Article
Biochemistry & Molecular Biology
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li
Summary: Protein ubiquitination is crucial for controlling protein degradation and cell signaling pathways. This study elucidated the crystal structure of TRIM75, a member of the RING E3 ligase family, revealing its tetrameric structure and function.
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL
(2022)
Article
Biology
Zahra Bahrami Dizicheh, I-Ling Chen, Patrick Koenig
Summary: By analyzing variable domain structures from llamas and alpacas, it was found that VHHs can be classified into two large structural clusters based on their CDR-H3 conformation. Extended CDR-H3 loops protrude into the solvent, while kinked CDR-H3 loops fold back onto framework regions. The CDR-H3 conformation of VHHs correlates with the germline from which the antibodies are derived.
COMMUNICATIONS BIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Andrey M. Grishin, Nataliya V. Dolgova, Shelby Landreth, Olivier Fisette, Ingrid J. Pickering, Graham N. George, Darryl Falzarano, Miroslaw Cygler
Summary: The study found that the disulfide bonds of the SARSCoV-2 Spike receptor-binding domain (RBD) play a crucial role in cell receptor binding and viral internalization. Reduction of the four disulfide bonds in the RBD increases flexibility of surface loops, affecting its binding affinity to the ACE2 cell receptor and viral replication.
JOURNAL OF MOLECULAR BIOLOGY
(2022)
Article
Biology
Martin A. Rossotti, Henk van Faassen, Anh T. Tran, Joey Sheff, Jagdeep K. Sandhu, Diana Duque, Melissa Hewitt, Xiaoxue Wen, Jegarubee Bavananthasivam, Saina Beitari, Kevin Matte, Genevieve Laroche, Patrick M. Giguere, Christian Gervais, Matthew Stuible, Julie Guimond, Sylvie Perret, Greg Hussack, Marc-Andre Langlois, Yves Durocher, Jamshid Tanha
Summary: This study presents a diverse collection of extensively characterized nanobodies targeting the spike glycoprotein of SARS-CoV-2. These nanobodies show broad neutralization efficacies against SARS-CoV-2 in vitro and in vivo, reducing viral burden by up to six orders of magnitude. They have high affinity, stability, and cross-reactivity, making them promising candidates for developing broad-spectrum therapeutics against current and emerging SARS-CoV-2 variants.
COMMUNICATIONS BIOLOGY
(2022)
Article
Chemistry, Organic
Jatuporn Meesin, Nawasit Chotsaeng, Chutima Kuhakarn
Summary: A novel dimerization of 3-chlorooxindoles promoted by potassium ethylxanthate was described to access isoindigo derivatives, with the reactions proceeding readily at room temperature in short reaction times. Mechanistic studies revealed the conversion of 3-chlorooxindole into O-ethyl S-(2-oxo-2,3-dihydro-1H-indol-3-yl) dithiocarbonate, followed by dimerization with the elimination of carbon disulfide to yield analytically pure isoindigos in moderate to good yields, without the need for chromatographic purification.
Article
Biochemistry & Molecular Biology
Kosuke Oyama, Makoto Nakakido, Takatoshi Ohkuri, Hitomi Nakamura, Kouhei Tsumoto, Tadashi Ueda
Summary: Researchers successfully created a new mutant, mut10, of the CH2 domain by introducing a disulfide bond, followed by a more advanced mutant, mut25, by combining mut10 and mut20. Mut25 exhibited enhanced thermal stability, increased resistance to enzymatic digestion, and reduced aggregation compared to the original CH2 domain and mut20. It is the most stable variant of the humanized whole CH2 domains reported so far, and has the potential to serve as a new platform for antibody therapeutics due to its ability to reduce immunogenicity by decreasing aggregation.
Article
Biochemistry & Molecular Biology
Ajit Kumar Singh, Ketul Saharan, Somanath Baral, Sheng Luan, Dileep Vasudevan
Summary: Chemically induced dimerization is a method used to regulate cellular processes by inducing close proximity between proteins. The heterodimerization induced by rapamycin and FK506 is commonly used to study dynamic cellular processes. The crystal structure of the AtFKBP53 FKBD in complex with rapamycin reveals that rapamycin can mediate homodimerization of FKBD, providing insights for the design of chemically induced dimerization systems.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Multidisciplinary Sciences
Yusuke Tomimoto, Rika Yamazaki, Hiroki Shirai
Summary: In this study, a computational method was used to design mutants with improved melting temperature (Tm) by calculating the free energy score. The results showed that this method significantly increased the Tm of single mutants while almost maintaining the affinity for the antigen. However, achieving both higher Tm and preserved affinity is extremely difficult, and it is recommended to use multiple approaches when designing antibody mutants.
SCIENTIFIC REPORTS
(2023)
Article
Chemistry, Multidisciplinary
Yizhou Wang, Xiangming Xu, Jian Yin, Gang Huang, Tianchao Guo, Zhengnan Tian, Rajeh Alsaadi, Yunpei Zhu, Husam N. Alshareef
Summary: In this study, large-area, mono-orientated 2D material (MoS2) is used for the first time to electrodeposit truly epitaxial Zn anodes. The continuous MoS2 films are shown to be an effective strategy for suppressing metal dendrites.
ADVANCED MATERIALS
(2023)
Article
Oncology
Mary E. Law, Elham Yaaghubi, Amanda F. Ghilardi, Bradley J. Davis, Renan B. Ferreira, Jin Koh, Sixue Chen, Sadie F. DePeter, Christopher M. Schilson, Chi-Wu Chiang, Coy D. Heldermon, Peter Norgaard, Ronald K. Castellano, Brian K. Law
Summary: Breast cancer mortality remains high, and there is a need for safer and more effective treatments. Disulfide bond Disrupting Agents (DDAs) have been identified as a potential class of anticancer compounds that specifically target EGFR and HER2 overexpressing cancer cells. The study found that DDAs act by downregulating EGFR, HER2, and HER3 and activating Death Receptors 4 and 5 (DR4/5). Further analysis revealed that AGR2, PDIA1, and ERp44 are the target proteins of DDAs. DDAs disrupt the mixed disulfide bonds between PDIA1, ERp44, and their client proteins, and enhance basal DR5 oligomerization by targeting AGR2 and ERp44.
Article
Chemistry, Applied
Jinjin Zhao, Danli Wang, Lifang Zhang, Xijun Lian
Summary: Strength and stiffness are important characteristics of high-quality dough products. This study explores the formation of disulfide bonds in alkali-soluble glutenin (ASG), which plays a key role in imparting these properties to noodles. The interaction between ASG and co-crystallized wheat amylopectin with NaCl is found to significantly increase the disulfide bond content of ASG. Furthermore, it is discovered that co-crystallized wheat amylopectin with NaCl can serve as a reinforcing agent for wheat flour.
FOOD HYDROCOLLOIDS
(2024)
Article
Biochemistry & Molecular Biology
Il-Sup Kim, Woong Choi, Ae Kyung Park, Hyun Kim, Jonghyeon Son, Jun Hyuck Lee, Seung Chul Shin, T. Doohun Kim, Han-Woo Kim
Summary: The CaDHN gene from the Arctic mouse-ear chickweed contains an unusual single cysteine residue that can form intermolecular disulfide bonds, enhancing the plant's tolerance to abiotic stress by regulating protein dimerization.
Article
Cell Biology
Gang Du, Linlin Zhao, Yumei Zheng, Anissa Belfetmi, Tiantian Cai, Boying Xu, Karen Heyninck, Kim Van Den Heede, Marie-Ange Buyse, Pietro Fontana, Michael Bowman, Lih-Ling Lin, Hao Wu, James Jeiwen Chou
Summary: Members of the TNFRSF can be activated to induce death of cancer cells or stimulate proliferation of immune cells. The self-association structure of the ectodomain of DR5-ECD, a representative member of TNFRSF, has been determined by NMR. The preligand association of DR5 serves an autoinhibitory role and disruption of the preligand cluster can enhance receptor signaling. This mechanism provides a new opportunity for developing agonistic molecules by targeting receptor preligand clustering.
Article
Multidisciplinary Sciences
Yuan Ren, Jie Yang, Barbara Fujita, Huaizhou Jin, Yongli Zhang, Julien Berro
Summary: Forces play important roles in various cellular processes, but it is challenging to measure them at the molecular scale in vivo. In this study, new in vivo force sensors were used to measure the forces on the protein End4p at different locations, revealing their redistribution across the endocytic machinery.
Article
Biochemistry & Molecular Biology
Anna M. Banas, Katarzyna M. Bocian-Ostrzycka, Stanislaw Dunin-Horkawicz, Jan Ludwiczak, Piotr Wilk, Marta Orlikowska, Agnieszka Wyszynska, Maria Dabrowska, Maciej Plichta, Marta Spodzieja, Marta A. Polanska, Agata Malinowska, Elzbieta Katarzyna Jagusztyn-Krynicka
Summary: The bacterial Dsb proteins catalyze the formation of disulfide bridges between cysteine residues, stabilizing protein structures. Campylobacter jejuni's oxidizing Dsb system consists of two monomeric DsbAs and one dimeric bifunctional protein. The two monomeric DsbAs in C. jejuni are dispensable proteins, with homologous structures to EcDsbL. Comparative proteomics showed that the Dsb system targets several respiratory and periplasmic transport proteins, essential for the bacterium's respiratory process in oxygen-limiting conditions. The detailed analysis provides insights into potential antibacterial targets.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Sunghark Kwon, Hyun H. Park
Article
Biochemical Research Methods
Sunghwan Kim, Hyun Ho Park
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
(2019)
Article
Crystallography
Chang Min Kim, Sunghark Kwon, Kyung Ho Jung, Hye Lin Chun, Hyun Ji Ha, Hyun Ho Park
Article
Biochemistry & Molecular Biology
Sunghark Kwon, Chang Woo Lee, Hye Yeon Koh, Hyun Park, Jun Hyuck Lee, Hyun Ho Park
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2020)
Review
Biochemistry & Molecular Biology
Hyun Ho Park
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2019)
Review
Biochemistry & Molecular Biology
Hyun Ji Ha, Hye Lin Chun, Hyun Ho Park
EXPERIMENTAL AND MOLECULAR MEDICINE
(2020)
Article
Biochemistry & Molecular Biology
Eui Man Jeong, Ki Baek Lee, Gi Eob Kim, Chang Min Kim, Jin-Haeng Lee, Hyo-Jun Kim, Ji-Woong Shin, Mee-ae Kwon, Hyun Ho Park, In-Gyu Kim
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2020)
Review
Biochemistry & Molecular Biology
Gi Eob Kim, Hyun Ho Park
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2020)
Article
Biochemistry & Molecular Biology
Chang Min Kim, Hyun Ho Park
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2020)
Article
Microbiology
Jisub Hwang, Chang-Sook Jeong, Chang Woo Lee, Seung Chul Shin, Han-Woo Kim, Sung Gu Lee, Ui Joung Youn, Chang Sup Lee, Tae-Jin Oh, Hak Jun Kim, Hyun Park, Hyun Ho Park, Jun Hyuck Lee
JOURNAL OF MICROBIOLOGY
(2020)
Article
Biochemistry & Molecular Biology
Hyun Ji Ha, Hyun Ho Park
Article
Fisheries
Chang Min Kim, Hyunseok Jang, Hyun Ji Ha, Gi Eob Kim, Hyun Ho Park
FISH & SHELLFISH IMMUNOLOGY
(2020)
Article
Multidisciplinary Sciences
Hye Lin Chun, So Yeon Lee, Sung Hoon Lee, Chang Sup Lee, Hyun Ho Park
SCIENTIFIC REPORTS
(2020)
Review
Biochemistry & Molecular Biology
Seong Ah Shin, Byeong Jun Joo, Jun Seob Lee, Gyoungah Ryu, Minjoo Han, Woe Yeon Kim, Hyun Ho Park, Jun Hyuck Lee, Chang Sup Lee
Article
Crystallography
Hyun Ho Park
Summary: IRG1 is an enzyme that is overexpressed during immune reactions and catalyzes the production of itaconate, which has antibacterial and antiviral activities. The exact mechanism of IRG1 enzymatic reaction remains unclear, but structural studies are expected to shed light on it.
