scholarly journals Dimerization of conserved ascaroside building blocks generates species-specific male attractants in Caenorhabditis nematodes

2020 ◽  
Vol 18 (27) ◽  
pp. 5253-5263 ◽  
Author(s):  
Chuanfu Dong ◽  
Franziska Dolke ◽  
Siva Bandi ◽  
Christian Paetz ◽  
Stephan H. von Reuß
Keyword(s):  
Building Blocks ◽  
Esi Ms ◽  
Species Specific ◽  
Precursor Ion Scanning

Comparative ascaroside profiling of Caenorhabditis nematodes using HPLC-ESI-(−)-MS/MS precursor ion scanning revealed a class of highly species-specific ascaroside dimers.

Morphogenetic Events in Normal and Synchronously Dividing Tetrahymena

Development ◽  
1959 ◽  
Vol 7 (2) ◽  
pp. 241-256
Author(s):  
Norman E. Williams ◽  
Otto H. Scherbaum
Keyword(s):  
Daughter Cell ◽  
Tetrahymena Pyriformis ◽  
Building Blocks ◽  
Specific Pattern ◽  
Central Position ◽  
Parent Cell ◽  
Ciliated Protozoan ◽  
Mass Cultures ◽  
Synchronous Cell ◽  
Species Specific

Synchronous cell-division has been induced in mass cultures of the small ciliated protozoan Tetrahymena pyriformis (Scherbaum & Zeuthen, 1954). While it is known that cells grow in a characteristic way during the synchronizing treatment the effect on the morphogenetic events associated with the cell cycle is not clear. Studies in ciliate morphogenesis generally have established the central position of the ciliary basal body, or kinetosome, in developmental processes. The kinetosomes are believed to be self-duplicating structures, the kinetosomal population of a daughter cell arising directly by kinetosomal reproduction in the parent cell. The species-specific pattern of the ectoplasmic cortex is largely a matter of the distribution of kinetosomes. Further, the kinetosomes appear to function either as building blocks or ‘local organizers’ in most, if not all, structural syntheses occurring in the cortex, i.e. in the production cilia, cirri, membranelles, trichocysts, and other ciliate structures (see Weisz, 1954).

scholarly journals Network oscillation rules imposed by species-specific electrical coupling

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Stefanos Stagkourakis ◽  
Carolina Thörn Pérez ◽  
Arash Hellysaz ◽  
Rachida Ammari ◽  
Christian Broberger
Keyword(s):  
Species Difference ◽  
Electrical Coupling ◽  
Building Blocks ◽  
Network Building ◽  
Resonance Frequencies ◽  
Junction Coupling ◽  
Species Specific ◽  
Cell To Cell Variability ◽  
Operational Modes ◽  
Ensemble Activity

Electrical junctions are widespread within the mammalian CNS. Yet, their role in organizing neuronal ensemble activity remains incompletely understood. Here, in a functionally well-characterized system – neuroendocrine tuberoinfundibular dopamine (TIDA) neurons - we demonstrate a striking species difference in network behavior: rat TIDA cells discharge in highly stereotyped, robust, synchronized slow oscillations, whereas mouse oscillations are faster, flexible and show substantial cell-to-cell variability. We show that these distinct operational modes are explained by the presence of strong TIDA-TIDA gap junction coupling in the rat, and its complete absence in the mouse. Both species, however, encompass a similar heterogeneous range of intrinsic resonance frequencies, suggesting similar network building blocks. We demonstrate that gap junctions select and impose the slow network rhythm. These data identify a role for electrical junctions in determining oscillation frequency and show how related species can rely on distinct network strategies to accomplish adaptive control of hormone release.

scholarly journals Species-Specific Receptor Recognition by a Minor-Group Human Rhinovirus (HRV): HRV Serotype 1A Distinguishes between the Murine and the Human Low-Density Lipoprotein Receptor

2002 ◽  
Vol 76 (14) ◽  
pp. 6957-6965 ◽  
Author(s):  
Manuela Reithmayer ◽  
Andrea Reischl ◽  
Luc Snyers ◽  
Dieter Blaas
Keyword(s):  
Sequence Similarity ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Building Blocks ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor ◽  
Species Specific ◽  
A Minor

ABSTRACT Human rhinoviruses (HRV) of the minor receptor group use several members of the low-density lipoprotein receptor superfamily for cell entry. These proteins are evolutionarily highly conserved throughout species and are almost ubiquitously expressed. Their common building blocks, cysteine-rich ligand binding repeats about 40 amino acids in length, exhibit considerable sequence similarity. Various numbers of these repeats are present in the different receptors. We here demonstrate that HRV type 1A (HRV1A) replicates in mouse cells without adaptation. Furthermore, although closely related to HRV2, it fails to bind to the human low-density lipoprotein receptor but recognizes the murine protein, whereas HRV2 binds equally well to both homologues. This difference went unnoticed due to the presence of other receptors, such as the low-density lipoprotein receptor-related protein, which allow species-independent attachment. The species specificity of HRV1A reported here will aid in defining amino acid residues establishing the contact between the viral surface and the receptor.

New insight on the structural diversity of holothurian fucosylated chondroitin sulfates

2019 ◽  
Vol 91 (7) ◽  
pp. 1065-1071 ◽  
Author(s):  
Nadezhda E. Ustyuzhanina ◽  
Maria I. Bilan ◽  
Nikolay E. Nifantiev ◽  
Anatolii I. Usov
Keyword(s):  
Biological Effect ◽  
Wide Spectrum ◽  
Structural Diversity ◽  
Building Blocks ◽  
Structural Features ◽  
Biological Properties ◽  
Structural Variations ◽  
Chondroitin Sulfates ◽  
Nmr Data ◽  
Species Specific

AbstractFucosylated chondroitin sulfates (FCS) are unique glycosaminoglycans isolated from body walls of sea cucumbers (holothuria). These biopolymers are composed of a chondroitin core [→4)-β-D-GlcA-(1→3)-β-D-GalNAc-(1→]nbearing fucosyl branches and sulfate groups. Structural variations of FCS are species specific and depend on type, amount and position of branches, as well as on degree and pattern of sulfation of a backbone and branches. A wide spectrum of biological properties was determined for these polysaccharides including anticoagulant, antithrombotic, antitumor, anti-inflammatory activities. Structural features of FCS influence significantly on their biological effect. In this review recent data about structural variations within holothurian FCS are summarized. The NMR data of the key building blocks are presented, which may be used for the analysis of new FCS.

Morita–Baylis–Hillman adducts as building blocks of heterocycles: a simple approach to 4-substituted pyrazolones, and mechanism investigation via ESI–MS(/MS)

2015 ◽  
Vol 146 (9) ◽  
pp. 1557-1570 ◽  
Author(s):  
Rosimeire C. Barcelos ◽  
Lucas A. Zeoly ◽  
Manoel T. Rodrigues ◽  
Bruno R. V. Ferreira ◽  
Marcos N. Eberlin ◽  
...  
Keyword(s):  
Building Blocks ◽  
Simple Approach ◽  
Esi Ms

scholarly journals Design and Synthesis of Crown Ether Functionalized Imidazoles as a New type of Building Blocks

2012 ◽  
Vol 9 (4) ◽  
pp. 2128-2133
Author(s):  
Sheng-Hui Li ◽  
Jing Xia
Keyword(s):  
Crown Ether ◽  
Elemental Analysis ◽  
Building Blocks ◽  
Efficient Synthesis ◽  
Esi Ms ◽  
Design And Synthesis ◽  
H Nmr ◽  
New Type

A simple, convenient and efficient synthesis for a series of crown ether functionalized imidazoles from benzo-15-crown-5 (B15C5), benzo-18-crown-6 (B18C6), imidazole (Im), 2-methylimidazole (mIm), benzimidazole (bIm) and 2-methyl benzimidazole (mbIm) is reported. All these compounds obtained were characterized by IR,1H NMR, ESI-MS and elemental analysis.

ChemInform Abstract: Morita-Baylis-Hillman Adducts as Building Blocks of Heterocycles: A Simple Approach to 4-Substituted Pyrazolones, and Mechanism Investigation via ESI-MS(/MS).

ChemInform ◽  
2015 ◽  
Vol 46 (52) ◽  
pp. no-no
Author(s):  
Rosimeire C. Barcelos ◽  
Lucas A. Zeoly ◽  
Manoel T. Jr. Rodrigues ◽  
Bruno R. V. Ferreira ◽  
Marcos N. Eberlin ◽  
...  
Keyword(s):  
Building Blocks ◽  
Simple Approach ◽  
Esi Ms

scholarly journals The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

2019 ◽  
Author(s):  
Ahmad Khalifa ◽  
Muneyoshi Ichikawa ◽  
Daniel Dai ◽  
Shintaroh Kubo ◽  
Corbin Black ◽  
...  
Keyword(s):  
Building Blocks ◽  
Post Translational Modifications ◽  
Ciliary Beating ◽  
Structural Support ◽  
Cryo Electron Microscopy ◽  
The Common ◽  
Species Specific ◽  
And Function ◽  
Standing Question ◽  
Junction Proteins

AbstractMicrotubules are cytoskeletal structures involved in structural support, microtubule-based transport and the organization of organelles in the cells. The building blocks of the microtubule, the α- and β-tubulin heterodimers, polymerize into protofilaments, that associate laterally to form the hollow microtubule. There exists a specific type of microtubule structures in the cilia, termed doublet microtubules, where high stability is required for ciliary beating and function. The doublet microtubule, consisting of a complete A-tubule and a partial B-tubule maintains its stability through unique interactions at its outer and inner junctions, where the A- and B-tubules meet.Using cryo-electron microscopy, we present the answer to the long-standing question regarding the identities, localizations and structures of the Chlamydomonas doublet microtubule inner junction proteins. Using a combination of sequence bioinformatics and mass spectrometry, we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction associated protein FAP126. We show that inner junction proteins PACRG and FAP20, together with FAP52, previously unidentified FAP276, FAP106 and FAP126, form an interaction hub at the inner junction, which involves tubulin sites for post-translational modifications. We further compare the Chlamydomonas and Tetrahymena doublet microtubule structures to understand the common and species-specific features of the inner junction.

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