression was identified as a strong independent risk factor for recurrence, with a hazard ratio (HR) of 4.55 (95% CI, 1.609-12.841, p = 0.004) and mortality (HR 4.99, 95% CI 1.794-12.880, p = 0.002). These findings identify S100P as a prognostic biomarker for dCCA, suggesting its clinical utility for postoperative risk stratification and patient management.</summary>
    <dc:date>2026-05-31T15:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Bronchoalveolar lavage proteomics in exacerbation of bronchiectasis</title>
    <link rel="alternate" href="https://scholar.dgist.ac.kr/handle/20.500.11750/59936" />
    <author>
      <name>Lee, Ju-yeon</name>
    </author>
    <author>
      <name>Yang, Jiyoul</name>
    </author>
    <author>
      <name>Kim, Jinyoung</name>
    </author>
    <author>
      <name>Do, YeJi</name>
    </author>
    <author>
      <name>Kim, Min-Sik</name>
    </author>
    <author>
      <name>Kye, Dong-eun</name>
    </author>
    <author>
      <name>Min, Geonhui</name>
    </author>
    <author>
      <name>Jeon, In-sook</name>
    </author>
    <author>
      <name>Kim, Eung-gook</name>
    </author>
    <author>
      <name>Choi, Joong-kook</name>
    </author>
    <author>
      <name>Choi, Minjae</name>
    </author>
    <author>
      <name>Lee, Hyun</name>
    </author>
    <author>
      <name>Yang, Bumhee</name>
    </author>
    <id>https://scholar.dgist.ac.kr/handle/20.500.11750/59936</id>
    <updated>2026-02-05T18:01:21Z</updated>
    <published>2025-09-30T15:00:00Z</published>
    <summary type="text">Title: Bronchoalveolar lavage proteomics in exacerbation of bronchiectasis
Author(s): Lee, Ju-yeon; Yang, Jiyoul; Kim, Jinyoung; Do, YeJi; Kim, Min-Sik; Kye, Dong-eun; Min, Geonhui; Jeon, In-sook; Kim, Eung-gook; Choi, Joong-kook; Choi, Minjae; Lee, Hyun; Yang, Bumhee
Abstract: Background: The molecular pathophysiology underlying the development of bronchiectasis with exacerbation at the proteomic level has not been clarified using bronchoalveolar lavage fluid samples. This study aimed to evaluate the bronchoalveolar lavage fluid inflammatory profiles associated with exacerbation of bronchiectasis. Methods: We analyzed the bronchoalveolar lavage fluid specimens from 4 patients in the exacerbation status and 4 patients in a stable status using liquid chromatography-tandem mass spectrometry. Results: A total of 1,577 proteins were identified using proteomic analysis, with 127 differentially expressed proteins. Of 127 differentially expressed proteins, 23 proteins showed more than 2-fold differences between exacerbation and stable status groups. The exacerbation status was associated with 18 upregulated proteins (TPI1, CRP, BPI, ORM1, PTPRE, S100A9, BPY2, TPM4, ERVFC1-1, CYS1, CLEC3B, S100A8, PSAT1, NDUFA10, MDGA1, SPRR3, ALDOA, and PSMB2) and five downregulated proteins (MUC5B, HSPE1, KLK13, IGHA1, and MUC5AC). Pathway analysis revealed that the neutrophil degranulation pathway (R-HSA-6798695) was the most enriched pathway in these proteins, followed by the C-type lectin receptor pathway (R-HSA-5621481). Conclusion: The bronchoalveolar lavage fluid protein expression in patients in the exacerbation status of bronchiectasis was significantly different from that in patients in the stable status, indicating that neutrophil degranulation and C-type lectin receptor pathways are the most enriched pathways during exacerbation.</summary>
    <dc:date>2025-09-30T15:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Synergistic NH2-MIL-101(Fe)/thermally reduced graphene oxide composite integrated voltammetric sensor for carcinogenic chrysene in particulate matter</title>
    <link rel="alternate" href="https://scholar.dgist.ac.kr/handle/20.500.11750/59932" />
    <author>
      <name>Karuppiah, Chelladurai</name>
    </author>
    <author>
      <name>Kim, Seongyeop</name>
    </author>
    <author>
      <name>Lee, So Yeon</name>
    </author>
    <author>
      <name>Lee, Gyudong</name>
    </author>
    <author>
      <name>Ahmed, Imteaz</name>
    </author>
    <author>
      <name>Jhung, Sung Hwa</name>
    </author>
    <author>
      <name>Baek, Song-Yee</name>
    </author>
    <author>
      <name>Yim, Yong-Hyeon</name>
    </author>
    <author>
      <name>Alam, Rafiqul</name>
    </author>
    <author>
      <name>Kim, Min-Sik</name>
    </author>
    <author>
      <name>Lee, Hye Jin</name>
    </author>
    <id>https://scholar.dgist.ac.kr/handle/20.500.11750/59932</id>
    <updated>2026-02-08T16:10:21Z</updated>
    <published>2025-11-30T15:00:00Z</published>
    <summary type="text">Title: Synergistic NH2-MIL-101(Fe)/thermally reduced graphene oxide composite integrated voltammetric sensor for carcinogenic chrysene in particulate matter
Author(s): Karuppiah, Chelladurai; Kim, Seongyeop; Lee, So Yeon; Lee, Gyudong; Ahmed, Imteaz; Jhung, Sung Hwa; Baek, Song-Yee; Yim, Yong-Hyeon; Alam, Rafiqul; Kim, Min-Sik; Lee, Hye Jin
Abstract: Atmospheric particulate matter (PM) containing polycyclic aromatic hydrocarbons (PAHs) poses serious health risks due to its carcinogenic nature. Chrysene (CHR), a priority pollutant known for its toxicity and persistence, necessitates the development of sensitive and cost-effective detection methods. In this study, we report, for the first time, a highly sensitive voltammetric sensor for CHR detection using a composite of NH2-MIL-101(Fe) and thermally reduced graphene oxide (TRGO) modified glassy carbon electrode (NH2-MIL-101(Fe)/TRGO/GCE). The composite was prepared via ultrasonication of TRGO with NH2-MIL-101(Fe) and synthesized using a microwave-assisted method. Comprehensive physicochemical characterization, including various spectroscopic
and electrochemical measurements alongside thermogravimetry and N2 adsorption isotherms, confirmed the composite’s crystallinity, high porosity, and conductivity. Under optimal conditions, the NH2-MIL-101(Fe)/ TRGO/GCE sensor achieved a low limit of detection (0.037 µM), high sensitivity (0.345 µA µM− 1 ), and a wide linear detection range (0.1–240 μM). The sensor demonstrated superior selectivity for CHR, even in the presence of other carcinogenic PAHs, including naphthalene, phenanthrene, fluorene, pyrene, and benzo[a]pyrene. These impressive attributes were primarily due to the synergistic effects of the composite, including strong π-π interaction and rapid electron transfer. Furthermore, the sensor showed excellent selectivity, reproducibility, and high recovery rates when applied to CHR detection in complex PM samples and other contaminant sources such as soil and river water. These results demonstrate the NH2-MIL-101(Fe)/TRGO/GCE sensor as a promising technology for pollutant analysis and environmental monitoring in practical applications.</summary>
    <dc:date>2025-11-30T15:00:00Z</dc:date>
  </entry>
  <entry>
    <title>A transcriptomic and proteomic map of primary human cell types</title>
    <link rel="alternate" href="https://scholar.dgist.ac.kr/handle/20.500.11750/59923" />
    <author>
      <name>Mun, Dong-Gi</name>
    </author>
    <author>
      <name>Madugundu, Anil K.</name>
    </author>
    <author>
      <name>Renuse, Santosh</name>
    </author>
    <author>
      <name>Nirujogi, Raja Sekhar</name>
    </author>
    <author>
      <name>Na, Chan Hyun</name>
    </author>
    <author>
      <name>Kim, Min-Sik</name>
    </author>
    <author>
      <name>Saraswat, Mayank</name>
    </author>
    <author>
      <name>Singh, Smrita</name>
    </author>
    <author>
      <name>Ramarajan, Madan G.</name>
    </author>
    <author>
      <name>Tiwary, Shivani</name>
    </author>
    <author>
      <name>Cox, Jurgen</name>
    </author>
    <author>
      <name>Prakash, Amol</name>
    </author>
    <author>
      <name>Halushka, Marc K.</name>
    </author>
    <author>
      <name>Burns, Kathleen H.</name>
    </author>
    <author>
      <name>Kandasamy, Richard k</name>
    </author>
    <author>
      <name>Pandey, Akhilesh</name>
    </author>
    <id>https://scholar.dgist.ac.kr/handle/20.500.11750/59923</id>
    <updated>2026-04-15T08:13:25Z</updated>
    <published>2025-12-31T15:00:00Z</published>
    <summary type="text">Title: A transcriptomic and proteomic map of primary human cell types
Author(s): Mun, Dong-Gi; Madugundu, Anil K.; Renuse, Santosh; Nirujogi, Raja Sekhar; Na, Chan Hyun; Kim, Min-Sik; Saraswat, Mayank; Singh, Smrita; Ramarajan, Madan G.; Tiwary, Shivani; Cox, Jurgen; Prakash, Amol; Halushka, Marc K.; Burns, Kathleen H.; Kandasamy, Richard k; Pandey, Akhilesh
Abstract: Molecular profiling of human primary cell types is essential for understanding human biology. We present a transcriptome and proteome map of 28 primary human cell types. Three major clusters of epithelial, endothelial, and mesenchymal cell types were observed in both the transcriptome and proteome levels along with the discovery of cell type enriched molecules including GRAP and C1orf116. The epithelial cell specific protein C1orf116 was further validated using immunohistochemistry across various human tissues. An exhaustive protein database search considering 39 post-translational modifications (PTMs) revealed novel insights into the PTM landscape including identification of understudied PTMs such as serine O-acetylation and histidine methylation. This also enabled comprehensive characterization of proteins with diverse PTMs. Interestingly, an unexpectedly higher frequency of dioxidation on tryptophan compared to methionine led to the identification of oxidative mitochondria complex subunit proteins. Further, a search strategy accounting for alternative translational start sites, splice junctions and translational readthrough refined genome annotation using proteomic evidence. For example, peptides from translational readthrough including extended sequence of LDHB and MDH1 were detected representing the first peptide-level evidence of these protein readthrough isoforms. Our comprehensive transcriptome and proteome data revealed cell type-specific molecular cues and heterogeneity, offering new insights into disease mechanisms often overlooked by tissue proteomics.</summary>
    <dc:date>2025-12-31T15:00:00Z</dc:date>
  </entry>
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