Structural Studies of Autophagy-Related Proteins

2019 ◽  
pp. 17-56 ◽  
Author(s):  
Melanie Schwarten ◽  
Oliver H. Weiergräber ◽  
Dušan Petrović ◽  
Birgit Strodel ◽  
Dieter Willbold
Keyword(s):  
Structural Studies ◽  
Related Proteins

scholarly journals Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2

PLoS ONE ◽  
2010 ◽  
Vol 5 (11) ◽  
pp. e13559 ◽  
Author(s):  
Melanie A. Adams-Cioaba ◽  
Yahong Guo ◽  
ChuanBing Bian ◽  
Maria F. Amaya ◽  
Robert Lam ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Fragile X ◽  
Structural Studies ◽  
Fragile X Mental Retardation ◽  
Related Proteins

scholarly journals Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Qie Kuang ◽  
Pasi Purhonen ◽  
Hans Hebert
Keyword(s):  
Membrane Proteins ◽  
General Idea ◽  
General Description ◽  
Two Dimensional ◽  
Structural Studies ◽  
Electron Crystallography ◽  
Electron Microscopic ◽  
Small Proteins ◽  
Crystallization Procedure ◽  
Related Proteins

Membrane proteins play important roles for living cells. Structural studies of membrane proteins provide deeper understanding of their mechanisms and further aid in drug design. As compared to other methods, electron microscopy is uniquely suitable for analysis of a broad range of specimens, from small proteins to large complexes. Of various electron microscopic methods, electron crystallography is particularly well-suited to study membrane proteins which are reconstituted into two-dimensional crystals in lipid environments. In this review, we discuss the steps and parameters for obtaining large and well-ordered two-dimensional crystals. A general description of the principle in each step is provided since this information can also be applied to other biochemical and biophysical methods. The examples are taken from our own studies and published results with related proteins. Our purpose is to give readers a more general idea of electron crystallography and to share our experiences in obtaining suitable crystals for data collection.

scholarly journals Structural studies of kinesin-related proteins complexed to microtubules

2000 ◽  
Vol 40 (supplement) ◽  
pp. S69
Author(s):  
K. Hirose ◽  
T. Akiba ◽  
Sharyn Endow ◽  
Maria Alonso ◽  
Robert Gross ◽  
...  
Keyword(s):  
Structural Studies ◽  
Related Proteins

scholarly journals Structural studies of Sm-related proteins from archaea

2000 ◽  
Vol 56 (s1) ◽  
pp. s89-s89
Author(s):  
I. Törõ ◽  
C. Mayer ◽  
S. Thore ◽  
J. Basquin ◽  
H. Dreher ◽  
...  
Keyword(s):  
Structural Studies ◽  
Related Proteins

scholarly journals A Structural Approach into Drug Discovery Based on Autophagy

Life ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 526
Author(s):  
Sung-Min Kang ◽  
Do-Hee Kim
Keyword(s):  
High Throughput Screening ◽  
Drug Target ◽  
Metabolic Diseases ◽  
Structural Information ◽  
Screening Methods ◽  
Structural Studies ◽  
Intracellular Degradation ◽  
Structure Activity ◽  
Related Proteins ◽  
Novel Drug

Autophagy is a lysosome-dependent intracellular degradation machinery that plays an essential role in the regulation of cellular homeostasis. As many studies have revealed that autophagy is related to cancer, neurodegenerative diseases, metabolic diseases, and so on, and it is considered as a promising drug target. Recent advances in structural determination and computational technologies provide important structural information on essential autophagy-related proteins. Combined with high-throughput screening methods, structure-activity relationship studies have led to the discovery of molecules that modulate autophagy. In this review, we summarize the recent structural studies on autophagy-related proteins and the discovery of modulators, indicating that targeting autophagy can be utilized as an effective strategy for novel drug development.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Structural Studies on Mitotic Spindle Fibres

1978 ◽  
Vol 36 (3) ◽  
pp. 615-626
Author(s):  
J.R. Mcintosh
Keyword(s):  
Chemical Composition ◽  
Mitotic Spindle ◽  
Structural Studies ◽  
Mitotic Apparatus ◽  
Chemical Studies ◽  
Medical Interest ◽  
Spindle Fibres

The mitotic apparatus is a structure of obvious biological and medical interest, but it has proved to be a difficult cellular machine to understand. The chemical composition of the spindle is only slightly elucidated, largely because of the difficulties in preparing useful isolates of the structure. Chemical studies of the mitotic spindle have been reviewed elsewhere (Mcintosh, 1977), and will not be discussed further here. One would think that structural studies on the mitotic apparatus (MA) in situ would be straightforward, but even with this approach there is some disagreement in the results obtained with various methods and by different investigators. In this paper I will review briefly the approaches which have been used in structural studies of the MA, pointing out the strengths and problems of each approach. I will summarize the principal findings of the different methods, and identify what seem to be fruitful avenues for further work.

Image registration with a computer driven S.T.E.M.

1978 ◽  
Vol 36 (1) ◽  
pp. 98-99
Author(s):  
A.M.H. Schepman ◽  
J.A.P. van der Voort ◽  
J.E. Mellema
Keyword(s):  
Spot Size ◽  
Scanning Transmission Electron Microscope ◽  
Small Computer ◽  
Structural Studies ◽  
Area Of Interest ◽  
Transmission Electron ◽  
Scanning Transmission ◽  
Specimen Area ◽  
On Line ◽  
Minimum Distances

A Scanning Transmission Electron Microscope (STEM) was coupled to a small computer. The system (see Fig. 1) has been built using a Philips EM400, equipped with a scanning attachment and a DEC PDP11/34 computer with 34K memory. The gun (Fig. 2) consists of a continuously renewed tip of radius 0.2 to 0.4 μm of a tungsten wire heated just below its melting point by a focussed laser beam (1). On-line operation procedures were developped aiming at the reduction of the amount of radiation of the specimen area of interest, while selecting the various imaging parameters and upon registration of the information content. Whereas the theoretical limiting spot size is 0.75 nm (2), routine resolution checks showed minimum distances in the order 1.2 to 1.5 nm between corresponding intensity maxima in successive scans. This value is sufficient for structural studies of regular biological material to test the performance of STEM over high resolution CTEM.

The Fine Structure of Phloem Cells

1985 ◽  
Vol 43 ◽  
pp. 632-635
Author(s):  
James Cronshaw
Keyword(s):  
Structural Studies ◽  
High Concentration ◽  
Long Distance ◽  
Phloem Tissue ◽  
Sieve Elements ◽  
Long Distance Transport ◽  
P Protein ◽  
Companion Cells ◽  
Electron Microscopical ◽  
Distance Transport

Long distance transport in plants takes place in phloem tissue which has characteristic cells, the sieve elements. At maturity these cells have sieve areas in their end walls with specialized perforations. They are associated with companion cells, parenchyma cells, and in some species, with transfer cells. The protoplast of the functioning sieve element contains a high concentration of sugar, and consequently a high hydrostatic pressure, which makes it extremely difficult to fix mature sieve elements for electron microscopical observation without the formation of surge artifacts. Despite many structural studies which have attempted to prevent surge artifacts, several features of mature sieve elements, such as the distribution of P-protein and the nature of the contents of the sieve area pores, remain controversial.

An ultrastructural study on the shark liver

1990 ◽  
Vol 48 (3) ◽  
pp. 512-513
Author(s):  
Masako Yamada ◽  
Yutaka Tanuma
Keyword(s):  
Portal Vein ◽  
Kupffer Cells ◽  
Ultrastructural Study ◽  
Lipid Droplets ◽  
Microscopic Level ◽  
The Other ◽  
Fish Stock ◽  
Structural Studies ◽  
Light Microscopic Level ◽  
Perfusion Fixation

Although many fine structural studies on the vertebrate liver have been reported on mammals, avians, reptiles, amphibians, teleosts and cyclostomes, there are no studies on elasmobranchii liver except one by T. Ito etal. (1962) who studied it on light microscopic level. The purpose of the present study was to as certain the ultrastructural details and cytochemical characteristics of normal elasmobranchii liver and was to compare with the other higher vertebrate ones.Seventeen Scyliorhinus torazame, one kind of elasmobranchii, were obtained from the fish stock of the Ueno Zoo aquarium, Ueno, Tokyo. The sharks weighing about 300-600g were anesthetized with MS-222 (Sigma), and the livers were fixed by perfusion fixation via the portal vein according to the procedure of Y. Saito et al. (1980) for 10 min. Then the liver tissues were immersed in the same fixative for 2 hours and postfixed with 1% OsO4-solution in 0.1 Mc acodylate buffer for one hour. In order to make sure a phagocytic activity of Kupffer cells, latex particles (0.8 μm in diameter, 0.05mg/100 g b.w.) were injected through the portal vein for one min before fixation. For preservation of lipid droplets in the cytoplasm, a series of these procedure were performed under ice cold temperature until the end of dehydration.

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