Osseous and Cartilaginous Nasal Reconstruction

2017 ◽  
Vol 33 (01) ◽  
pp. 043-051 ◽  
Author(s):  
Samuel Hahn
Keyword(s):  
Three Dimensional ◽  
Preoperative Assessment ◽  
Dimensional Structure ◽  
Nasal Reconstruction ◽  
Functional Deficits ◽  
Form And Function ◽  
Nasal Defect ◽  
And Function ◽  
Grafting Materials ◽  
Autogenous Grafts

AbstractThe nose is a complex, three-dimensional structure that is supported by a framework of osseous and cartilaginous structures. Disruption of this framework can result in nasal deformity and functional deficits. Nasal reconstruction requires restoration of the osseous and cartilaginous framework. This requires careful preoperative assessment of the nasal defect and understanding the nasal and facial aesthetics that are supported by the osseous and cartilaginous support structures. Structural grafts can be classified as restorative, supportive, or contouring. Surgeons must understand the requirements for each type of grafting and which materials to use to provide the necessary structural reconstruction. Autogenous, homologous, and allogenic materials can be used for reconstruction of the structural deficits. Autogenous grafts from the septum, ear, rib, and calvarium are preferred for structural reconstruction, but surgeons should be well versed with alternative structural grafting materials. Smaller defects can be corrected through cartilaginous grafts, while larger defects require more rigid bony support to withstand the contractive forces of wound healing. Titanium mesh can serve as a viable alternative for rigid structural reconstruction. The ultimate goal of nasal reconstruction is to restore nasal form and function, and successful reconstruction starts with establishing a stable, functional, and anatomically sound osseocartilaginous framework.

In situ microtomy and serial block face imaging by SEM

1992 ◽  
Vol 50 (1) ◽  
pp. 778-779 ◽  
Author(s):  
Alan M. Kuzirian ◽  
Stephen B. Leighton
Keyword(s):  
Three Dimensional ◽  
Three Dimensions ◽  
Dimensional Structure ◽  
Form And Function ◽  
Central Focus ◽  
Block Face ◽  
And Function ◽  
Flow Of Information ◽  
The Brain

The ability to view objects, including subcellular structures, in three-dimensions is crucial to understanding their form and function. For example, the three-dimensional (3-D) structure of the brain and its neurons has been the central focus of neuroanatomists for well over 100 years. Yet, what role a nerve cell’s three dimensional structure plays in controlling the flow of information within the nervous system remains a mystery. Part of the problem has been the difficulty in obtaining an accurate 3-D picture of a nerve cell’s shape as well as documenting its synaptic interconnections. Although many neurobiologists have turned to biochemical studies in recent years, it is becoming clear that precise structure and network diagrams will be necessary to relate the work of cell biologists with that of computational neuroscientists.

Three dimensional structure and fluid flow through the hydrospires of the blastoid echinoderm, Pentremites rusticus

2010 ◽  
Vol 84 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Ronald C. Schmidtling ◽  
Charles R. Marshall
Keyword(s):  
Fluid Flow ◽  
Digital Image ◽  
Full Range ◽  
Three Dimensional ◽  
Initial Study ◽  
Dimensional Structure ◽  
Cross Sectional ◽  
Form And Function ◽  
Flow Through ◽  
And Function

The fluid flow through the complex hydrospires of the spiraculate blastoid Pentremites rusticus was analyzed using the first high-resolution three-dimensional digital image (and animation) of the hydrospires taken from a serially sectioned specimen. Measurements of the cross-sectional areas within the hydrospires, in conjunction with the Principle of Continuity, were used to infer the relative water velocity throughout the structures. Even though the calyx narrows adorally, the hydrospires expand in size, keeping pace with the increasing volume of water that entered through the hydrospire pores. Thus, the water maintained a relatively constant velocity within the hydrospire canals, 3.4 to 4.5 times the incurrent velocity. The spiracular openings are sufficiently large that no substantial increase in the exit velocity of the seawater would have been achieved unless the spiracular cover plates were used to reduce the size of the spiracular openings, which we infer was probably the case. The three-dimensional images underscore the fact that the two hydrospires that lie under each ambulacrum do not share the same spiracle and are not connected. Thus, we here redefine the term “hydrospire set” to refer to the pair of hydrospires that are connected. A number of anomalous accessory pores and canals were identified in the digital images. This initial study is based on a single specimen, and thus we were unable to determine the full range of variation present in Pentremites rusticus. Nonetheless, the digital image and the application of the Principle of Continuity offer new insights into the form and function of these remarkable respiratory structures.

Conformation of Ribosomes from Escherichia Coli

1974 ◽  
Vol 32 ◽  
pp. 210-211
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Binding Sites ◽  
Ribosomal Proteins ◽  
Fluorescent Dyes ◽  
Protein Biosynthesis ◽  
Three Dimensional ◽  
Spatial Arrangement ◽  
Dimensional Structure ◽  
Complete Understanding ◽  
And Function

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.

Structural Role of rRNAs on the Ribosomal Subunits from E. Coli by Scanning Transmission Electron Microscopy

1981 ◽  
Vol 39 ◽  
pp. 424-425
Author(s):  
M. Boublik ◽  
N. Robakis ◽  
J.S. Wall
Keyword(s):  
Three Dimensional ◽  
Uranyl Acetate ◽  
Dimensional Structure ◽  
Electron Microscopic ◽  
Ribosomal Subunits ◽  
E Coli ◽  
Freeze Dried ◽  
16S Rna ◽  
Scanning Transmission ◽  
And Function

The three-dimensional structure and function of biological supramolecular complexes are, in general, determined and stabilized by conformation and interactions of their macromolecular components. In the case of ribosomes, it has been suggested that one of the functions of ribosomal RNAs is to act as a scaffold maintaining the shape of the ribosomal subunits. In order to investigate this question, we have conducted a comparative TEM and STEM study of the structure of the small 30S subunit of E. coli and its 16S RNA.The conventional electron microscopic imaging of nucleic acids is performed by spreading them in the presence of protein or detergent; the particles are contrasted by electron dense solution (uranyl acetate) or by shadowing with metal (tungsten). By using the STEM on freeze-dried specimens we have avoided the shearing forces of the spreading, and minimized both the collapse of rRNA due to air drying and the loss of resolution due to staining or shadowing. Figure 1, is a conventional (TEM) electron micrograph of 30S E. coli subunits contrasted with uranyl acetate.

scholarly journals Impact of genetic variation on three dimensional structure and function of proteins

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0171355 ◽  
Author(s):  
Roshni Bhattacharya ◽  
Peter W. Rose ◽  
Stephen K. Burley ◽  
Andreas Prlić
Keyword(s):  
Genetic Variation ◽  
Three Dimensional ◽  
Structure And Function ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
And Function

The Study on the Clinical Phenotype and Function of HPRT1 Gene

2021 ◽  
Author(s):  
Miao Guo ◽  
Yucai Chen ◽  
Longlong Lin ◽  
Yilin Wang ◽  
Anqi Wang ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Clinical Manifestations ◽  
Protein Translation ◽  
Dimensional Structure ◽  
Normal Individuals ◽  
Second Generation Sequencing ◽  
Self Harm ◽  
And Function ◽  
Neurogenetic Disease ◽  
Generation Sequencing

Abstract Background: Lesch-Nyhan disease (LND) is a rare x-linked purine metabolic neurogenetic disease caused by enzyme hypoxanthine-guanine phosphoriribosyltransferase(HGprt) deficiency, also known as self-destructive appearance syndrome. A series of manifestations are caused by abnormal purine metabolism. The typical clinical manifestations are hyperuricemia, growth retardation, mental retardation, short stature, dance-like athetosis, aggressive behavior, and compulsive self-harm.. Results: we identified a point mutation c.151C > T (p. Arg51*) in a pedigree. We analyzed the clinical characteristics of children in a family, and obtained the blood of their parents and siblings for second-generation sequencing. At the same time, we also analyzed and compared the expression of HPRT1 gene and predicted the three-dimensional structure of the protein. And we analyzed the clinical manifestations caused by the defect of the HPRT1 genethe mutation led to the termination of transcription at the 51st arginine, resulting in the production of truncated protein, and the relative expression of HPRT1 gene in patients was significantly lower than other family members and 10 normal individuals. Conclusion: this mutation leads to the early termination of protein translation and the formation of a truncated HPRT protein, which affects the function of the protein and generates corresponding clinical manifestations.

scholarly journals Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
A.E. Naas ◽  
A.K. MacKenzie ◽  
B. Dalhus ◽  
V.G.H. Eijsink ◽  
P.B. Pope
Keyword(s):  
Active Site ◽  
Three Dimensional ◽  
Structural Features ◽  
Structure And Function ◽  
Dimensional Structure ◽  
Active Site Cleft ◽  
Polysaccharide Utilization Locus ◽  
And Function ◽  
Rumen Metagenome

Abstract Previous gene-centric analysis of a cow rumen metagenome revealed the first potentially cellulolytic polysaccharide utilization locus, of which the main catalytic enzyme (AC2aCel5A) was identified as a glycoside hydrolase (GH) family 5 endo-cellulase. Here we present the 1.8 Å three-dimensional structure of AC2aCel5A and characterization of its enzymatic activities. The enzyme possesses the archetypical (β/α)8-barrel found throughout the GH5 family and contains the two strictly conserved catalytic glutamates located at the C-terminal ends of β-strands 4 and 7. The enzyme is active on insoluble cellulose and acts exclusively on linear β-(1,4)-linked glucans. Co-crystallization of a catalytically inactive mutant with substrate yielded a 2.4 Å structure showing cellotriose bound in the −3 to −1 subsites. Additional electron density was observed between Trp178 and Trp254, two residues that form a hydrophobic “clamp”, potentially interacting with sugars at the +1 and +2 subsites. The enzyme’s active-site cleft was narrower compared to the closest structural relatives, which in contrast to AC2aCel5A, are also active on xylans, mannans and/or xyloglucans. Interestingly, the structure and function of this enzyme seem adapted to less-substituted substrates such as cellulose, presumably due to the insufficient space to accommodate the side-chains of branched glucans in the active-site cleft.

scholarly journals Weighing trees with lasers: advances, challenges and opportunities

2018 ◽  
Vol 8 (2) ◽  
pp. 20170048 ◽  
Author(s):  
M. I. Disney ◽  
M. Boni Vicari ◽  
A. Burt ◽  
K. Calders ◽  
S. L. Lewis ◽  
...  
Keyword(s):  
Laser Scanning ◽  
Large Scale ◽  
Three Dimensional ◽  
Point Clouds ◽  
3D Models ◽  
Tree Form ◽  
Form And Function ◽  
Challenges And Opportunities ◽  
And Function ◽  
Non Destructive

Terrestrial laser scanning (TLS) is providing exciting new ways to quantify tree and forest structure, particularly above-ground biomass (AGB). We show how TLS can address some of the key uncertainties and limitations of current approaches to estimating AGB based on empirical allometric scaling equations (ASEs) that underpin all large-scale estimates of AGB. TLS provides extremely detailed non-destructive measurements of tree form independent of tree size and shape. We show examples of three-dimensional (3D) TLS measurements from various tropical and temperate forests and describe how the resulting TLS point clouds can be used to produce quantitative 3D models of branch and trunk size, shape and distribution. These models can drastically improve estimates of AGB, provide new, improved large-scale ASEs, and deliver insights into a range of fundamental tree properties related to structure. Large quantities of detailed measurements of individual 3D tree structure also have the potential to open new and exciting avenues of research in areas where difficulties of measurement have until now prevented statistical approaches to detecting and understanding underlying patterns of scaling, form and function. We discuss these opportunities and some of the challenges that remain to be overcome to enable wider adoption of TLS methods.

Multiplicity spin, structure, and charge of iron-verdohemeoxygenase complex: A comparison study by the DFT method

2020 ◽  
Vol 24 (10) ◽  
pp. 1208-1214
Author(s):  
Hamideh Tasharofi ◽  
Maryam Daghighi Asli ◽  
Parisa Rajabali Jamaat
Keyword(s):  
Heme Oxygenase ◽  
Density Functional ◽  
Complex Structure ◽  
Three Dimensional ◽  
Dft Method ◽  
Basis Set ◽  
Dimensional Structure ◽  
Central Metal ◽  
Stable States ◽  
And Function

Recently the three-dimensional structure of verdoheme heme oxygenase complex was revealed. However, many parameters of verdoheme heme oxygenase’s complex structure and their role and function on Heme degradation were unknown. In this work the structure of iron verdoheme in complex with heme oxygenase was compared by the density functional theory (DFT)-based B3LYP method using the 6-31G basis set. Many parameters such as charge of verdoheme and iron as central metal, electron distribution, spin multiplicity of the molecule and proximal substituents effects on verdoheme ring stabilization and their arrangement are discussed and compared for twelve different conformations of the molecules to find the most energetically stable states.

Sign in / Sign up

Export Citation Format

Share Document