ANATOMY

Adenine & Thymine structure Adenine C5H5N5 (A) and thymine C5H6N2O2 (T) are complementary base pairs that form part of the DNA molecule. They are two of the four bases that make up DNA, along with cytosine (C) and guanine (G). Adenine and thymine pair by forming two hydrogen bonds between the two bases. The hydrogen bonds form between the electronegative oxygen atom on thymine and the slightly positive hydrogen on adenine the hydrogen bonds between adenine and thymine are important for DNA to maintain its double helix structure. In DNA replication and transcription, reactions often start at A-T rich sites because it takes less energy to break the two hydrogen bonds between A and T than it does to break the three hydrogen bonds between G and C. Adenine and guanine are double-ringed purines, while cytosine and thymine are smaller, single-ringed pyrimidines. These two bases form 2 hydrogen bonds uniting the electronegative O atom (on thymine) and N atom (on adenine) with the slightly positive exposed hydrogens on each molecule , we now conclude that it is essential to supplement with Hydrogen peroxide for the Hydrogen and Oxygen nucleic bonds also Activated Charcoal supplements because of the carbon backbone of the nucleobases Adenine is a purine characterized by its double ring structure Thymine is a pyrimidine characterized by single ring structure  
https://www.youtube.com/watch?v=gclpzqdV7hs
The Race to Sequence the Human Genome and What It Means | Retro Report
https://www.youtube.com/watch?v=BMfz506M-AY
Decoding Watson (2019) | Full Documentary | American Masters

Aorta The aorta is the main and largest artery in the human body, originating from the left ventricle of the heart, branching upwards immediately after, and extending down to the abdomen, where it splits at the aortic bifurcation into two smaller arteries (the common iliac arteries). The aorta distributes oxygenated blood to all parts of the body through the systemic circulation. Silica, a naturally occurring form of silicon dioxide, is a component of the aorta, a major artery in the body. Silica plays a role in maintaining the structural integrity of the aorta and is thought to be involved in preventing the development of atherosclerosis, a condition where plaque builds up in the arteries. Studies have shown that silicon content in the aorta can decrease with the progression of atherosclerosis, suggesting a link between silicon and cardiovascular health. Silica in the Aorta: The aorta, like other connective tissues, contains a significant amount of silicon, which is crucial for its structural integrity. This includes its role in synthesizing collagen and elastin, which are essential for the elasticity and strength of the aortic wall. Atherosclerosis and Silica: Research indicates that silicon levels in the aorta can decrease as atherosclerosis progresses. This reduction in silicon content parallels lipid infiltration, changes in elastic fibers, and alterations in the ground substance of the aortic wall. Potential Benefits: The antiatheromatous action of silicon has been explored, with studies suggesting that it can inhibit the development of atherosclerotic plaques and reduce lipid deposits in the aorta. Silicate Ions and Aortic Aneurysm: Recent research has focused on the use of silicate ions, a soluble form of silica, in treating aortic aneurysms and dissections. Studies have shown that silicate ions can alleviate these conditions by regulating the microenvironment of the aorta, reducing inflammation, and promoting cell health.  Hypertension and Silica: Soluble silica has also been found to suppress high blood pressure in spontaneously hypertensive rats and improve related aortic gene expressions. This suggests that silica may play a role in maintaining healthy blood pressure and vascular function. silica is 4 times higher in the aorta wall off children than seniors 

ATP the most important molecule in the body without ATP you would be dead in 30 seconds Adenosine triphosphate (ATP) is a nucleoside triphosphate that provides energy to drive and support many processes in living cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis. Found in all known forms of life, it is often referred to as the "molecular unit of currency" for intracellular energy transfer. When consumed in a metabolic process, ATP converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. It is also a precursor to DNA and RNA, and is used as a coenzyme. An average adult human processes around 50 kilograms (about 100 moles) daily. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base (adenine), the sugar ribose, and the triphosphate. order phosphorus from healthyhey.com they take a month to deliver but healthyhey.com delivers phosphorus no other company delivers phosphorus around the internet

Digestive organs God created the human body when he created Adam in the garden of Eden , in this video all digestive organs of the human body are explained in detail and their functioning is described. We will look at the salivary glands, the esophagus, the stomach, the small intestine, the large intestine and the liver with the gall bladder. Psalms 84:2 My soul longeth, yea, even fainteth for the courts of the LORD: my heart and my flesh crieth out for the living God.
https://www.youtube.com/watch?v=X3TAROotFfM
Human digestive system - How it works! (Animation)
https://www.youtube.com/watch?v=svkPGF0SbPA&t=9s
Digestive system

Immune system , the immune system is a network of biological systems that protects an organism from diseases. It detects and responds to a wide variety of pathogens, from viruses to parasitic worms, as well as cancer cells and objects such as wood splinters, distinguishing them from the organism's own healthy tissue. Many species have two major subsystems of the immune system. The innate immune system provides a preconfigured response to broad groups of situations and stimuli. The adaptive immune system provides a tailored response to each stimulus by learning to recognize molecules it has previously encountered. Both use molecules and cells to perform their functions. Nearly all organisms have some kind of immune system. Bacteria have a rudimentary immune system in the form of enzymes that protect against viral infections. Other basic immune mechanisms evolved in ancient plants and animals and remain in their modern descendants. These mechanisms include phagocytosis, antimicrobial peptides called defensins, and the complement system. Jawed vertebrates, including humans, have even more sophisticated defense mechanisms, including the ability to adapt to recognize pathogens more efficiently. Adaptive (or acquired) immunity creates an immunological memory leading to an enhanced response to subsequent encounters with that same pathogen. This process of acquired immunity is the basis of vaccination. Dysfunction of the immune system can cause autoimmune diseases, inflammatory diseases and cancer. Immunodeficiency occurs when the immune system is less active than normal, resulting in recurring and life-threatening infections. In humans, immunodeficiency can be the result of a genetic disease such as severe combined immunodeficiency, acquired conditions such as HIV/AIDS, or the use of immunosuppressive medication. Autoimmunity results from a hyperactive immune system attacking normal tissues as if they were foreign organisms. Common autoimmune diseases include Hashimoto's thyroiditis, rheumatoid arthritis, diabetes mellitus type 1, and systemic lupus erythematosus. Immunology covers the study of all aspects of the immune system.
https://www.youtube.com/watch?v=UZTf3OXJDWA&t=110s
Human Immune System - How it works! (Animation)

Kidneys God created the human body when God created Adam in the garden of Eden, in this video we take a look at the Kidneys which produce red blood cells and filter out waste fluids. 1 Corinthians 15:35-40 But some man will say, How are the dead raised up? and with what body do they come? 36 Thou fool, that which thou sowest is not quickened, except it die: 37 And that which thou sowest, thou sowest not that body that shall be, but bare grain, it may chance of wheat, or of some other grain: 38 But God giveth it a body as it hath pleased him, and to every seed his own body. 39 All flesh is not the same flesh: but there is one kind of flesh of men, another flesh of beasts, another of fishes, and another of birds. 40 There are also celestial bodies, and bodies terrestrial: but the glory of the celestial is one, and the glory of the terrestrial is another.
https://www.youtube.com/watch?v=AuTlwFreqlc
Kidney Failure
https://www.youtube.com/watch?v=CShAIAD-ask
How Your Kidneys Work
https://www.youtube.com/watch?v=SZ3BZBBC-Qc
How is urine produced in the body?KIDNEY, NEPHRON, BLADDER FUNCTION|Anatomy of the Urinary System

Red Blood cells , blood pressure video to prevent atherosclerosis take collagen iron & mineral supplements
https://www.youtube.com/watch?v=Ab9OZsDECZw
How blood pressure works - Wilfred Manzano

Regenerating bone
https://www.youtube.com/watch?v=ft4Xruv4A8w
Revolution in Bone Regeneration

Regenerative medicine Lee Spievak, a 69-year-old Ohio hobby shop worker, has apparently regrown his finger—over just four months!—after slicing off the top half-inch in the propellor of a model airplane (doctors were unable to attach the severed bit, as Spievak couldn’t find it after the accident). The newly grown replacement, which sprouted from the stump, is perfectly formed, and contains tissue, nerves, nail, skin and even a fingerprint. The treatment—a powder called extra cellular matrix—comes from the cells that line a pig’s bladder, and was invented by Dr Stephen Badylak from the University of Pittsburgh. Spievak’s brother Alan (who works in regenerative medicine) sent it to him to try out. Every day for 10 days, Spievak sprinkled a bit of this “pixie dust” on his finger. Apparently after just two applications, he saw a difference.
https://www.youtube.com/watch?v=h7wIZ7k1dmM
Limb Regeneration
https://www.youtube.com/watch?v=GwcT1ViM-hw
Regenerative Medicine: Re-Growing Body Parts

Tp53, also known as Tumor protein P53, cellular tumor antigen p53 , or transformation-related protein 53 (TRP53) is a regulatory protein that is often mutated in human cancers. The p53 proteins (originally thought to be, and often spoken of as, a single protein) are crucial in vertebrates, where they prevent cancer formation. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation. Hence TP53 is classified as a tumor suppressor gene. The TP53 gene is the most frequently mutated gene (50%>) in human cancer, indicating that the TP53 gene plays a crucial role in preventing cancer formation. TP53 gene encodes proteins that bind to DNA and regulate gene expression to prevent mutations of the genome. In addition to the full-length protein, the human TP53 gene encodes at least 12 protein isoforms.  Vitamin B6 activates Tp53 and elevates p21 gene expression in cancer cells and the mouse colon. The nutritional supplements taurine & Panacur Fenbendazole activates Tp53-dependent & independent tumor suppressor mechanisms in various cellular models of ovarian cancer. In vitro experiments have shown that vitamin C (ascorbic acid) can reduce cell proliferation and induce apoptosis through upregulation of Tp53, p21, and Bax and downregulation of Bcl-2 in T-cell colonies . Furthermore, Harakeh and colleagues demonstrated that the administration of nontoxic doses of ascorbic acid increased the expression of p53 . Vitamin C increases the ability of the anticancer drug bleomycin to produce DSBs, which makes cancer cells more dependent on functional DNA repair for survival . Vitamin B6 activates the p53 pathway, which is responsible for controlling p21 mRNA transcription in HT29, Caco2, LoVo, HEK293T, and HepG2 cancer cells. p21 mRNA levels were higher in the colon of mice fed a diet with adequate vitamin B6 than those fed a vitamin B6-deficient diet, and this may help to understand the antitumor effect of vitamin B6 via the activation of p53 and elevation of p21 mRNA . A previous study suggested that 1,25-dihydroxyvitamin D increased oxidative stress through inhibiting transcription of Nrf2, enhancing DNA damage and activation of p16/Rb and p53/p21 signaling in a 1α(OH)ase−/− mouse model . Folic acid (vitamin B9) might play an important role in the chemoprevention of gastric carcinogenesis. In humans, the tumor suppressor Tp53 expression in the gastric mucosa was significantly increased, while the expression of Bcl-2 oncogene protein decreased after folic acid supplementation . Furthermore, N-acetylcysteine (NAC) inhibits PDK1 expression through PPARα-mediated induction of p53 and reduction of p65 protein expression and unveils a novel mechanism by which NAC in combination with the PPARα ligand inhibits the growth of non-small-cell lung carcinoma (NSCLC) cells . β-Carotene, ascorbic acid, and vitamin E (α-tocopherol) protect against oxidative stress but reveal no direct influence on p53 expression in rats subjected to stress . In contrast, β-carotene exacerbates DNA oxidative damage and modifies p53-related pathways of cell proliferation and apoptosis in cultured RAT-1 fibroblasts exposed to tobacco smoke condensate (tar). Quercetin increased the phosphorylation of p53 protein and induced apoptosis of the human leukemia cell line in a dose-dependent manner . A recent study revealed that quercetin inhibits HeLa cell proliferation through cell cycle arrest at the G2/M phase and apoptosis induction through the disruption of mitochondrial membrane potential and activation of the intrinsic apoptotic pathway through p53 induction . Further, apigenin can induce p21, p53, and nonsteroidal anti-inflammatory drug-activated gene-1 (NAG-1) proteins in kinase pathways, including protein kinase C delta (PKCd) and ATM, which plays an important role in activating these proteins in colorectal cancer cell growth arrest. Further, kaempferol warrants as an antiangiogenetic agent, which reduced human umbilical vein endothelial cell viability-induced DNA damage and DNA fragmentation through activating the levels of caspase-3, caspase-8, and caspase-9 signaling, which were upregulated by ROS-mediated p53/ATM molecules following stimulations of p53 downstream protein levels of Fas/CD95, death receptor 4 (DR4), and DR5 . Another study revealed Acacetin, an O-methylated flavone, which can strongly inhibit tumor growth and induce tumor shrinkage in mice, which is closely correlated with its increasing p53 expression accompanied by decreased retinoic acid receptor gamma (RARγ) and reduced AKT activity in liver cancer cell lines . It was further reported that low Securin levels and high p53 levels play an important role in determining the sensitivity of human colon cancer cells to fisetin. Depletion of securin enhances fisetin-induced apoptosis and decreases the resistance of p53-deficient cells to fisetin and might be an attractive strategy for the treatment of human colon cancers . The inhibitory effect of fisetin against bladder cancer by activation of p53 and downregulation of the nuclear factor-kappa B (NF-κB) pathway in a rat bladder carcinogenesis model has been documented, which is a safe and efficacious agent and promising therapeutic approach for bladder cancer . Furthermore, Luteolin treatment increases the expression of p53 and p21 proteins and decreases the expression of MDM4 protein in both NSCLC cells and tumor tissues . Theaflavins induced G2/M arrest by modulating the expression of various proteins, which are involved in signaling. Moreover, theaflavins via p53 signaling inhibited Bcl-2 and interfered phagocytes via modulation of I-κB/NF-κB, as well as the expression of VEGF, and the phosphorylation of VEGFR was reduced in LNCaP cells . Furthermore, epigallocatechin-3-gallate activates p53-dependent downstream targets p21/WAF1 and Bax and downregulates NF-κB-dependent Bcl-2 that results in growth arrest & apoptosis in LNCaP cells . Our previous study revealed that effector proteins like Chk1, Chk2, and p53 were found to be phosphorylated in NNK acetate-treated BEAS-2B cells, and pretreatment with apple flavonoids showed a significant reduction in the levels of phosphorylation of ATR, Chk1, and p53 in NNK acetate-treated cells. Apple flavonoids protect BEAS-2B cells challenged against various carcinogens by assisting DNA repair mechanisms. Scientists link elephants' high resistance to cancer to their 20 copies of the p53 gene – the 'guardian of the genome' – compared with the single p53 gene found in other mammals.
https://www.youtube.com/watch?v=2RG9caushI0
The Role of p53 in Cancer
https://www.youtube.com/watch?v=6SjkIYClAkQ
p53 Tumour Suppressor (2016) by Etsuko Uno wehi.tv
https://www.youtube.com/watch?v=akALHORX9MY
What Goes Wrong in Cancer?

Sirtuins are a family of signaling proteins involved in metabolic regulation. They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. Chemically, sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2', the gene responsible for cellular regulation in yeast. From in vitro studies, sirtuins were thought to be implicated in influencing cellular processes like aging, transcription, apoptosis, inflammation and stress resistance, as well as energy efficiency and alertness during low-calorie situations. As of 2018, there was no clinical evidence that sirtuins affect human aging, and a 2022 review criticized researchers who propagate this claim. Yeast Sir2 and some, but not all, sirtuins are protein deacetylases. Unlike other known protein deacetylases, which simply hydrolyze acetyl-lysine residues, the sirtuin-mediated deacetylation reaction couples lysine deacetylation to NAD+ hydrolysis. This hydrolysis yields O-acetyl-ADP-ribose, the deacetylated substrate and nicotinamide, which is an inhibitor of sirtuin activity itself. These proteins utilize NAD+ to maintain cellular health and turn NAD+ to nicotinamide (NAM). The dependence of sirtuins on NAD+ links their enzymatic activity directly to the energy status of the cell via the cellular NAD+:NADH ratio, the absolute levels of NAD+, NADH or NAM or a combination of these variables. Sirtuins that deacetylate histones are structurally and mechanistically distinct from other classes of histone deacetylases (classes I, IIA, IIB and IV), which have a different protein fold and use Zn2+ as a cofactor. Recent findings imply that phytochemicals such as resveratrol, curcumin, quercetin, fisetin, berberine, and kaempferol may regulate the activity of sirtuins. Resveratrol mainly activates SIRT1 and indirectly activates AMPK.
https://www.youtube.com/watch?v=auuYUPx4uK4
How To Beat Cellular Aging | Sirtuins, NAD+ and Aging
https://www.youtube.com/watch?v=tjq6-FONcJA
The longevity sirtuin – what you need to know about SIRT6
https://www.youtube.com/watch?v=r0sj12JGDzE
All-Natural SIRT6 Longevity Supplement Pioneered & Verified By A Prestigious Professor
https://www.youtube.com/watch?v=gLFKQ-nAWdQ
Why SIRT6 Contributes To A LONGER LIFESPAN? | Dr Vera Gorbunova Clips

Sugar Phosphate structure Sugar phosphates C6H13O9P are carbohydrates that have a phosphate group attached to them. They are phosphoric acid esters of monosaccharides. Sugar phosphates are intermediates in carbohydrate metabolism and are found in nucleic acids, such as DNA and RNA. Glucose 6-phosphate: A sugar phosphate that can be formed when glucose is phosphorylated at the C primary hydroxyl group , Glucose 1-phosphate: A sugar phosphate that can be formed when glucose is phosphorylated at the C anomeric hydroxyl group , Deoxyribose phosphate: A sugar phosphate that is a constituent of nucleotides and nucleic acids ,Ribose phosphate: A sugar phosphate that is a constituent of nucleotides and nucleic acids Sugar phosphates are involved in the metabolic pathways of biosynthesis and degradation. They are also involved in the energy metabolism of cells Sugar phosphates (sugars that have added or substituted phosphate groups) are often used in biological systems to store or transfer energy. They also form the backbone for DNA and RNA. Sugar phosphate backbone geometry is altered in the vicinity of the modified nucleotides. The phosphodiester backbone of DNA and RNA consists of pairs of deoxyribose or ribose sugars linked by phosphates at the respective 3' and 5' positions. The backbone is negatively charged and hydrophilic, which allows strong interactions with water. Sugar-phosphate backbone forms the structural framework of nucleic acids, including DNA and RNA. Sugar phosphates are defined as carbohydrates to which a phosphate group is bound by an ester or an either linkage, depending on whether it involves an alcoholic or a hemiacetalic hydroxyl, respectively. Solubility, acid hydrolysis rates, acid strengths, and ability to act as sugar group donors are the knowledge of physical and chemical properties required for the analysis of both types of sugar phosphates. The photosynthetic carbon reduction cycle is closely associated with sugar phosphates, and sugar phosphates are one of the key molecules in metabolism,(Sugar phosphates are major players in metabolism due to their task of storing and transferring energy. Not only ribose 5-phosphate but also fructose 6-phosphate are an intermediate of the pentose-phosphate pathway which generates nicotinamide adenine dinucleotide phosphate (NADPH) and pentoses from glucose polymers and their degradation products.) oxidative pentose phosphate pathways, gluconeogenesis, important intermediates in glycolysis. Sugar phosphates are not only involved in metabolic regulation and signaling but also involved in the synthesis of other phosphate compounds.

Sugar phosphate backbone Sugar phosphates (sugars that have added or substituted phosphate groups) are often used in biological systems to store or transfer energy. They also form the backbone for DNA and RNA. Sugar phosphate backbone geometry is altered in the vicinity of the modified nucleotides. In a sugar-phosphate structure, the carbon atoms are located within the sugar molecule, specifically numbered 1', 2', 3', 4', and 5' (read as "one prime" to "five prime"), with the phosphate group attaching to the 5' carbon of the sugar molecule; essentially forming the "backbone" of a nucleic acid like DNA or RNA where the carbon atoms are part of the sugar ring structure. The sugar phosphate backbone is made of carbon that's why it's important to take activated charcoal as a supplement

Tau proteins (abbreviated from tubulin associated unit) form a group of six highly soluble protein isoforms produced by alternative splicing from the gene MAPT (microtubule-associated protein tau). They have roles primarily in maintaining the stability of microtubules in axons and are abundant in the neurons of the central nervous system (CNS), where the cerebral cortex has the highest abundance. They are less common elsewhere but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. Pathologies and dementias of the nervous system such as Alzheimer's disease and Parkinson's disease are associated with tau proteins that have become hyperphosphorylated insoluble aggregates called neurofibrillary tangles. The tau proteins were identified in 1975 as heat-stable proteins essential for microtubule assembly, and since then they have been characterized as intrinsically disordered proteins.
The tau hypothesis states that excessive or abnormal phosphorylation of tau results in the transformation of normal adult tau into paired-helical-filament (PHF) tau and neurofibrillary tangles (NFTs). The stage of the disease determines NFTs' phosphorylation. In AD, at least 19 amino acids are phosphorylated; pre-NFT phosphorylation occurs at serine 199, 202 and 409, while intra-NFT phosphorylation happens at serine 396 and threonine 231. Through its isoforms and phosphorylation, tau protein interacts with tubulin to stabilize microtubule assembly. All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments (PHFs) in the AD brain. Tau mutations have many consequences, including microtubule dysfunction and alteration of the expression level of tau isoforms. Mutations that alter function and isoform expression of tau lead to hyperphosphorylation. The process of tau aggregation in the absence of mutations is not known but might result from increased phosphorylation, protease action or exposure to polyanions, such as glycosaminoglycans. Hyperphosphorylated tau disassembles microtubules and sequesters normal tau, MAPT 1 (microtubule associated protein tau 1), MAPT 2 and ubiquitin into tangles of PHFs. This insoluble structure damages cytoplasmic functions and interferes with axonal transport, which can lead to cell death. Hyperphosphorylated forms of tau protein are the main component of PHFs of NFTs in the brain of AD patients. It has been well demonstrated that regions of tau six-residue segments, namely PHF6 (VQIVYK) and PHF6* (VQIINK), can form tau PHF aggregation in AD. Apart from the PHF6, some other residue sites like Ser285, Ser289, Ser293, Ser305 and Tyr310, located near the C-terminal of the PHF6 sequences, play key roles in the phosphorylation of tau. Hyperphosphorylated tau differs in its sensitivity and its kinase as well as alkaline phosphatase activity and is, along with beta-amyloid, a component of the pathologic lesion seen in Alzheimer disease. A recent hypothesis identifies the decrease of reelin signaling as the primary change in Alzheimer's disease that leads to the hyperphosphorylation of tau via a decrease in GSK3β inhibition. A68 is a name sometimes given (mostly in older publications) to the hyperphosphorylated form of tau protein found in the brains of individuals with Alzheimer's disease. In 2020, researchers from two groups published studies indicating that an immunoassay blood test for the p-tau-217 form of the protein could diagnose Alzheimer's up to decades before dementia symptoms were evident. Autophagy clears up misfolded tau proteins
https://www.youtube.com/watch?v=izRAjlx876Y
Tau Protein Pathology in Alzheimer's Disease
https://www.youtube.com/watch?v=vtOKJequi3A
A new perspective on the role of phosphorylation in Alzheimer’s and other tau pathologies

Telomerase are made of Nitrogen Hydrogen Oxygen & phosphorus make sure to supplement in order to increase your telomeres Telomerase, also called terminal transferase, is a ribonucleoprotein that adds a species-dependent telomere repeat sequence to the 3' end of telomeres. A telomere is a region of repetitive sequences at each end of the chromosomes of most eukaryotes. Telomeres protect the end of the chromosome from DNA damage or from fusion with neighbouring chromosomes. The fruit fly Drosophila melanogaster lacks telomerase, but instead uses retrotransposons to maintain telomeres. Telomerase is a reverse transcriptase enzyme that carries its own RNA molecule (e.g., with the sequence 3′-CCCAAUCCC-5′ in Trypanosoma brucei) which is used as a template when it elongates telomeres. Telomerase is active in gametes and most cancer cells, but is normally absent in most somatic cells. The existence of a compensatory mechanism for telomere shortening was first found by Soviet biologist Alexey Olovnikov in 1973, who also suggested the telomere hypothesis of aging and the telomere's connections to cancer and perhaps some neurodegenerative diseases. Telomerase in the ciliate Tetrahymena was discovered by Carol W. Greider and Elizabeth Blackburn in 1984. Together with Jack W. Szostak, Greider and Blackburn were awarded the 2009 Nobel Prize in Physiology or Medicine for their discovery. Later the cryo-EM structure of telomerase was first reported in T. thermophila, to be followed a few years later by the cryo-EM structure of telomerase in humans. The role of telomeres and telomerase in cell aging and cancer was established by scientists at biotechnology company Geron with the cloning of the RNA and catalytic components of human telomerase and the development of a polymerase chain reaction (PCR) based assay for telomerase activity called the TRAP assay, which surveys telomerase activity in multiple types of cancer. The negative stain electron microscopy (EM) structures of human and Tetrahymena telomerases were characterized in 2013. Two years later, the first cryo-electron microscopy (cryo-EM) structure of telomerase holoenzyme (Tetrahymena) was determined. In 2018, the structure of human telomerase was determined through cryo-EM by UC Berkeley scientists.
https://www.youtube.com/watch?v=i6nE6gUp2cw
Telomerase Function - Animation
https://www.youtube.com/watch?v=wf6QiIlGxSg
Telomerase Replication in Eukaryotes | End Replication

The Krebs cycle The citric acid cycle—also known as the Krebs cycle, Szent–Györgyi–Krebs cycle, or TCA cycle (tricarboxylic acid cycle)—is a series of biochemical reactions to release the energy stored in nutrients through the oxidation of acetyl-CoA derived from carbohydrates, fats, proteins, and alcohol. The chemical energy released is available in the form of ATP. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a "cycle", it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized. The name of this metabolic pathway is derived from the citric acid (a tricarboxylic acid, often called citrate, as the ionized form predominates at biological pH[6]) that is consumed and then regenerated by this sequence of reactions to complete the cycle. The cycle consumes acetate (in the form of acetyl-CoA) and water, reduces NAD+ to NADH, releasing carbon dioxide. The NADH generated by the citric acid cycle is fed into the oxidative phosphorylation (electron transport) pathway. The net result of these two closely linked pathways is the oxidation of nutrients to produce usable chemical energy in the form of ATP. In eukaryotic cells, the citric acid cycle occurs in the matrix of the mitochondrion. In prokaryotic cells, such as bacteria, which lack mitochondria, the citric acid cycle reaction sequence is performed in the cytosol with the proton gradient for ATP production being across the cell's surface (plasma membrane) rather than the inner membrane of the mitochondrion. For each pyruvate molecule (from glycolysis), the overall yield of energy-containing compounds from the citric acid cycle is three NADH, one FADH2, and one GTP.
https://www.youtube.com/watch?v=ubzw64PQPqM
KREBS CYCLE MADE SIMPLE - TCA Cycle Carbohydrate Metabolism Made Easy
https://www.youtube.com/watch?v=JOncWQUpMzc
Krebs Cycle | Made Easy!
https://www.youtube.com/watch?v=juM2ROSLWfw
Krebs / citric acid cycle | Cellular respiration | Biology | Khan Academy
https://www.youtube.com/watch?v=Lf4irlyN1eE
Metabolism Overview