09-05-2021-0207 - chol palm black blud N-Party (with Surprise Cake)

 

Wrist X ray showing changes in rickets. Mainly cupping is seen here.

 The underlying mechanism involves insufficient calcification of the growth plate.^[6]Diagnosis is generally based on blood tests finding a low calcium, low phosphorus, and a high alkaline phosphatase together with X-rays.^[2]

https://en.wikipedia.org/wiki/Rickets

https://en.wikipedia.org/wiki/Phosphorus

hide v t e Malnutrition
Protein-energy malnutrition	Kwashiorkor Marasmus Catabolysis
Vitamin deficiency	B vitamins B1  Beriberi Wernicke–Korsakoff syndrome Wernicke's encephalopathy Korsakoff's syndrome B2 Riboflavin deficiency B3  Pellagra B6  Pyridoxine deficiency B7  Biotin deficiency B9 Folate deficiency B12  Vitamin B12 deficiency Other A: Vitamin A deficiency  Bitot's spots C: Scurvy D: Vitamin D deficiency  Rickets Osteomalacia Harrison's groove E: Vitamin E deficiency K: Vitamin K deficiency
Mineral deficiency	Sodium Potassium Magnesium Calcium Iron Zinc Manganese Copper Iodine Chromium Molybdenum Selenium Keshan disease
Growth	Delayed milestone Failure to thrive Short stature  Idiopathic
General	Anorexia Weight loss Cachexia Underweight

Authority control: National libraries	France (data) United States Japan

Categories: 

• Skeletal disorders
• Vitamin D
• Vitamin deficiencies

Rickettsia
Red-stained Rickettsia rickettsii visible in cells of an Ixodid vector tick

https://en.wikipedia.org/wiki/Rickettsia

Anaplasmosis
Anaplasma centrale infecting the red blood cells of a cow: The arrow points to typical infected cell.
Specialty	Veterinary medicine

Rickettsialpox
Rickettsialpox lesion
Specialty	Infectious disease
Prognosis	Resolves in 2-3 weeks without treatment

Brucella ceti is a gram negative bacterial pathogen of the Brucellaceae family that causes brucellosis in cetaceans. Brucella ceti has been found in both classes of cetaceans, mysticetes and odontocetes.^[1] Brucellosis in some dolphins and porpoises can result in serious clinical signs including fetal abortions, male infertility, neurobrucellosis, cardiopathies, bone and skin lesions, strand events, and death.^[1]

https://en.wikipedia.org/wiki/Brucella_ceti

Brucella suis is a bacterium that causes swine brucellosis, a zoonosis that affects pigs. The disease typically causes chronic inflammatory lesions in the reproductive organs of susceptible animals or orchitis, and may even affect joints and other organs.^[1] 

https://en.wikipedia.org/wiki/Brucella_suis

Black blud - https://en.wikipedia.org/wiki/Bubonic_plague

chole palm - https://en.wikipedia.org/wiki/Poxviridae

BB - https://en.wikipedia.org/wiki/Hepatitis_C_virus

CP - https://en.wikipedia.org/wiki/Herpesviridae

BB - https://en.wikipedia.org/wiki/Oncovirus

BB - https://en.wikipedia.org/wiki/Viral_hemorrhagic_septicemia

CP - https://en.wikipedia.org/wiki/Infectious_causes_of_cancer

CP - https://en.wikipedia.org/wiki/Enzootic_nasal_adenocarcinoma

CP - https://en.wikipedia.org/wiki/Ovine_pulmonary_adenocarcinoma

BB - https://en.wikipedia.org/wiki/Clonally_transmissible_cancer

BB - https://en.wikipedia.org/wiki/Kaposi%27s_sarcoma-associated_herpesvirus

BBCP - https://en.wikipedia.org/wiki/Human_papillomavirus_infection

BBCP - https://en.wikipedia.org/wiki/Fungal_infection

BB

https://en.wikipedia.org/wiki/Epstein–Barr_virus

https://en.wikipedia.org/wiki/Progressive_multifocal_leukoencephalopathy

https://en.wikipedia.org/wiki/Human_metapneumovirus

https://en.wikipedia.org/wiki/Transformation_(genetics)

https://en.wikipedia.org/wiki/Mobile_genetic_elements

https://en.wikipedia.org/wiki/Transposable_element

https://en.wikipedia.org/wiki/Embryo

https://en.wikipedia.org/wiki/Extrachromosomal_DNA

https://en.wikipedia.org/wiki/Plasmid

https://en.wikipedia.org/wiki/Phagemid

CP

https://en.wikipedia.org/wiki/Subacute_sclerosing_panencephalitis

https://en.wikipedia.org/wiki/Respiratory_syncytial_virus

https://en.wikipedia.org/wiki/Follicular_dendritic_cell_sarcoma

https://en.wikipedia.org/wiki/Mumps

https://en.wikipedia.org/wiki/HIV

https://en.wikipedia.org/wiki/Genetic_recombination

BB

https://en.wikipedia.org/wiki/Mollicutes

https://en.wikipedia.org/wiki/Halspiviridae

CP

https://en.wikipedia.org/wiki/Plasmaviridae

https://en.wikipedia.org/wiki/Molluscum_contagiosum

Virus, Bacters; cell.

https://en.wikipedia.org/wiki/Category:Health_effects_of_tobacco

 Inflammation.

Stages of liver

https://en.wikipedia.org/wiki/Hepatitis

https://nikiyaantonbettey.blogspot.com/2021/09/09-04-2021-1628-grandma-rubes-world.html

above. Kesha cannibal

https://www.thepeoplehistory.com/toys.html

above. 

Bing Crosby - White Christmas (1942) Original Version

above. wade

1960s

 

https://www.familysavvy.com/coconut-sugared-popcorn-in-a-whirlypop/

Above. Scotland

Above. Scotland

Diphenidine

Legal status

https://en.wikipedia.org/wiki/Diphenidine

Arsphenamine, also known as Salvarsan or  compound 606, is a drug that was introduced at the beginning of the 1910s as the first effective treatment for syphilis and African trypanosomiasis.^[2] This organoarsenic compound was the first modern antimicrobial agent.^[3]

The structure of Arsphenamine has been proposed to be akin to the dimer azobenzene (A), but mass spectral studies published in 2005 suggest^[1] it is actually a mixture of the trimer (B) and the pentamer (C).

https://en.wikipedia.org/wiki/Arsphenamine

 It is chemically a 1-substituted-4-prenyl-piperazine derivative, 

https://en.wikipedia.org/wiki/AD-1211

Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobicmolecules to a protein or chemical compound. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed. Prenyl groups have been shown to be important for protein–protein binding through specialized prenyl-binding domains.

https://en.wikipedia.org/wiki/Prenylation

Myristoylation is a lipidation modification where a myristoyl group, derived from myristic acid, is covalently attached by an amide bond to the alpha-amino group of an N-terminal glycine residue.^[1] Myristic acid is a 14-carbon saturated fatty acid (14:0) with the systematic name of n-Tetradecanoic acid. This modification can be added either co-translationally or post-translationally.  N-myristoyltransferase (NMT) catalyzes the myristic acid addition reaction in the cytoplasm of cells.^[2] This lipidation event is the most found type of fatty acylation ^[3] and is common among many organisms including animals, plants, fungi, protozoans ^[4] and viruses. Myristoylation allows for weak protein–protein and protein–lipid interactions^[5]and plays an essential role in membrane targeting, protein–protein interactionsand functions widely in a variety of signal transduction pathways.

https://en.wikipedia.org/wiki/Myristoylation

Palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane proteins.^[2]The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments,^[3]as well as in modulating protein–protein interactions.^[4] In contrast to prenylation and myristoylation, palmitoylation is usually reversible (because the bond between palmitic acid and protein is often a thioester bond). The reverse reaction in mammalian cells is catalyzed by acyl-protein thioesterases (APTs) in the cytosol and palmitoyl protein thioesterases in lysosomes. Because palmitoylation is a dynamic, post-translational process, it is believed to be employed by the cell to alter the subcellular localization, protein–protein interactions, or binding capacities of a protein.

An example of a protein that undergoes palmitoylation is hemagglutinin, a membrane glycoprotein used by influenza to attach to host cell receptors.^[5] The palmitoylation cycles of a wide array of enzymes have been characterized in the past few years, including H-Ras, Gsα, the β2-adrenergic receptor, and endothelial nitric oxide synthase (eNOS). In signal transduction via G protein, palmitoylation of the α subunit, prenylation of the γ subunit, and myristoylation is involved in tethering the G protein to the inner surface of the plasma membrane so that the G protein can interact with its receptor.^[6]

https://en.wikipedia.org/wiki/Palmitoylation

The velvet worm (Onychophora) is closely related to arthropods^[73]

https://en.wikipedia.org/wiki/Arthropod

Peripatus
Scientific classification
Kingdom:	Animalia
Phylum:	Onychophora
Class:	Udeonychophora
Order:	Euonychophora
Family:	Peripatidae
Genus:	Peripatus Guilding, 1826
Species
See text

https://en.wikipedia.org/wiki/Peripatus