TY  - JOUR
A1  - Smith, Sarah R.
A1  - Dupont, Chris L.
A1  - McCarthy, James K.
A1  - Broddrick, Jared T.
A1  - Obornik, Miroslav
A1  - Horak, Ales
A1  - Füssy, Zoltán
A1  - Cihlar, Jaromir
A1  - Kleessen, Sabrina
A1  - Zheng, Hong
A1  - McCrow, John P.
A1  - Hixson, Kim K.
A1  - Araujo, Wagner L.
A1  - Nunes-Nesi, Adriano
A1  - Fernie, Alisdair R.
A1  - Nikoloski, Zoran
A1  - Palsson, Bernhard O.
A1  - Allen, Andrew E.
T1  - Evolution and regulation of nitrogen flux through compartmentalized metabolic networks in a marine diatom
JF  - Nature Communications
N2  - Diatoms outcompete other phytoplankton for nitrate, yet little is known about the mechanisms underpinning this ability. Genomes and genome-enabled studies have shown that diatoms possess unique features of nitrogen metabolism however, the implications for nutrient utilization and growth are poorly understood. Using a combination of transcriptomics, proteomics, metabolomics, fluxomics, and flux balance analysis to examine short-term shifts in nitrogen utilization in the model pennate diatom in Phaeodactylum tricornutum, we obtained a systems-level understanding of assimilation and intracellular distribution of nitrogen. Chloroplasts and mitochondria are energetically integrated at the critical intersection of carbon and nitrogen metabolism in diatoms. Pathways involved in this integration are organelle-localized GS-GOGAT cycles, aspartate and alanine systems for amino moiety exchange, and a split-organelle arginine biosynthesis pathway that clarifies the role of the diatom urea cycle. This unique configuration allows diatoms to efficiently adjust to changing nitrogen status, conferring an ecological advantage over other phytoplankton taxa.
KW  - Biochemistry
KW  - Computational biology and bioinformatics
KW  - Evolution
KW  - Microbiology
KW  - Molecular biology
Y1  - 2019
U6  - https://doi.org/10.1038/s41467-019-12407-y
SN  - 2041-1723
VL  - 10
PB  - Nature Publ. Group
CY  - London
ER  - 
TY  - JOUR
A1  - Tian, Guang-Zong
A1  - Hu, Jing
A1  - Zhang, Heng-Xi
A1  - Rademacher, Christoph
A1  - Zou, Xiao-Peng
A1  - Zheng, Hong-Ning
A1  - Xu, Fei
A1  - Wang, Xiao-Li
A1  - Linker, Torsten
A1  - Yin, Jian
T1  - Synthesis and conformational analysis of linear homo- and heterooligomers from novel 2-C-branched sugar amino acids (SAAs)
JF  - Scientific reports
N2  - Sugar amino acids (SAAs), as biologically interesting structures bearing both amino and carboxylic acid functional groups represent an important class of multifunctional building blocks. In this study, we develop an easy access to novel SAAs in only three steps starting from nitro compounds in high yields in analytically pure form, easily available by ceric (IV) mediated radical additions. Such novel SAAs have been applied in the assembly of total nine carbopeptoids with the form of linear homo-and heterooligomers for the structural investigations employing circular dichroism (CD) spectroscopy, which suggest that the carbopeptoids emerge a well-extended, left (or right)-handed conformation similar to polyproline II (PPII) helices. NMR studies also clearly demonstrated the presence of ordered secondary structural elements. 2D-ROESY spectra were acquired to identify i+1NH <-> (C1H)-C-i, (C2H)-C-i correlations which support the conformational analysis of tetramers by CD spectroscopy. These findings provide interesting information of SAAs and their oligomers as potential scaffolds for discovering new drugs and materials.
Y1  - 2018
U6  - https://doi.org/10.1038/s41598-018-24927-6
SN  - 2045-2322
VL  - 8
PB  - Nature Publ. Group
CY  - London
ER  - 
TY  - JOUR
A1  - Yang, Guang
A1  - Zheng, Wei
A1  - Tao, Guoqing
A1  - Wu, Libin
A1  - Zhou, Qi-Feng
A1  - Kochovski, Zdravko
A1  - Ji, Tan
A1  - Chen, Huaijun
A1  - Li, Xiaopeng
A1  - Lu, Yan
A1  - Ding, Hong-ming
A1  - Yang, Hai-Bo
A1  - Chen, Guosong
A1  - Jiang, Ming
T1  - Diversiform and Transformable Glyco-Nanostructures Constructed from Amphiphilic Supramolecular Metallocarbohydrates through Hierarchical Self-Assembly: The Balance between Metallacycles and Saccharides
JF  - ACS nano
N2  - During the past decade, self-assembly of saccharide-containing amphiphilic molecules toward bioinspired functional glycomaterials has attracted continuous attention due to their various applications in fundamental and practical areas. However, it still remains a great challenge to prepare hierarchical glycoassemblies with controllable and diversiform structures because of the complexity of saccharide structures and carbohydrate-carbohydrate interactions. Herein, through hierarchical self-assembly of modulated amphiphilic supramolecular metallocarbohydrates, we successfully prepared various well-defined glyco-nanostructures in aqueous solution, including vesicles, solid spheres, and opened vesicles depending on the molecular structures of metallocarbohydrates. More attractively, these glyco-nanostructures can further transform into other morphological structures in aqueous solutions such as worm-like micelles, tubules, and even tupanvirus-like vesicles (TVVs). It is worth mentioning that distinctive anisotropic structures including the opened vesicles (OVs) and TVVs were rarely reported in glycobased nano-objects. This intriguing diversity was mainly controlled by the subtle structural trade-off of the two major components of the amphiphiles, i.e., the saccharides and metallacycles. To further understand this precise structural control, molecular simulations provided deep physical insights on the morphology evolution and balancing of the contributions from saccharides and metallacycles. Moreover, the multivalency of glyco-nanostructures with different shapes and sizes was demonstrated by agglutination with a diversity of sugarbinding protein receptors such as the plant lectins Concanavalin A (ConA). This modular synthesis strategy provides access to systematic tuning of molecular structure and self-assembled architecture, which undoubtedly will broaden our horizons on the controllable fabrication of biomimetic glycomaterials such as biological membranes and supramolecular lectin inhibitors.
KW  - glycomaterials
KW  - diversiform structures
KW  - hierarchical self-assembly
KW  - metallocarbohydrates
KW  - anisotropic structures
Y1  - 2019
U6  - https://doi.org/10.1021/acsnano.9b07134
SN  - 1936-0851
SN  - 1936-086X
VL  - 13
IS  - 11
SP  - 13474
EP  - 13485
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Tang, Alan T.
A1  - Sullivan, Katie Rose
A1  - Hong, Courtney C.
A1  - Goddard, Lauren M.
A1  - Mahadevan, Aparna
A1  - Ren, Aileen
A1  - Pardo, Heidy
A1  - Peiper, Amy
A1  - Griffin, Erin
A1  - Tanes, Ceylan
A1  - Mattei, Lisa M.
A1  - Yang, Jisheng
A1  - Li, Li
A1  - Mericko-Ishizuka, Patricia
A1  - Shen, Le
A1  - Hobson, Nicholas
A1  - Girard, Romuald
A1  - Lightle, Rhonda
A1  - Moore, Thomas
A1  - Shenkar, Robert
A1  - Polster, Sean P.
A1  - Roedel, Claudia Jasmin
A1  - Li, Ning
A1  - Zhu, Qin
A1  - Whitehead, Kevin J.
A1  - Zheng, Xiangjian
A1  - Akers, Amy
A1  - Morrison, Leslie
A1  - Kim, Helen
A1  - Bittinger, Kyle
A1  - Lengner, Christopher J.
A1  - Schwaninger, Markus
A1  - Velcich, Anna
A1  - Augenlicht, Leonard
A1  - Abdelilah-Seyfried, Salim
A1  - Min, Wang
A1  - Marchuk, Douglas A.
A1  - Awad, Issam A.
A1  - Kahn, Mark L.
T1  - Distinct cellular roles for PDCD10 define a gut-brain axis in cerebral cavernous malformation
JF  - Science Translational Medicine
N2  - Cerebral cavernous malformation (CCM) is a genetic, cerebrovascular disease. Familial CCM is caused by genetic mutations in KRIT1, CCM2, or PDCD10. Disease onset is earlier and more severe in individuals with PDCD10 mutations. Recent studies have shown that lesions arise from excess mitogen-activated protein kinase kinase kinase 3 (MEKK3) signaling downstream of Toll-like receptor 4 (TLR4) stimulation by lipopolysaccharide derived from the gut microbiome. These findings suggest a gut-brain CCM disease axis but fail to define it or explain the poor prognosis of patients with PDCD10 mutations. Here, we demonstrate that the gut barrier is a primary determinant of CCM disease course, independent of microbiome configuration, that explains the increased severity of CCM disease associated with PDCD10 deficiency. Chemical disruption of the gut barrier with dextran sulfate sodium augments CCM formation in a mouse model, as does genetic loss of Pdcd10, but not Krit1, in gut epithelial cells. Loss of gut epithelial Pdcd10 results in disruption of the colonic mucosal barrier. Accordingly, loss of Mucin-2 or exposure to dietary emulsifiers that reduce the mucus barrier increases CCM burden analogous to loss of Pdcd10 in the gut epithelium. Last, we show that treatment with dexamethasone potently inhibits CCM formation in mice because of the combined effect of action at both brain endothelial cells and gut epithelial cells. These studies define a gut-brain disease axis in an experimental model of CCM in which a single gene is required for two critical components: gut epithelial function and brain endothelial signaling.
Y1  - 2019
U6  - https://doi.org/10.1126/scitranslmed.aaw3521
SN  - 1946-6234
SN  - 1946-6242
VL  - 11
IS  - 520
PB  - American Assoc. for the Advancement of Science
CY  - Washington
ER  -