scholarly journals Functional Difference Between Deuterated and Protonated Macromolecules

10.5772/36649 ◽  
2012 ◽  
Author(s):  
Takashi Sugiyama ◽  
Tohru Yoshiok
Keyword(s):  
Functional Difference

scholarly journals Force Generation on the Hallux Is More Affected by the Ankle Joint Angle than the Lesser Toes: An In Vivo Human Study

Biology ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 48
Author(s):  
Junya Saeki ◽  
Soichiro Iwanuma ◽  
Suguru Torii
Keyword(s):  
Repeated Measures ◽  
Joint Angle ◽  
Plantar Flexion ◽  
Human Study ◽  
Force Generation ◽  
Functional Difference ◽  
Multiple Comparison Test ◽  
The Difference ◽  
Metatarsophalangeal Joints

The structure of the first toe is independent of that of the other toes, while the functional difference remains unclear. The purpose of this study was to investigate the difference in the force generation characteristics between the plantar-flexion of the first and second–fifth metatarsophalangeal joints (MTPJs) by comparing the maximal voluntary plantar-flexion torques (MVC torque) at different MTPJs and ankle positions. The MVC torques of the first and second–fifth MTPJs were measured at 0°, 15°, 30°, and 45° dorsiflexed positions of the MTPJs, and at 20° plantar-flexed, neutral, and 20° dorsiflexed positions of the ankle. Two-way repeated measures analyses of variance with Holm’s multiple comparison test (MTPJ position × ankle position) were performed. When the MTPJ was dorsiflexed at 0°, 15°, and 30°, the MVC torque of the first MTPJ when the ankle was dorsiflexed at 20° was higher than that when the ankle was plantar-flexed at 20°. However, the ankle position had no significant effect on the MVC torque of the second–fifth MTPJ. Thus, the MVC torque of the first MTPJ was more affected by the ankle position than the second–fifth MTPJs.

Convergent solutions of functional difference equations

1997 ◽  
Vol 3 (3-4) ◽  
pp. 277-288
Author(s):  
R. Medina ◽  
M. Pinto
Keyword(s):  
Difference Equations ◽  
Functional Difference ◽  
Functional Difference Equations

scholarly journals Human Dendritic Cells Mediate Cellular Apoptosis via Tumor Necrosis Factor–Related Apoptosis-Inducing Ligand (Trail)

1999 ◽  
Vol 190 (8) ◽  
pp. 1155-1164 ◽  
Author(s):  
Neil A. Fanger ◽  
Charles R. Maliszewski ◽  
Ken Schooley ◽  
Thomas S. Griffith
Keyword(s):  
Dendritic Cells ◽  
Tumor Cells ◽  
Cell Types ◽  
Target Cells ◽  
Functional Difference ◽  
Cellular Apoptosis ◽  
Soluble Trail ◽  
Innate Effector ◽  
Human Dendritic Cells ◽  
Necrosis Factor

TRAIL (TNF-related apoptosis-inducing ligand) is a member of the TNF family that induces apoptosis in a variety of cancer cells. In this study, we demonstrate that human CD11c+ blood dendritic cells (DCs) express TRAIL after stimulation with either interferon (IFN)-γ or -α and acquire the ability to kill TRAIL-sensitive tumor cell targets but not TRAIL-resistant tumor cells or normal cell types. The DC-mediated apoptosis was TRAIL specific, as soluble TRAIL receptor blocked target cell death. Moreover, IFN-stimulated interleukin (IL)-3 receptor (R)α+ blood precursor (pre-)DCs displayed minimal cytotoxicity toward the same target cells, demonstrating a clear functional difference between the CD11c+ DC and IL-3Rα+ pre-DC subsets. These results indicate that TRAIL may serve as an innate effector molecule on CD11c+ DCs for the elimination of spontaneously arising tumor cells and suggest a means by which TRAIL-expressing DCs may regulate or eliminate T cells responding to antigen presented by the DCs.

scholarly journals Enhanced antimicrobial peptide-induced activity in the mollusc Toll-2 family through evolution via tandem Toll/interleukin-1 receptor

2016 ◽  
Vol 3 (6) ◽  
pp. 160123 ◽  
Author(s):  
Jun Cao ◽  
Yihong Chen ◽  
Min Jin ◽  
Qian Ren
Keyword(s):  
Antimicrobial Peptide ◽  
Phylogenetic Analyses ◽  
Functional Divergence ◽  
Interleukin 1 ◽  
Intragenic Recombination ◽  
Functional Difference ◽  
S2 Cells ◽  
Over Expression ◽  
Motif Composition ◽  
Domain Insertion

Toll receptors play an important role in the innate immunity of invertebrates. All reported Tolls have only one Toll/interleukin-1 receptor (TIR) domain at the C-terminal. In this study, numerous Tolls with tandem TIRs at the C-terminal were found in molluscs. Such Tolls presented an extra TIR (TIR-1) compared with Toll-I. Thus, Toll-I might be the ancestor of tandem TIRs containing Toll. To test this hypothesis, 83 Toll-I and Toll-2 (most have two TIRs, but others seem to be the evolutionary intermediates) genes from 29 shellfish species were identified. These Tolls were divided into nine groups based on phylogenetic analyses. A strong correlation between phylogeny and motif composition was found. All Toll proteins contained the TIR-2 domain, whereas the TIR-1 domain only existed in some Toll-2 protein, suggesting that TIR-1 domain insertion may play an important role in Toll protein evolution. Further analyses of functional divergence and adaptive evolution showed that some of the critical sites responsible for functional divergence may have been under positive selection. An additional intragenic recombination played an important role in the evolution of the Toll-I and Toll-2 genes. To investigate the functional difference of Toll-I and Toll-2, over expression of Hcu_Toll-I or Hcu_Toll-2-2 in Drosophila S2 cells was performed. Results showed that Hcu_Toll-2-2 had stronger antimicrobial peptide (AMP) activity than Hcu_Toll-I. Therefore, enhanced AMP-induced activity resulted from tandem TIRs in Toll-2s of molluscs during evolution history.

scholarly journals GAGA Factor Isoforms Have Distinct but Overlapping Functions In Vivo

2001 ◽  
Vol 21 (24) ◽  
pp. 8565-8574 ◽  
Author(s):  
Anthony J. Greenberg ◽  
Paul Schedl
Keyword(s):  
Fusion Protein ◽  
Transcriptional Activation ◽  
Functional Difference ◽  
Wild Type ◽  
Gaga Factor ◽  
Phenotypic Analysis ◽  
Alternatively Spliced

ABSTRACT The Drosophila melanogaster GAGA factor (encoded by the Trithorax-like [Trl] gene) is required for correct chromatin architecture at diverse chromosomal sites. The Trl gene encodes two alternatively spliced isoforms of the GAGA factor (GAGA-519 and GAGA-581) that are identical except for the length and sequence of the C-terminal glutamine-rich (Q) domain. In vitro and tissue culture experiments failed to find any functional difference between the two isoforms. We made a set of transgenes that constitutively express cDNAs coding for either of the isoforms with the goal of elucidating their roles in vivo. Phenotypic analysis of the transgenes in Trl mutant background led us to the conclusion that GAGA-519 and GAGA-581 perform different, albeit largely overlapping, functions. We also expressed a fusion protein with LacZ disrupting the Q domain of GAGA-519. This LacZ fusion protein compensated for the loss of wild-type GAGA factor to a surprisingly large extent. This suggests that the Q domain either is not required for the essential functions performed by the GAGA protein or is exclusively used for tetramer formation. These results are inconsistent with a major role of the Q domain in chromatin remodeling or transcriptional activation. We also found that GAGA-LacZ was able to associate with sites not normally occupied by the GAGA factor, pointing to a role of the Q domain in binding site choice in vivo.

Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB

2021 ◽  
Vol 77 (9) ◽  
pp. 1206-1215
Author(s):  
Norbert Schormann ◽  
Sangeetha Purushotham ◽  
Joshua L. Mieher ◽  
Manisha Patel ◽  
Hui Wu ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Scavenger Receptor ◽  
Protein Docking ◽  
Terminal Region ◽  
Tooth Surface ◽  
Functional Difference ◽  
Streptococcus Gordonii ◽  
Viridans Streptococci ◽  
The Individual ◽  
Terminal Domains

Streptococcus gordonii is a member of the viridans streptococci and is an early colonizer of the tooth surface. Adherence to the tooth surface is enabled by proteins present on the S. gordonii cell surface, among which SspB belongs to one of the most well studied cell-wall-anchored adhesin families: the antigen I/II (AgI/II) family. The C-terminal region of SspB consists of three tandemly connected individual domains that display the DEv-IgG fold. These C-terminal domains contain a conserved Ca2+-binding site and isopeptide bonds, and they adhere to glycoprotein 340 (Gp340; also known as salivary agglutinin, SAG). Here, the structural and functional characterization of the C123 SspB domain at 2.7 Å resolution is reported. Although the individual C-terminal domains of Streptococcus mutans AgI/II and S. gordonii SspB show a high degree of both sequence and structural homology, superposition of these structures highlights substantial differences in their electrostatic surface plots, and this can be attributed to the relative orientation of the individual domains (C1, C2 and C3) with respect to each other and could reflect their specificity in binding to extracellular matrix molecules. Studies further confirmed that affinity for Gp340 or its scavenger receptor cysteine-rich (SRCR) domains requires two of the three domains of C123 SspB, namely C12 or C23, which is different from AgI/II. Using protein–protein docking studies, models for this observed functional difference between C123 SspB and C123 AgI/II in their binding to SRCR1 are presented.

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