A conserved aromatic moiety in the ectodomain is a key determinant for structural integrity and protein trafficking of TNFR superfamily

2020 ◽  
Vol 34 (12) ◽  
pp. 15687-15700
Author(s):  
Hong Wang ◽  
Joo Hyoung Lee ◽  
Yong Wang ◽  
Hwa‐seon Seo ◽  
Jianbo Wang ◽  
...  
Keyword(s):  
Protein Trafficking ◽  
Structural Integrity ◽  
Aromatic Moiety ◽  
Tnfr Superfamily

Electron Beam Damage of Biomolecules Assessed by Energy Loss Spectroscopy

1978 ◽  
Vol 36 (3) ◽  
pp. 61-69
Author(s):  
M. Isaacson ◽  
M.L. Collins ◽  
M. Listvan
Keyword(s):  
Electron Microscopy ◽  
Radiation Damage ◽  
Structural Integrity ◽  
Analytical Electron Microscopy ◽  
High Dose ◽  
Dose Rates ◽  
Special Cases ◽  
Analytical Electron ◽  
Atom Migration ◽  
Beam Damage

Over the past five years it has become evident that radiation damage provides the fundamental limit to the study of blomolecular structure by electron microscopy. In some special cases structural determinations at very low doses can be achieved through superposition techniques to study periodic (Unwin & Henderson, 1975) and nonperiodic (Saxton & Frank, 1977) specimens. In addition, protection methods such as glucose embedding (Unwin & Henderson, 1975) and maintenance of specimen hydration at low temperatures (Taylor & Glaeser, 1976) have also shown promise. Despite these successes, the basic nature of radiation damage in the electron microscope is far from clear. In general we cannot predict exactly how different structures will behave during electron Irradiation at high dose rates. Moreover, with the rapid rise of analytical electron microscopy over the last few years, nvicroscopists are becoming concerned with questions of compositional as well as structural integrity. It is important to measure changes in elemental composition arising from atom migration in or loss from the specimen as a result of electron bombardment.

Structural integrity after cold storage of human epidermal model in hypothermosol: A correlative ultrastructural and fluorescent assay

1994 ◽  
Vol 52 ◽  
pp. 270-271
Author(s):  
Henry H. Eichelberger ◽  
John G. Baust ◽  
Robert G. Van Buskirk
Keyword(s):  
Cold Storage ◽  
Structural Integrity ◽  
Culture Media ◽  
Cell Structure ◽  
Natural State ◽  
Sodium Cacodylate ◽  
Ruthenium Tetroxide ◽  
Cacodylate Buffer ◽  
Before And After

For research in cell differentiation and in vitro toxicology it is essential to provide a natural state of cell structure as a benchmark for interpreting results. Hypothermosol (Cryomedical Sciences, Rockville, MD) has proven useful in insuring the viability of synthetic human epidermis during cold-storage and in maintaining the epidermis’ ability to continue to differentiate following warming.Human epidermal equivalent, EpiDerm (MatTek Corporation, Ashland, MA) consisting of fully differentiated stratified human epidermal cells were grown on a microporous membrane. EpiDerm samples were fixed before and after cold-storage (4°C) for 5 days in Hypothermosol or skin culture media (MatTek Corporation) and allowed to recover for 7 days at 37°C. EpiDerm samples were fixed 1 hour in 2.5% glutaraldehyde in sodium cacodylate buffer (pH 7.2). A secondary fixation with 0.2% ruthenium tetroxide (Polysciences, Inc., Warrington, PA) in sodium cacodylate was carried out for 3 hours at 4°C. Other samples were similarly fixed, but with 1% Osmium tetroxide in place of ruthenium tetroxide. Samples were dehydrated through a graded acetone series, infiltrated with Spurrs resin (Polysciences Inc.) and polymerized at 70°C.

High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

1990 ◽  
Vol 48 (1) ◽  
pp. 610-610
Author(s):  
Werner Kühlbrandt ◽  
Da Neng Wang ◽  
K.H. Downing
Keyword(s):  
High Resolution ◽  
Electron Diffraction ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Structural Integrity ◽  
Light Harvesting ◽  
Lhc Ii ◽  
Diffraction Patterns ◽  
Difference Fourier ◽  
2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

Role of molecular chaperones in steroid receptor action

2004 ◽  
Vol 40 ◽  
pp. 41-58 ◽  
Author(s):  
William B Pratt ◽  
Mario D Galigniana ◽  
Yoshihiro Morishima ◽  
Patrick J M Murphy
Keyword(s):  
Transcriptional Activation ◽  
Protein Trafficking ◽  
Steroid Receptors ◽  
Transcriptional Regulatory ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
Receptor Action ◽  
Binding Cleft ◽  
Hsp 90

Unliganded steroid receptors are assembled into heterocomplexes with heat-shock protein (hsp) 90 by a multiprotein chaperone machinery. In addition to binding the receptors at the chaperone site, hsp90 binds cofactors at other sites that are part of the assembly machinery, as well as immunophilins that connect the assembled receptor-hsp90 heterocomplexes to a protein trafficking pathway. The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. In the nucleus, the chaperone machinery interacts with the receptor in transcriptional regulatory complexes after hormone dissociation to release the receptor and terminate transcriptional activation. By forming heterocomplexes with hsp90, the chaperone machinery stabilizes the receptor to degradation by the ubiquitin-proteasome pathway of proteolysis.

COMPARATIVE STUDY OF THE STRUCTURAL INTEGRITY OF SPERMATOZOA IN EPIDIDYMAL, EJACULATED AND CRYOPRESERVED SEMEN OF STALLIONS

2017 ◽  
Vol 52 (2) ◽  
pp. 274-281
Author(s):  
M.M. Atroshchenko ◽  
◽  
V.V. Kalaschnikov ◽  
Ye.Ye. Bragina ◽  
A.M. Zaitsev ◽  
...  
Keyword(s):  
Comparative Study ◽  
Structural Integrity

A philosophy for structural integrity of large panel buildings

PCI Journal ◽  
1976 ◽  
Vol 21 (3) ◽  
pp. 46-69 ◽  
Author(s):  
Mark Fintel ◽  
Donald M. Schultz
Keyword(s):  
Structural Integrity ◽  
Large Panel

Identification of Possible High Integrity Containers for Low-Level Nuclear Waste Disposal

1981 ◽  
Vol 6 ◽  
Author(s):  
Jeffrey D. Williams
Keyword(s):  
South Carolina ◽  
Structural Integrity ◽  
Exchange Resin ◽  
Ion Exchange Resin ◽  
Economic Factors ◽  
Burial Site ◽  
Low Level ◽  
High Integrity ◽  
Low Level Radioactive Waste ◽  
Selection Of

ABSTRACTIncreased concern by the State of South Carolina over the condition and capacity of the low-level radioactive waste burial site at Barnwell has prompted them to promulgate new regulations on waste burial containers. As of September 30, 1981, ion exchange resin and filter media waste with an activity of 1 μCi/cc or greater and with isotopes with halflives greater than five years disposed at Barnwell shall be solidified or confined in a “high integrity container”. The materials and designs of these containers are required to provide waste isolation from the environment for a period of 300 years and provide the structural integrity specified in 49 CFR 173.398(b). HITTMAN has been active in the design and development of containers suitable for this purpose with this paper detailing the analyses involved. Material selections were limited to stainless steel, fiberglass, and polyethylenes. Structural concerns focused on overpressure requirements, drop-testing requirements, and lifting capabilities. With a lifetime dose of up to 108 rads, the possibilities of radiation damage were considered. Preliminary selection of polyethylene was based on satisfactory resolution of these issues and economic factors.

Bio-Inspired Submicron Electrodes

2003 ◽  
Vol 775 ◽  
Author(s):  
Ivan Stanish ◽  
Daniel A. Lowy ◽  
Alok Singh
Keyword(s):  
Electrode Surface ◽  
Structural Integrity ◽  
Electron Flow ◽  
Charge Storage ◽  
Electroactive Material ◽  
Electron Coupling ◽  
Strong Potential ◽  
Electrical Potentials ◽  
Submicron Scale ◽  
Potential Gradients

AbstractImmobilized polymerized electroactive vesicles (IPEVs) are submicron biocapsules capable of storing charge in confined environments and chemisorbing on surfaces. Methods to immobilize stable submicron sized electroactive vesicles and the means to measure electroactivity of IPEVs at nanolevels have been demonstrated. IPEVs can withstand steep potential gradients applied across their membrane, maintain their structural integrity against surfaces poised at high/low electrical potentials, retain electroactive material over several days, and reversibly mediate (within the membrane) electron flow between the electrode surface and vesicle interior. IPEVs have strong potential to be used for charge storage and electron coupling applications that operate on the submicron scale and smaller.

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