Untitled Flashcards Set

  1. Primary vs secondary transduction

    1. Primary: bringing things outside of the cell to inside (uses signal info from outside+ Receptor)

    2. Secondary: intracellular proteins and secondary messengers bring it to target proteins

  2. Differences between mitochondrial and nuclear genome: mitochondrial has different stop codons and it’s smaller than the nuclear genome

  3. Components of glycocalyces: glycoproteins, proteoglycans, glycolipids

    1. glycocalyces: thick, fibrous, and hydrated meshwork of carbohydrates and proteins that covers the surface of cells

  4. Components of the Plasma membrane: Phosphatidylserine, Cholesterol, Caveolin

  5. What are the steps in mRNA splicing?

  6. What is polyadenylation and what deos it use?

    1. Adding a poly-A- tail with AAUAAA hexanucleotide

  7. Why are introns removed in splicing? They have low complexity

  8. What position does position 3 of the anticodon correspond to? Position 1 on the codon

  9. What causes changes in supercoils? Breaks or nicks, NOT HISTONES

  10. What kind of RNAs don’t have 7- methyl guanosine cap? tRNA

  11. What is Sphingomyelin? It’s a major phospholipid located on the plasma membrane

  12. What are Lipid rafts? small, dynamic areas in the plasma membrane that are rich in cholesterol and sphingolipids

  13. What are LDL receptors? Low density lipoproteins, this is associated with receptor dependent endocytosis

  14. Functions of lysosomes? 1. Degradation of components acquired from late endosomes , Degradation of phagosomes (in some cell types) , and Degradation of autophagosomes (in all cells)

  15. Where does catalase activity occur? In peroxisomes

  16. What are the only amino acids that have one codone? Tryptophan (UGG) and methionine (AUG)

  17. What are the different phases in clinical trails?

    1. safety with small sample size

    2. does it work? with small sample size

    3. Does it work? with double blind

    4. Post market surveillance with lts of poeple, would find out potential rare adverse side effects from here

  18. Half life is relevant to 1st order kinetics

  19. What are the only tissues that respond to insulin? Muscles with glut 4

  20. almost all methyl transferases int embody use? SAM

    1. EXCEPT homosytene to methionine (B12 and THB)

    2. Lysosomal enzymes partition within the late endosome a new vesicle buds from it, and a lysosome is formed.

  21. For a man with 70kg man with 42L body water, what are the following Vd and its association?

    1. higher Vd= more stuff in the cell, less stuff in the plasma

    2. The following numbers= where the drug is retained

      1. > 5Vd= drug is found in the plasma/ intervascular space

      2. 14= drug is in the extra cellular space (interstitial and vascular space)

      3. >40L= drug is in the body resevuar (tissue aka intercellular)

  22. Excreetion vs elimination

    1. elimination= not being used (metabolism and excretion)

    2. excretion= gone of body via pee pee

  23. In drug stuff, about Css

    1. 5 Half lives= until how long to get to Css

    2. Css formulas how to figure out how much Css there is

    3. Once you his steady state (after 5 half lives) plasma concentration= Css

  24. Galactocerebroside: primarily found in the nervous system and kidney.

  25. GM1 ganglioside: type of Glycolipid that serves as the receptor for cholera toxin in the gut and E. Coli heat labile enterotoxin

  26. GM2 ganglioside is primary found in nervous system

  27. What type of molecules are allowed to transverse the bilayer?  small nonpolar molecule (ex: O2)

  28. Glycocalyces: thick carbs on the outside of the cell. They allow for cellular adhesion and therefore the “catching” of neutrophils

  29. Lipid Rafts: role in signal recognition

  30. What is Nalidixic acid and what does it do?

    1. it blocks bacterial gyrase—> block DNA replication or transcription

    2. Also associated with Ciproflaxin to do the same job

    3. has no impact on eukaryotes

  31. is the coming sequencing of mRNA the same as the sense or antisense?

    1. same as the sense part of DNA but instead of T there’s U

  32. What are the subunits in DNA pol I? klenow fragment (no 5’ exonuclease) which is used for removing RNA primer (Okazaki fragments)

  33. What are the subunits in DNA Pol II? single subunit

  34. What are the subunits in DNA pol III? dnaG (primate/ RNA polymerase),alpha epsilon not core

  35. What are the subunits of RNA polymerase? omega subunit (promotor recognition)

  36. What is the function of DNA Pol I? DNA repair (filling in gaps for lagging strand)

  37. What is the function of DNA POL II? unkonwn, maybe editing in DNA replication?

  38. What is the function of DNA POL III? leading and lagging strand synthesis

  39. What is the function of RNA polymerase? RNA synthesis

  40. What does 3ʹ to 5ʹ exonuclease activity do? proofreading

  41. What is needed for Telomerase to function? TERC (Telomerase Reverse transcriptase) and TERC (RNA complex)

  42. What causes suppression of transcription? deacetylation of histones and methylation of DNA

  43. What causes enhancement of transcription? acetylation of histones and demethylation of DNA.

  44. What does the Retinoblastoma protein (RB or pRB) suppresses? the G1–S phase transition

  45. What transcription factors bind to “AAUAAA” for polyadenylation?CPSF-30 and WDR33 

  46. What binds to the cleavage site where Poly A polymerase adds adenosine?CPSF-73 

  47. What is the fucniton of PABPN1? regulate the length of Poly A tails

  48. What binds to the GUUGU region? CstF-64

  49. What is the lariat structure? It’s involved in Intron Splicing and formed by 2’A-5’G binding in a nuetrophillic attack

  50. What is the shine delargo sequence? AGGAGGU

  51. Radial spoke protein function: connects the outer and inner microtubule doublets, contributes to bending and general coordination/ regulation of the beating cycle

  52. Inner and outer Dynein arms function: connect to the (-) end of the adjacent outer microtubule doublet and “pull” to initiate motion

  53. Nexin function: connects outer microtubule doublets together

  54. What is Epidermolysis Bullosa associated with? Intermediate Filament- Cytokeratin

  55. What is Bullous Pemphigoid associated with? Intermediate Filament- BP230

  56. What are stress fibers? microfilament complex found near the plasma membrane of non-muscle cells. They are abundant in the endothelial cells of large arteries, the aorta being a great example.

  57. Alpha Actin function: structural and regulatory roles in cytoskeleton organization and muscle contraction

  58. What organelle is in charge of drug detoxification? the smooth ER

    1. What happens when it want to detoxify something? It enlarges

  59. What’s the process of cargo trafficking from the ER—> Golgi and back

    1. ER—> Golgi: uses COPII and Dyeinin to move things

    2. Golgi—> ER: uses COPI and Kinesin to move things

  60. What is Zellweger Syndrome? mutation in genes encoding transporters and receptors necessary to get proteins into the peroxisomes. 

  61. What is X-linked Adrenoleukodystrophy? mutation in the ADL gene which is used in peroxisomes to import enzymes that break down long chain fatty acids

  62. What does the tethering protein bind to? the Rab G on the vesicle encasing protein

  63. What does the v-snare bind to? The v-snare on the vesicle binds to the t-snare on the target membrane

  64. What is familial hypercholesterolemia: issue with a defective LDL receptor on the cystolic side--> can’t recruit Adaptins or Clathrins

  65. Regulated pathway vs Constitutive pathway:

    1. Regulated: cells that need a specific receptor in order to be secreted via exocytosis. Ex: Mass cell/ Ige

    2. Constitutive: always being expressed

  66. mTor function: negatively regulated macroautophagy

    1. Raamycine is used for cancer treatment

    2. Insulin and IGF are used as signals

  67. What residues does Ubiquitin Ligase (E3) add ubiquitin molecules to at the degradation site of the substrate protein? Lysine

  68. What does cancer need to survive? Lots of proteosome activity

    1. What inhibits this? Bortezomib and Carfilzomib

  69. What decreases the plasma membrane fluidity if added to the plasma membrane? Cholesterol

  70. Supercoiling steps: 

    1. using topoisomerase to break one or both DNA strands. 

    2. induce negative supercoiling by ATP hydrolysis followed by rejoining of DNA strands.

  71. What favors renaturation? lower temperatures, High salt concentration, high GC content, and increased C0T

  72. What adds negative supercoiling upstream to reduce stress or tension in the DNA? Gyrase in prokaryotes and Topoisomerase in prokaryotes

  73. What’s the function of Deacetylases? To remove acetyl groups—> tightly bound chromatin—> decreased transcription levels. If there’s an issue in deacetylases—> increased acetyl groups—> increased transcription

  74. Where is the Poly A tail added? between the upstream sequence element (AAUAAA) and GUUGUU. 

  75. What enzymes are needed for something to enter the Mitochondrial matrix? TOM and TIM, both layers separate the outside of the mitochondria to the mitochondrial matrix

  76. What is the process of ATP generation: H+ goes through the Intermembrane space to the Mitrochondrial matrix via the F0 part of ATP Synthase located in the IMM. The ATP generated leaves the mitochondria via an anti porter (exchange ADP for ATP)

  77. How many different Energy molecules are needed for each step in translation? 4 moles of ATP needed to charge amino acids on tRNA, 1 GTP brings charged tRNA to ribosome, and 1 GTP does translocation or movement from A site to P site or P site to E site or E site to exiting initiation complex. 

  78. What is Mechanical Integrity associated with? Intermediate filaments are needed to maintain positioning and structural support of the cell

  79. What is the correct order of the forward trafficking path? ER—> VTC—> cis Golgi—> trans Golgi

  80. What are the different types of storage diseases? Tay- Sash’s, Gaucher’s Niemann Pick, Hurler’s, and Huntington’s

  81. Which pathways use serine/ Threonine kinase: Ras signaling (MAP), TGF-B, and Wnt signaling

  82. Which pathway is tyrosine kinase associated? JAK- STAT

  83. What pathways is activated by GPCR: Hippo and Ras

  84. What inhibits PRP Synthase? ADP and GDP

  85. What’s the main difference between Kelley- Seegmiller and Lesch Nyhan? Lesch Nyhan has self harm and Kelley- Seegmiller doesn’t Kelley- Seegmiller also usually doesn’t have elevated Serum uric acid levels

  86. An issues with the PRPP synthase is what type of mode of inheretance? It’s X- linked recessive

  87. What is the relation of protonated and ionized things in weak acids and bases? Main Takeaways: PH=PKa+ Log (X/HX) between acids and bases

  88. List al the pharmacist equations?

  90. What’s the difference between Kelly Seegmiller and Lesh Nyan? 

    1. Both: gout, hyperuricemia, and renal stones

    2. Lesh Nyhan=  only one with neurological defects

  91. What is the translation initiation for Prokaryotes vs Eukaryotes: Prolaryotes use Shine Delgado; Eukaryotes use AUG

  92. Difference between Eukorates and Prokaryotes for DNA replication: Eukaryotes= greek letter, prokaryoptes= DNA polI, DNA pol II, and DNA pol III

  93. Where are mitochondrial proteins found? In the Inner membrane

    1. only H+ are in the inter membrane space

  94. Describe the Amphiatic property of the plasma membrane: polar on the outside and nonpolar on the inside

  95. Where do phospholipids diffuse: within their own leaflet (they don’t flip)

  96. Location of Phosphoatidylinositol: minor phospholipid of the inner leaflet

  97. What are Glycolipids and where are they found?

    1. derived from sphingosine, in outer leaflet

    2. Function: form part of Glycocalyx

    3. Ex: galactocerebroside and GM1

  98. What are the integral membrane proteins: transmembrane protein and Covalently attached proteins

    1. Ex: GPI- anchored= type of covalent protein, attached to the outer part that becomes part of lipid rafts. It’s attached to the glycosylphophatidylinositol core in the ER

  99. What kind of protein can be removed from the membrane? Peripheral membrane proteins

  100. What are the different special membrane domains?

    1. Lipid rafts: lots of phospholipids, cholesterol, glycolipids

      1. fnx: receptor signaling and nutrient absorption in the intestines

    2. Caveolae: work in endocytosis/ transcytosis—> scaffold for signaling pathways

    3. Glycocalyx: carb rich on the outside of the membrane, anything with glyc0- in it is in it+ proteoglycans. 

      1. Fnxn: Binds to food particles in the intestine, cell recognitions and protection from the environment

  101. What type of membrane protein is associated with AD? Lipid rafts, they promote AB formation

  102. How do viruses enter the cell? on lipid raft assoiciated receptors/  (HIV) or they bud off the cell via lipid rafts (SARS- CoV-2)

  103. What’s an example of the Oligosaccharide structure? Glycocalyx

  104. What are Nucelic acids connected by? and what’s special about the 1st nucleic acid?

    1. It’s connected by Phosphodiester bonds and the 1st one has a 5’triphosphate (ppp)

  105. Nucleoside vs Nucleotide? Nuceloside= sugar and base; nucleotide= sugar+ base + phosphate

  106. What deos miRNA do? regulates gene expression?

  107. tRNA def? transfer adaptor between mRNA and AAs in protein synthesis

  108. What’s used to wind/ unwind DNA with ATP hydrolysis?

    1. Prokaryote: DNA gyrase

    2. Eukaryote: Topoisomerase I and II (1= 1nick; 2= 2 breaks)

  109. Does breaking bonds require the use of ATP? NO

  110. When does DNA denaturation happen? high temperatures, low salt concentrations, and low GC

  111. when does DNA renaturation happen? low temp, high salt concentration, and high GC

  112. What is the exception to the Eukaryotic chromosomes being linear? Mitochondrial chromosomes are circular and maternally inherited

  113. What is a Primase and what does it do? makes short RNA fragments for DNA Pol III to build onto

    1. Prokaryotes:DNA pol 1

    2. Eukaryotes: RNase H

  114. What’re the subunits for DNA Pol III and RNA Pol? DNA Pol III—> primate subunit; RNA pol—> sigma subunit

  115. Are DNA Pol A and B eukaryotic or prokaryotic? What are their functions? 

    1. Eukaryotic

    2. A= primate activity, functions in early replications

    3. B= DNA repair

  116. What do the following different mutations lead to?

    1. Spontaneous—> tautomeric shift (chemical changes)

    2. Radiation—> ionizing (X rays and etc)

    3. UV—> Thymine dimers

  117. Abilities of DNA Pol: DNA polymerization, 3—>5 exonuclease (proofreading), 5—> 3 exonuclease (removes okazaki fragments

  118. Types of DNA repair

    1. normal (excision) with DNA pol

    2. Spurinic/ cytidine deamination: DNA glycosylase and AP endonuclease

  119. What is the telomerase sequence and when is used? What are the components?

    1. TTAGGG, used for tagging at chromosomes

    2. Components: TERT and TERC

  120. What are the difference between Eukaryote and Prokaryote RNA polymerase?

    1. Prokaryote: RNA polymerase and dang (primer)

    2. Eukaryote: 

      1. RNA pol I: 

      2. RNA pol II: all have 5’ caps

      3. RNA pol III: has no cap, has a part of SRP

  121. What are the promotors for transcription regulation: TATA BOX (upstream of mRNA), CCAAT, and housekeeping box (GC)

  122. What doe enhancers not depend on? Orientation and distance independent

  123. What’s the Euk transcription initiation process?

    1. TFIIB+ TFIID BIND To TATA BOX—> preinitiation complex forms

    2. RNA pol II + TFIIF —bind to it> Initiation complex formation

    3. TFIIE/ TFIIH bind to it —> phosphorylate complex forms

  124. How do enhancer/ repressor binding proteins work? they recruit TFs to the strata site, by binding as dimers

  125. How do histones increase/ decrease transcription

    1. acetylation—> increase transcription

    2. methylation—> decrease transcription with cystonine residues

  126. What does pRB do normally? repress Cyclin D1 surpassing the cell cycle

  127. What sanctions make up the nonprosessing section of the genome? LINES, SINES, AND INTRONS

  128. What are the steps of Polyadenylation? btw only happens in eukaryotes

    1. recognize AAUAAA (signal) and GU rich area, then celaves between it

    2. add 250 As at the 3’ end

  129. What are Purine rings assembles from? Glutanmine, glycine, aspartate, and formyl THF 

  130. What does HGRT catalyze? the process of hypoxanthine—> IMP and guanine—> GMP

  131. What are Pyrimadine rings assembles from? glutamine and aspartate (PRP is added after the ring is formed)

  132. Hereditary Orotic Acidurea? mutation in pathway of OMP—> UMP 

    1. —> pyrimidine deficiency and increased orotic acid crystals

  133. Pyyrimadine pathway synthesis? carbonyl phsophate+ aspartate—> rotate—> OMP+ PRPP—> UMP

  134. What are the enzymes involved in purine degradation? adenosine deaminase and xanthine oxidase

  135. What are the important enzymes for pyrimidine degradation? Dihydropyrimidine Dehydrogenase (DPD)

    1. it’s degraded into water soluble AAs

  136. DPD deficiency? autosomal recessive—> pyrimidine accumulation

  137. Adenosine Deaminase (ADA) deficiency?—> imunodeficince—> lack of functional T and B cells

  138. What’s the main function for the mitochondrial inner membrane? store proteins and maintain electrochemical gradient

  139. What are the different subunits in the ATP synthase complex?

    1. F0= transmembrane channel (H+ moves through)

    2. F1: rotor subunit that generates ATP

  140. What are some other mitochondrial function? steroid synthesis, cellular apoptosis, and Ca+ collection

  141. What are the functions of the following mitochondrial transport proteins

    1. N terminus signal sequence: targets proteins to mitochondria

    2. Chaperone proteins: asset the process and refold proteins when in the matrix

  142. MERF? t RNA mutation, epilepsy associated

  143. MELAS?stoke/ seizure related

  144. Function of peroxisome? Long chain FA, and degrading toxic molecules via H removal

  145. ADL? issues with degrading long chain FA b/c the long chain FA can’t enter the peroxisomes

  146. What codon codes for Ile? AUA

  147. What condone codes for Trp? UGG

  148. What’s the process for Prokaryotic translation?

    1. IF1 and IF3 bind to small subunit (30s) and prevent the ribosomal subunits from associated

    2. IF2 with GTP kicks of IF3—> association of Met with the small ribosome

    3. large subunit (50s) binds removing IF1 and IF2—> imitation complex forms

    4. elongation= by peptide transferase

  149. What’s associated with the Mitochondrial 12S rRNA mutation? sensorineural defense because of amino glycoside antibiotics

  150. What are the important parts of eukaryotic translation initiation? adding of the 5’ 7methyl G cap and Kozak sequence next to the start codon

  151. What causes mosaicism? mitotic nondisjunction

  152. What key term is associated with Edwards syndrome? rocker bottom feet

  153. What percentage increase is cause by chromosomal translocation? 33%

  154. What is a deletion for Digeorge? 22q11.2 deletion

  155. What’s a chromosome 5 deletion? Sri du chat

  156. What’s a chromosome 7 deletion? William’s which is associated with a broad forehead, connective tissue, and join issue

  157. What kind of genetic issues is MD? X linked recessive

  158. What kind of genetic issue is Lesch Nyhan? X linked recessive

  159. Where are the SRY region located?near the PAR, activated by SF-1 and blocked by DAX-1

  160. What’s a triplet expansion disorder? higher than 3 nucleotide—> diseased phenotype. Shows anticipation

  161. What’s a diseases is associated with a gain of function mutation? Huntington’s because it’s autosomal dominance

  162. What kind of disorder is Myotonic dystrophy?

    1. autosomal dominant

    2. triplet expansion CTG on the DMTK gene

  163. Epigenetic def: heritable alteration of gene expression without changing DNA sequence

  164. What are the exceptions to HWP: Heterozygote advantage and Founder effect

  165. What are microtubules made of? Hollow rods with 13 profillaments, and a/b tubing heterodimers

  166. Function of paclitaxel? anticancer drug that halts cell division by stabilizing the mitotic spindle—> preventing depolarization 

  167. Function of Vincristine? anticancer drug that depolymerize mitotic spindle microtubules

  168. What do MTs make up? cilia (making mucus from lungs) and flagella (sperm motility)

    1. Structure: axone (9+2 arrangement) is made up of a radial spoke protein and axonemal dyeing—> whipping motion

  169. Primary Cilliary Dyskinisea? issue with radial spoke/ dyeing mutation—> frequencyt respiratory tract infections

  170. Abberent mitosis? —> cancerous growth b/c 2/ more spindle poles b’c of too many centrosomes

  171. What ar einvaidasomes and what are the different types? have Mrs to degrade ECM

    1. podosome: many, short lived, and invasive

    2. invadopodia; few, long- lived, and more invasive

  172. What deos dystrophin bind to? actin

  173. What are the different Intermediate filament subunits

    1. I= keratin

    2. 2= keratin

    3. 3= vimenten (fibroblasts), desmin (muscles), GFAP (glial cells)

    4. 4= Nuero filaments (in nuerons)

    5. 5= Nucelar lamins (in nuclei)

  174. Where does Phospholipid synthesis happen? Cystolic leaf of the ER, which is evenly distributed through scrambalase

  175. Where and how does Cholesterol synthesis happen? In the SER and RER via denovosynthesis (using HMG reductase and Cofactor A, which is the target of statin drugs)

  176. SER functions

    1. prosisome ans autophagosome generation

    2. drug detoxification via cytochrome P450

    3. Steroid hormone via cytochrome P450

    4. Calcium release and uptake

  177. what do Cytochrome P450 enzymes do? Alter chemical into carcinogens (aflatoxin and Penzo[a]pyrene

  178. What’s the process of protein synthesis

    1. small ribosome binds and Met tRNA which binds to mRNA

    2. Large unit binds

    3. SRP can halt translation if it meets the signal so that it can move the protein synthesis into the RER

      1. it moves by binding to SRP Rc+ a translator protein

    4. If SRP moves it halfway into the RER membrane it becomes an integral membrane protein and transmembrane protein (multi or single pass)

  179. What things are involved in protein folding in the ER? BiP acts as a chaperone but the major protein folding happens by Calnexin and Calreticulin

  180. What things drive the Glycosylation reactions in the ER? N acetyl glucosamine, mannose, and glucose

  181. What is the KDEL sequence an example of? a AA sipcode that tells the details of the appropriate destination of the protein

  182. CYP2D6: a type of cytochrome P450 enzyme

    1. involved in coding, some people can be an ultratapid metabolizer—> extreen effects of the drug

  183. What are the things proteins involved in vesicle transport?

    1. Tethering, Rab, and SNARE

      1. Tethering recognizes Rab on the Vessicle and uses that to bring the vesicle closer to the membrane

      2. the v-Snare on the vessicle and t-Snare on the target membrane bind—> vessicle fusion with the membrane

  184. What accomplishes membrane recycling? The constitutive pathway and a mix of ends and exocytosis

  185. What part of Receptor mediated endocytosis requires ATP? When the clatherine coat breaks off

  186. Atherosclerosis? LDL receptor mutation prevents Rc endocytosis of LDL—> LDL accumulation —> atherosclerotic plaques in vessels

  187. Early end-some pH vs Late end-some pH: early= 6-6.5; late= 5-5.6

  188. What does constitutive secretion do and what’s the process: Purpose: renew cell’s PM

    1. Trans face of Golgi (clatherin and dynamic used in budding)—> microtubule transport with kinesis—> PM via actin in myosin

  189. What are carrier proteins: do conformational change to move things, can be passive or active

    1. uniport, symport, antiport

  190. What in lysosome allows for degradation, and what kind of degradation is done? Acid hydrolases, does degradation of organelles and long- lived proteins

    1. inactive by neutral pH

  191. Difference between primary and secondary lysosomes? homogenous= primary; heterogenous= secondary and residual bodies

  192. Lysosome biosynthesis:

    1. Lysosomal enzymes are synthesized in the RER and processed in the cis and medial Golgi compartments. 

    2. Mannose-6-phosphate moieties are added in the Golgi apparatus

    3. Mannose-6-phosphate receptors in the trans-Golgi network bind to the lysosomal enzymes, these vesicles form and travel to the late endosomal compartment and M-6-P receptors recycle back to the TGN(trans-Golgi Network).

  193. What is Macrophage involved in?

    1. active in starvation (cells eat themselves)

    2. cancer (help tumor survive)

    3. wasting disease- dystrophy and Parkinson (cell die because of macroautophagic loss of organelles)

  194. What are the different lysosomal storage diseases? Tay- Sash’s,, Gaucher’s, Neimann- Pick, Hurler’s, and Hunter’s

  195. What’s I-Cell disease?

    1. they don’t get M6P tags—> lysosomal enzymes are secreted—> lack of lysosomal enzymes—> bad lysosomes—> inability to degrade it appropriately

  196. what kind of degradation is done in proteosomes? short lived protein degradation

  197. Structure of proteosomes? Hollow cylindrical central core with 2 caps on the end, the protease active site faces

  198. mechanism of Proteosome action?

    1. E1 uses ATP to activate Ubiquitin—> E2 and E3 binds (ubiquitin ligase)—> add ubiquitin molecules to attach and protein breakdown

    2. Ubiquinine ligase can become activated by phosphorylation, ligand binding, or by adding a subunit

  199. How can Kinase phosphorylation cause protein degration? It can unmask specific domains—> destabilization of the N terminus

  200. How does Chemotherapy work? normally proteosome activity is enhanced by tumor survival—> Chemotherapy target proteosomes toinhibit their activity

  201. How does Limb Girdle MD work?  dyferlin mutation—> worsening MD

  202. What do cell surface receptors vs intracellular receptors bound to? cell surface receptors= binds to hydrophilic; intracellular receptor=binds to hydrophobic

  203. What is a 7 pass receptor? G protein

  204. What is a single pass receptor? enzyme linked 

  205. When does the a- subunit? become inactive? after the target molecule is done being activated

  206. Ca+ signaling pathway:

    1. a subunit—> activates Phospholipase C—> PIP2 activation—> celaving of IP3 and DAG—> IP3 opening Ca+ on Er —> Ca+ release from ER—> help DAG activate PKC

    2. Ca+ binds to calmodulin—> CAM kinase

  207. What are the SRC domains and how are they activated?

  1. What are the different FDA ratings for drug safety

    1. A= no fetus risk

    2. B= no fetus risk in animals (no women)

    3. C= animal studies shows adverse, no women studies

    4. D= human fetal risk

    5. E= fetal abnormalities

  2. Info about Intramuscular drug amin route? slower than IV, no 1st pass effect

  3. Acids are more likely to be ___ at ___ pH

  4. Bases are more likely to be ___ at ___ pH

  5. Large organs have ___ uptake of drugs becasue there’s a ___ gradient between the organs and blood

  6. Warafin—> drug accumulation in ___?  binds to plasma albumin—> increase concentration in vascular

  7. Chloroquine—> drug accumulation in ___?  binds to proteins albumin—> decreased drug concentration in vascular

  8. What’s usually in bone reservoirs? tetracycline antibiotics and heavy metals—> bone crystal lattice 

  9. What are the different plasma concentrations for different compartments? extracellular= 4L, interstitial= 10L, and intracellular = 28

  10. What happens in Phase 1 drug metabolism reactions?

    1. redox reactions

    2. incrase/ decrease drug effectiveness

    3. 1st pass metabolism

    4. CY3A4/5 + other cytochrome P450 enzymes

    5. cytochrome P450 enzymes are inhibited by cimetidine

  11. What happens in Phase 2 drug metabolism reactions?

    1. UGT= main enzyme

    2. drug conjugation for water soluble enzymes

  12. What drugs undergo mixed order kinetics?

    1. phenytoin and aceylsalic acid

    2. drug rate= proportional at low dose

    3. drug rate= constant at high dose

  13. Why is acetometaphin toxic/ ti gets converted to toxic active protics via metabolism and kills the liver via oxidation after glutathione is all used

  14. Kidney excretion: only unbound drugs can be filtered, secretion happens in active transport in proximal tubule, reabsorption happens via passive transport in the distal tubule

  15. What drugs are not innactiveaed by metabolism? amino glycoside antibiotics and digoxin—> controlle day renal excretion

  16. Max peak of drug plasma conentration= initial x accumulation factor

  17. Agonist vs Antagonist:

    1. Agonist: activates the receptor once bonded (affinity for receptor and efficacy)

    2. Antagonist: bids to receptor but precedes the response (yes affinity but no efficacy)

  18. Dynein vs Dynamin

    1. Dynamin= endocytossi

    2. Dynenine= flagella movement

  19. What’s a way for Ibiunine ligase to function? by recognizing certain proteins, lysosome deflation doesn’t do this

  20. Where are Introns taken out? GU and AG

  21. I cell disease:  targeting information in the Golgi is lost—> enzymes do not acquire mannose-6-phosphate and are lost to the ECM via the constitutive secretory pathway. Lysosomes are present but empty—>“lysosomal ghosts”. Aka there’s a lack of lack of lysosomal hydrolases in lysosomes.