Structure and Function of Phage RNA: A Summary of Current Knowledge

1973 ◽  
pp. 13-28
Author(s):  
C. Weissmann ◽  
M. A. Billeter ◽  
H. Weber ◽  
H. M. Goodman ◽  
J. Hindley
Keyword(s):  
Current Knowledge ◽  
Structure And Function ◽  
And Function

scholarly journals Structure and Function of the CFTR Chloride Channel

1999 ◽  
Vol 79 (1) ◽  
pp. S23-S45 ◽  
Author(s):  
DAVID N. SHEPPARD ◽  
MICHAEL J. WELSH
Keyword(s):  
Cystic Fibrosis ◽  
Chloride Channel ◽  
Atp Hydrolysis ◽  
Current Knowledge ◽  
Structure And Function ◽  
Binding Domains ◽  
Transporter Family ◽  
Membrane Spanning ◽  
And Function ◽  
R Domain

Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79 , Suppl.: S23–S45, 1999. — The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl− channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.

scholarly journals The Significance of Calcium in Photosynthesis

2019 ◽  
Vol 20 (6) ◽  
pp. 1353 ◽  
Author(s):  
Quan Wang ◽  
Sha Yang ◽  
Shubo Wan ◽  
Xinguo Li
Keyword(s):  
Signal Transduction ◽  
Binding Sites ◽  
Current Knowledge ◽  
Structure And Function ◽  
Biochemical Reactions ◽  
Chloroplast Proteins ◽  
Secondary Messenger ◽  
And Function ◽  
The Relationship ◽  
Physiological And Biochemical

As a secondary messenger, calcium participates in various physiological and biochemical reactions in plants. Photosynthesis is the most extensive biosynthesis process on Earth. To date, researchers have found that some chloroplast proteins have Ca2+-binding sites, and the structure and function of some of these proteins have been discussed in detail. Although the roles of Ca2+ signal transduction related to photosynthesis have been discussed, the relationship between calcium and photosynthesis is seldom systematically summarized. In this review, we provide an overview of current knowledge of calcium’s role in photosynthesis.

scholarly journals Mathematical Modelling of the Structure and Function of the Lymphatic System

Mathematics ◽  
2020 ◽  
Vol 8 (9) ◽  
pp. 1467
Author(s):  
Anastasia Mozokhina ◽  
Rostislav Savinkov
Keyword(s):  
Lymph Nodes ◽  
Mathematical Modelling ◽  
Mathematical Models ◽  
Lymphatic System ◽  
Current Knowledge ◽  
Structure And Function ◽  
Lymph Flow ◽  
And Function

This paper presents current knowledge about the structure and function of the lymphatic system. Mathematical models of lymph flow in the single lymphangion, the series of lymphangions, the lymph nodes, and the whole lymphatic system are considered. The main results and further perspectives are discussed.

Macromolecular constituents of basement membranes: a review of current knowledge on their structure and function

1983 ◽  
Vol 61 (8) ◽  
pp. 942-948 ◽  
Author(s):  
Paul G. Scott
Keyword(s):  
Type Iv Collagen ◽  
Current Knowledge ◽  
Heparan Sulphate ◽  
Structural Features ◽  
Structure And Function ◽  
Basement Membranes ◽  
Type Iv ◽  
Type V ◽  
And Function ◽  
Additional Form

Macromolecules which appear to be integral constituents of basement membranes include type IV collagen, the glycoprotein laminin, and heparan sulphate proteoglycan. Another glycoprotein, fibronectin, may occupy an intermediate position between some lining cells and their basement membranes but is not, however, restricted to this location. An additional form of collagen, genetic type V which differs significantly from type IV collagen in structure, appears to be associated with some basement membranes, possibly linking them to underlying connective tissue. The main structural features of each of these macromolecules, as presently understood, are reviewed here as a background to the experimental papers in this "mini-symposium."

scholarly journals Tunneling Nanotubes and Tumor Microtubes in Cancer

Cancers ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 857 ◽  
Author(s):  
Cora Roehlecke ◽  
Mirko H. H. Schmidt
Keyword(s):  
Therapeutic Potential ◽  
Current Knowledge ◽  
Cell Communication ◽  
Structure And Function ◽  
Intercellular Signaling ◽  
Tunneling Nanotubes ◽  
Dynamic Membrane ◽  
Membrane Protrusions ◽  
Direct Cell ◽  
And Function

Intercellular communication among cancer cells and their microenvironment is crucial to disease progression. The mechanisms by which communication occurs between distant cells in a tumor matrix remain poorly understood. In the last two decades, experimental evidence from different groups proved the existence of thin membranous tubes that interconnect cells, named tunneling nanotubes, tumor microtubes, cytonemes or membrane bridges. These highly dynamic membrane protrusions are conduits for direct cell-to-cell communication, particularly for intercellular signaling and transport of cellular cargo over long distances. Tunneling nanotubes and tumor microtubes may play an important role in the pathogenesis of cancer. They may contribute to the resistance of tumor cells against treatments such as surgery, radio- and chemotherapy. In this review, we present the current knowledge about the structure and function of tunneling nanotubes and tumor microtubes in cancer and discuss the therapeutic potential of membrane tubes in cancer treatment.

The physiology of lactoferrin

2002 ◽  
Vol 80 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Jeremy H Brock
Keyword(s):  
Current Knowledge ◽  
Binding Protein ◽  
Biochemical Properties ◽  
Structure And Function ◽  
Iron Nutrition ◽  
Future Research ◽  
Iron Binding ◽  
Physiological Functions ◽  
Iron Binding Protein ◽  
And Function

This paper reviews our current knowledge of the structure and function of the iron-binding protein lactoferrin. In particular, it attempts to relate the various proposed physiological functions of lactoferrin to its most characteristic biochemical properties, i.e. its ability to bind iron and its highly basic nature. The extent to which various physiological functions can be considered as definitely established is critically reviewed, and suggestions for future research are proposed.Key words: lactoferrin, iron, nutrition, immunology, infection, inflammation.

Subcellular Localization of Beta Hemoglobin Using pSNAPf fusion Protein

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 5560-5560
Author(s):  
Samia Jaffar ◽  
Aida Metzenberg ◽  
Gregor B. Adams
Keyword(s):  
Subcellular Localization ◽  
New Technologies ◽  
Conflicts Of Interest ◽  
Current Knowledge ◽  
Structure And Function ◽  
Beta Subunits ◽  
Cellular Interactions ◽  
Human Hemoglobin ◽  
Protein Subunits ◽  
And Function

Abstract Abstract: Much of what is known about hemoglobin relates to its structure and function. However, there is a great deal to learn about its assembly. The application of new technologies has allowed us to investigate the process of hemoglobin synthesis extensively. It has been shown that heme, synthesized in the mitochondria, is exported into the cytoplasm where it rapidly binds with apoglobin synthesized by polyribosomes. In this study,subcellular localization of newly synthesized alpha and beta subunits of human hemoglobin were examined using fluorescence microscopic imaging of cultured human erythroleukemic cells (cell line HEL 92.1.7). Experiments were used to determine the location of newly synthesized protein subunits. This paper will highlight the current knowledge of hemoglobin assembly, function and cellular interactions; and illustrate how cellular labels can be used to investigate this protein. It is hoped that future experiments will help to determine more details of the mechanism of globin assembly, which will be useful in the investigation of hemoglobinopathies. Disclosures No relevant conflicts of interest to declare.

Comparative structure and function of marsupial spermatozoa

1994 ◽  
Vol 6 (4) ◽  
pp. 421 ◽  
Author(s):  
PD Temple-Smith
Keyword(s):  
Sperm Motility ◽  
Comparative Studies ◽  
Current Knowledge ◽  
Structure And Function ◽  
Basic Organization ◽  
Nuclear Shaping ◽  
Comparative Structure ◽  
Nuclear Rotation ◽  
And Function ◽  
Posterior Ring

Marsupial sperm structure has been the focus of many comparative studies in the last 30 years. Although the basic organization of the marsupial spermatozoon is similar to that of eutherian mammals, spermatozoa from this branch of therian evolution have developed a specific suite of characters which clearly distinguish them from the Eutheria. This review surveys these specializations and examines current knowledge on their respective functions and the forces which shaped their evolution. Nuclear shaping and stability, the asymmetric positioning of the acrosome, and the unusual neck articulation are discussed. Although recent observations have provided evidence of a marsupial equatorial segment and posterior ring, the marsupial equivalent of the eutherian postacrosomal sheath has not been identified. The unusual neck structure of marsupial spermatozoa and the mobile articulation of the connecting piece are discussed in relation to nuclear rotation and the events associated with this process. Increasing flagellar length in some species is associated with extremes in flagellar organization and its effect on sperm motility is discussed.

scholarly journals Structure and Function of the Plasma Membrane

1968 ◽  
Vol 52 (1) ◽  
pp. 257-278 ◽  
Author(s):  
Edward D. Korn
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Current Knowledge ◽  
Structure And Function ◽  
Attractive Alternative ◽  
Membrane Function ◽  
Classical Models ◽  
And Function ◽  
Direct Attack ◽  
Membrane Biosynthesis

The paucimolecular unit membrane model of the structure of the plasma membrane is critically reviewed in relation to current knowledge of the chemical and enzymatic composition of isolated plasma membranes, the properties of phospholipids, the chemistry of fixation for electron microscopy, the conformation of membrane proteins, the nature of the lipid-protein bonds in membranes, and possible mechanisms of transmembrane transport and membrane biosynthesis. It is concluded that the classical models, although not disproven, are not well supported by, and are difficult to reconcile with, the data now available. On the other hand, although a model based on lipoprotein subunits is, from a biochemical perspective, an attractive alternative, it too is far from proven. Many of the questions may be resolved by studies of membrane function and membrane biosynthesis rather than by a direct attack on membrane structure.

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