Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies

2006 ◽  
Vol 30 (11) ◽  
pp. 1662 ◽  
Author(s):  
Antonino Mazzaglia ◽  
Antonio Valerio ◽  
Valentina Villari ◽  
Anna Rencurosi ◽  
Luigi Lay ◽  
...  
Keyword(s):  
Specific Protein ◽  
Protein Recognition ◽  
Size Controlled

Specific protein recognition of an mRNA cap through its alkylated base

1997 ◽  
Vol 4 (5) ◽  
pp. 350-354 ◽  
Author(s):  
Alec E. Hodel ◽  
Paul D. Gershon ◽  
Xuenong Shi ◽  
Shi-Mei Wang ◽  
Florante A. Quiocho
Keyword(s):  
Specific Protein ◽  
Protein Recognition

N-Acetylglucosamine biofunctionalized CdSeTe quantum dots as fluorescence probe for specific protein recognition

The Analyst ◽  
2013 ◽  
Vol 138 (2) ◽  
pp. 666-670 ◽  
Author(s):  
Fang-Fang Cheng ◽  
Guo-Xi Liang ◽  
Yuan-Yuan Shen ◽  
Rohit Kumar Rana ◽  
Jun-Jie Zhu
Keyword(s):  
Quantum Dots ◽  
Fluorescence Probe ◽  
Specific Protein ◽  
Protein Recognition

Highly Hydrophilic Surfaces from Polyglycidol Grafts with Dual Antifouling and Specific Protein Recognition Properties

Langmuir ◽  
2011 ◽  
Vol 27 (15) ◽  
pp. 9285-9294 ◽  
Author(s):  
Sarra Gam-Derouich ◽  
Monika Gosecka ◽  
Sandrine Lepinay ◽  
Mireille Turmine ◽  
Benjamin Carbonnier ◽  
...  
Keyword(s):  
Specific Protein ◽  
Protein Recognition ◽  
Hydrophilic Surfaces

scholarly journals HPV E6 and MAGUK protein interactions: determination of the molecular basis for specific protein recognition and degradation

Oncogene ◽  
2001 ◽  
Vol 20 (39) ◽  
pp. 5431-5439 ◽  
Author(s):  
Miranda Thomas ◽  
Britt Glaunsinger ◽  
David Pim ◽  
Ron Javier ◽  
Lawrence Banks
Keyword(s):  
Protein Interactions ◽  
Molecular Basis ◽  
Specific Protein ◽  
Protein Recognition ◽  
Hpv E6 ◽  
Maguk Protein

Glycopolymer brushes with specific protein recognition property

2017 ◽  
Vol 134 (36) ◽  
pp. 45238 ◽  
Author(s):  
Talya Tugana Kursun ◽  
Dilek Cimen ◽  
Tuncer Caykara
Keyword(s):  
Specific Protein ◽  
Protein Recognition ◽  
Recognition Property

Densitometric Identification of Primitive Erythroblasts After Reaction With Diaminobenzidine

1973 ◽  
Vol 31 ◽  
pp. 328-329
Author(s):  
John A. Trotter
Keyword(s):  
Red Blood Cells ◽  
Analytical Method ◽  
Blood Cells ◽  
Guinea Pigs ◽  
Specific Protein ◽  
Visual Examination ◽  
Hemoglobin Synthesis ◽  
Peroxidatic Activity ◽  
Small Density

Hemoglobin is the specific protein of red blood cells. Those cells in which hemoglobin synthesis is initiated are the earliest cells that can presently be considered to be committed to erythropoiesis. In order to identify such early cells electron microscopically, we have made use of the peroxidatic activity of hemoglobin by reacting the marrow of erythropoietically stimulated guinea pigs with diaminobenzidine (DAB). The reaction product appeared as a diffuse and amorphous electron opacity throughout the cytoplasm of reactive cells. The detection of small density increases of such a diffuse nature required an analytical method more sensitive and reliable than the visual examination of micrographs. A procedure was therefore devised for the evaluation of micrographs (negatives) with a densitometer (Weston Photographic Analyzer).

Specific Labeling of Protein Domains with Antibody Fragments

1981 ◽  
Vol 39 ◽  
pp. 416-417
Author(s):  
U. Aebi ◽  
L.E. Buhle ◽  
W.E. Fowler
Keyword(s):  
Image Processing ◽  
Specific Protein ◽  
Antibody Fragments ◽  
Supramolecular Organization ◽  
Two Dimensional ◽  
Ordered Structures ◽  
Virus Capsids ◽  
Processing Techniques

Many important supramolecular structures such as filaments, microtubules, virus capsids and certain membrane proteins and bacterial cell walls exist as ordered polymers or two-dimensional crystalline arrays in vivo. In several instances it has been possible to induce soluble proteins to form ordered polymers or two-dimensional crystalline arrays in vitro. In both cases a combination of electron microscopy of negatively stained specimens with analog or digital image processing techniques has proven extremely useful for elucidating the molecular and supramolecular organization of the constituent proteins. However from the reconstructed stain exclusion patterns it is often difficult to identify distinct stain excluding regions with specific protein subunits. To this end it has been demonstrated that in some cases this ambiguity can be resolved by a combination of stoichiometric labeling of the ordered structures with subunit-specific antibody fragments (e.g. Fab) and image processing of the electron micrographs recorded from labeled and unlabeled structures.

Immunocytochemical localization of p65 with one-nanometer gold particles following silver development

1989 ◽  
Vol 47 ◽  
pp. 1042-1043
Author(s):  
Richard W. Burry ◽  
Diane M. Hayes
Keyword(s):  
Plasma Membrane ◽  
Bovine Serum Albumin ◽  
Calf Serum ◽  
Specific Protein ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Gold Particles ◽  
Pass Through ◽  
Label Distribution ◽  
Phosphate Buffered Saline

Electron microscopic (EM) immunocytochemistry localization of the neuron specific protein p65 could show which organelles contain this antigen. Antibodies (Ab) labeled with horseradish peroxidase (HRP) followed by chromogen development show a broad diffuse label distribution within cells and restricting identification of organelles. Particulate label (e.g. 10 nm colloidal gold) is highly desirable but not practical because penetration into cells requires destroying the plasma membrane. We report pre-embedding immunocytochemistry with a particulate marker, 1 nm gold, that will pass through membranes treated with saponin, a mild detergent.Cell cultures of the rat cerebellum were fixed in buffered 4% paraformaldehyde and 0.1% glutaraldehyde (Glut.). The buffer for all incubations and rinses was phosphate buffered saline with: 1% calf serum, 0.2% saponin, 0.1% gelatin, 50 mM glycine 1 mg/ml bovine serum albumin, and (not in the HRP labeled cultures) 0.02% sodium azide. The monoclonal #48 to p65 was used with three label systems: HRP, 1 nm avidin gold with IntenSE M development, and 1 nm avidin gold with Danscher development.

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