Hideharu Yukitake
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Hideharu Yukitake has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
- Mariko Naito
Department of Microbiology and Oral Infection, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan
2 shared publications - Benjamin Peng
Cooperative Research Centre for Oral Health Science, Melbourne Dental School, University of Melbourne, Victoria, Australia
1 shared publication - Eric Charles Reynolds
Oral Health Cooperative Research Centre, Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Australia
1 shared publication - Fumi Seto-Tetsuo
Division of Microbiology, Oral Infection, Department of Molecular Microbiology and Immunity, Nagasaki University Graduate School of Biomedical Sciences, Sakamoto 1-7-1, Nagasaki, Nagasaki, 852-8588, Japan
1 shared publication - Keiko Sato
Department of Frontier Oral Science, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan
1 shared publication - Koji Nakayama
Department of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan
1 shared publication
Latest Publications
- 31 January 2026
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 805, 153304
Supernatants from DNase-deficient Prevotella intermedia strains enhance oral squamous cell carcinoma cell migration and invasion by activating inflammatory and epithelial–mesenchymal transition pathways
- 31 January 2026
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 805, 153304
Supernatants from DNase-deficient Prevotella intermedia strains enhance oral squamous cell carcinoma cell migration and invasion by activating inflammatory and epithelial–mesenchymal transition pathways
- Open Access
- 25 May 2010
- Published by Springer Nature in BMC Microbiology
- Vol. 10 (1) , 152
Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization
Background: The periodontal pathogen Porphyromonas gingivalis is an obligate anaerobe that requires heme for growth. To understand its heme acquisition mechanism, we focused on a hemin-binding protein (HBP35 protein), possessing one thioredoxin-like motif and a conserved C-terminal domain, which are proposed to be involved in redox regulation and cell surface attachment, respectively. Results: We observed that the hbp35 gene was transcribed as a 1.1-kb mRNA with subsequent translation resulting in three proteins with molecular masses of 40, 29 and 27 kDa in the cytoplasm, and one modified form of the 40-kDa protein on the cell surface. A recombinant 40-kDa HBP35 exhibited thioredoxin activity in vitro and mutation of the two putative active site cysteine residues abolished this activity. Both recombinant 40- and 27-kDa proteins had the ability to bind hemin, and growth of an hbp35 deletion mutant was substantially retarded under hemin-depleted conditions compared with growth of the wild type under the same conditions. Conclusion: P. gingivalis HBP35 exhibits thioredoxin and hemin-binding activities and is essential for growth in hemin-depleted conditions suggesting that the protein plays a significant role in hemin acquisition.
- 25 May 2010
- Published by Springer Nature in BMC Microbiology
- Vol. 10 (1) , 152
Open AccessCharacterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization
Background: The periodontal pathogen Porphyromonas gingivalis is an obligate anaerobe that requires heme for growth. To understand its heme acquisition mechanism, we focused on a hemin-binding protein (HBP35 protein), possessing one thioredoxin-like motif and a conserved C-terminal domain, which are proposed to be involved in redox regulation and cell surface attachment, respectively. Results: We observed that the hbp35 gene was transcribed as a 1.1-kb mRNA with subsequent translation resulting in three proteins with molecular masses of 40, 29 and 27 kDa in the cytoplasm, and one modified form of the 40-kDa protein on the cell surface. A recombinant 40-kDa HBP35 exhibited thioredoxin activity in vitro and mutation of the two putative active site cysteine residues abolished this activity. Both recombinant 40- and 27-kDa proteins had the ability to bind hemin, and growth of an hbp35 deletion mutant was substantially retarded under hemin-depleted conditions compared with growth of the wild type under the same conditions. Conclusion: P. gingivalis HBP35 exhibits thioredoxin and hemin-binding activities and is essential for growth in hemin-depleted conditions suggesting that the protein plays a significant role in hemin acquisition.