Li Na Zhao

Lund University

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G.T. Montelione

Rensselaer Polytechnic Institute

Philipp Kaldis

Lund University

T.B. Acton

Ollscoil na Gaillimhe – University of Galway

Yuguang Mu

Nanyang Technological University

Lock Yue Chew

Nanyang Technological University

J.F. Hunt

Columbia University

K. Cunningham

Vanderbilt University

J. Seetharaman

St. Jude Children's Research Hospital

Rong Xiao

Huazhong Agricultural University

Burkhard Rost

Technical University of Munich

Cooperative Institutions

Agency for Science, Technology and Research

Chinese Academy of Medical Sciences & Peking Union Medical College

Rutgers, The State University of New Jersey

National University of Singapore

Chinese Academy of Sciences

Capital Medical University

North China Electric Power University

Joint Center for Structural Genomics

Structural Genomics Consortium

Sichuan University

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Research progress on mechanisms of organ protection by Ulinastatin

Chin J Crit Care Intensive Care Med (2019)

Li Na Zhao

Ulinastatin is a commonly used drug to treat patients with critical illness. This review systematically described the protective effects of Ulinastatin on human organs and the underlying mechanisms, such as antiinflammatory, antioxidation, immune regulation and antiapoptosis, in order to provide evidence for the rational application of Ulinastatin. Key words: Ulinastatin; Organ Protection; Acute inflammatory disease

Ulinastatin

10.3877/cma.j.issn.2096-1537.2019.03.013

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NMR solution structure of peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato. Northeast Structural Genomics Consortium target PsR211

Journal of Back and Musculoskeletal Rehabilitation (2007)

Kiran Kumar Singarapu Dinesh K. Sukumaran D. Parish Alexander Eletsky Q. Zhang

Pseudomonas syringae

Structural genomics

10.2210/pdb2jva/pdb

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Solution NMR structure of the folded N-terminal fragment of UPF0291 protein ynzCfrom Bacillus subtilis. Northeast Structural Genomics target SR384-1-46.

Journal of Back and Musculoskeletal Rehabilitation (2007)

James M. Aramini Seema Sharma Yuanpeng J. Huang Li Na Zhao L. Owens

Structural genomics

Fragment (logic)

10.13018/bmr15476

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Proof-of-Concept Method to Study Uncharacterized Methyltransferases Using PRDM15

International Journal of Molecular Sciences (2023)

Li Na Zhao Ernesto Guccione Philipp Kaldis

The PRDM family of methyltransferases has been implicated in cellular proliferation and differentiation and is deregulated in human diseases, most notably in cancer. PRDMs are related to the SET domain family of methyltransferases; however, from the 19 PRDMs only a few PRDMs with defined enzymatic activities are known. PRDM15 is an uncharacterized transcriptional regulator, with significant structural disorder and lack of defined small-molecule binding pockets. Many aspects of PRDM15 are yet unknown, including its structure, substrates, reaction mechanism, and its methylation profile. Here, we employ a series of computational approaches for an exploratory investigation of its potential substrates and reaction mechanism. Using the knowledge of PRDM9 and current knowledge of PRDM15 as basis, we tried to identify genuine substrates of PRDM15. We start from histone-based peptides and learn that the native substrates of PRDM15 may be non-histone proteins. In the future, a combination of sequence-based approaches and signature motif analysis may provide new leads. In summary, our results provide new information about the uncharacterized methyltransferase, PRDM15.

Histone Methylation

Sequence motif

10.3390/ijms24021327

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The cardiovascular effects of YIGSR and RGD containing peptides

Kluwer Academic Publishers eBooks (2005)

Chen Zilin Li-Ping Tu Karl Specht Li Na Zhao Ming Zhao

10.1007/0-306-46859-x_68

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NMR CHEMICAL SHIFT ASSIGNMENTS OF PUTATIVE UNCHARACTERIZED PROTEIN. FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET GsR195

Journal of Back and Musculoskeletal Rehabilitation (2008)

Gaohua Liu Li Na Zhao Colleen Ciccosanti Mei Jiang Rong Xiao

Structural genomics

10.13018/bmr15833

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X-ray Crystal Structure of Protein AGR_C_3712 from Agrobacterium tumefaciens. Northeast Structural Genomics Consortium Target AtR88.

S.M. Vorobiev M. Abashidze J. Seetharaman Li Na Zhao Lingling Ma

Structural genomics

10.2210/pdb2nys/pdb

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GC-MS Analysis of Fat-Soluble Components of Wild Russula in Fangcheng Area of Henan Province

Materials science forum (2020)

Li Na Zhao Yi Shuo Wang Yu Han Sarah Bacus

Objective: To study the lipid soluble constituents of wild Russula in Fangcheng-Henan province. Methods: The lipid soluble chemical constituents of wild Russula in henan province were analyzed by GC-MS. Results: The Fatty acids was the highest content of lipid soluble components in wild Russula, 27 compounds were identified, accounting for 99.44% of the total detected components, the main compounds were (E)- 9-octadecenoic acid (44.93%), linoleic acid (28.18%), Palmitic acid (12.07%) and (E)- 12,15-octadecenoic acid (4.17%). Conclusion: The study provides experimental datas for the further development and utilization of wild Russula.

Russula

10.4028/www.scientific.net/msf.980.171

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Cascading proton transfers are a hallmark of the catalytic mechanism of SAM‐dependent methyltransferases

FEBS Letters (2020)

Li Na Zhao Philipp Kaldis

The S-adenosyl methionine (SAM)-dependent methyltransferases attach a methyl group to the deprotonated methyl lysine using SAM as a donor. An intriguing, yet unanswered, question is how the deprotonation takes place. PRDM9 with well-defined enzyme activity is a good representative of the methyltransferase family to study the deprotonation and subsequently the methyl transfer. Our study has found that the pKa of Tyr357 is low enough to make it an ideal candidate for proton abstraction from the methyl lysine. The partially deprontonated Tyr357 is able to change its H-bond pattern thus bridging two proton tunneling states and providing a cascading proton transfer. We have uncovered a new catalytic mechanism for the deprotonation of the methyl lysine in methyltransferases.

Methyl group

10.1002/1873-3468.13799

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The Toxicity of Amyloid ß Oligomers

International Journal of Molecular Sciences (2012)

Li Na Zhao Hon Wai Long Yuguang Mu Lock Yue Chew

Abstract: In this review, we elucidate the mechanisms of Aβ oligomer toxicity which may contribute to Alzheimer’s disease (AD). In particular, we discuss on the interaction of Aβ oligomers with the membrane through the process of adsorption and insertion. Such interaction gives rises to phase transitions in the sub-structures of the Aβ peptide from α-helical to β-sheet structure. By means of a coarse-grained model, we exhibit the tendency of β-sheet structures to aggregate, thus providing further insights to the process of membrane induced aggregation. We show that the aggregated oligomer causes membrane invagination, which is a precursor to the formation of pore structures and ion channels. Other pathological progressions to AD due to Aβ oligomers are also covered, such as their interaction with the membrane receptors, and their direct versus indirect effects on oxidative stress and intraneuronal accumulation. We further illustrate that the molecule curcumin is a potential Aβ toxicity inhibitor as a β-sheet breaker by having a high propensity to interact with certain Aβ residues without binding to them. The comprehensive understanding gained from these current researches on the various toxicity mechanisms show promises in the provision of better therapeutics and treatment strategies in the near future.

Amyloid (mycology)

10.3390/ijms13067303

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Citations (135)