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Chapter 39 – Plant Responses to Stimuli Signal Transduction
Chapter 39 – Plant Responses to Stimuli Signal Transduction

... o Etiolation – adaptations for growing in darkness  Exposure to light – shoots & roots grow normally (de-etiolation) Hormone  Chemical signal that coordinates different parts of an organism o Growth, development, & responses to stimuli Reception  Internal & external signals are detected by recept ...
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... 2. Frequently, when we are talking about allosteric proteins, we are talking about proteins with ___________ structure. 3. The allosteric regulators bind to sites that are not active sites and elicit their effects by causing a Change in Shape of the Catalytic Subunit ...
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... • Pepsinogen is converted into the enzyme pepsin when it comes into contact with hydrochloric acid • Pepsin is the only proteolytic enzyme that digests collagen, the major protein of connective tissue ...
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... with a membrane-attack-complex/ perforin (MACPF) domain. When combined, aegerolysins and these MACPF-proteins can perforate artificial and biological membranes that contain the specific lipid receptor, by forming transmembrane pore complexes. Similarly, the genomes of some aegerolysin-producing bact ...
Moonlighting and pleiotropy among regulators of the degradation
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... Multifunctional proteins are generally referred to as either pleiotropic or moonlighting proteins. Although define similarly, the meaning is these terms is quite different. While a moonlighting protein harbors several autonomous functions, pleiotropy refers to a single-functional protein, which infl ...
GENE-SILENCING IN THE BRAIN IN VIVO USING siRNA
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... consequences, such as hyperlocomotor activity after DAT knockdown, antidepressant like activity with 5-HTT SiRNA and anxiolytic activity following mGluR7 receptor knock down. Remarkably and surprisingly, in vivo mRNA (and protein) down regulation of as little as 25-30% resulted in significant functi ...
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... GPCRs are involved in a range of signaling pathways, including light detection, odorant detection, and detection of certain hormones and neurotransmitters Many different mammalian cell-surface receptors including GPCRs are coupled to a trimeric signal-transducing G protein – made of an alpha, beta a ...
New partners for protein kinases - Journal of Molecular Cell Biology
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... CHK2 kinase, particularly focusing on its responses to DNA damage. CHK2 is well known as a nuclear serine/threonine protein kinase involved in the spreading of DNA damage signal through a phosphorylation cascade. The authors not only discussed the classical partners for CHK2 participating in DNA dam ...
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Endoplasmic reticulum - Protein synthesis

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... region affect amino acids necessary for its phosphorylation dependent interaction with protein degradation machinery • APC mutations affect axin and b-catenin binding • Axin mutations truncate the protein thus eliminating b-catenin binding sites ...
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Abstract - Earth Journals publisher
Abstract - Earth Journals publisher

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... Receptors which are coupled via G-proteins (for example adrenalin receptors) When activated, these receptors make G-proteins fall into two p f parts which diffuse ff away y f from m the receptor. Activated G-proteins bind to other proteins and change their function. This may lead to activation of so ...
Exam III - chem.uwec.edu
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... sequences. An example can be found on Grb-2 adaptor protein in the epidermal growth factor (EGF) signal transduction pathway ...
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... Physiological and pharmacological regulation of gastric secretion: the basis for therapy of acid-peptic disorders. Shown are the interactions among an enterochromaffin-like (ECL) cell that secretes histamine, a ganglion cell of the enteric nervous system (ENS), a parietal cell that secretes acid, an ...
Proteins Hwk KEY
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... Structural component of connective tissue and bone Reversibly binds oxygen so it can be delivered to the tissues from the lungs; found inside red blood cells Also known as antibodies, these proteins bind to and inactivate antigens (molecules on germs) Hormone secreted by the pancreas that promotes t ...
Cartoon modeling of proteins
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... How does this ordered soup of proteins maintain a such a large number of tightly synchronised feedback control systems? ...
Cartoon modeling of proteins
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... How does this ordered soup of proteins maintain a such a large number of tightly synchronised feedback control systems? ...
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Biosynthesis and degradation of proteins

... • IAPs are proteins that block apoptosis by binding to and inhibiting caspases. The apoptosis-stimulating protein Smac antagonizes the effect of IAPs on caspases. • TIMPs are inhibitors of metalloproteases that are secreted by cells. A domain of the inhibitor protein interacts with the catalytic Zn+ ...
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... 1. Cells have mechanisms to respond to environment. 2. Many signals are transduced through phosphorylation cascades. 3. ATP is kinetically stable but thermodynamically labile molecules. Enzymes that use APT as phosphate donor and transfer the phopsphate onto an acceptor molecule are called kinases. ...
APChapter11 2014 - Auburn School District
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... and interacts with a G-protein. This interaction causes the GDP bound to the inactive G-protein to be displaced by GTP, thereby activating the G-protein GTPase hydrolyses the bound GTP back to GDP ...
Chapter 11: Cell Communication 10/7/2015
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... single molecule of ligand results in a ...
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... Biologists at the U.S. Department of Energy's Brookhaven National Laboratory, Stony Brook University, and the University of Wurzburg, Germany, have deciphered the structure of a large protein complex responsible for adding sugar molecules to newly formed proteins - a process essential to many protei ...
General Principles
General Principles

... cell and activating an intracellular enzyme – usually guanylyl cyclase, which produces cyclic GMP in the target cell. But most extracellular signaling molecules are hydrophilic and are able to activate receptor proteins only on the surface of the target cell; these receptors act as signal transducer ...
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G protein–coupled receptor



G protein–coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein–coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. Two of the United States's top five selling drugs (Hydrocodone and Lisinopril) act by targeting a G protein–coupled receptor. The 2012 Nobel Prize in Chemistry was awarded to Brian Kobilka and Robert Lefkowitz for their work that was ""crucial for understanding how G protein–coupled receptors function."". There have been at least seven other Nobel Prizes awarded for some aspect of G protein–mediated signaling.There are two principal signal transduction pathways involving the G protein–coupled receptors: the cAMP signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein's α subunit, together with the bound GTP, can then dissociate from the β and γ subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the α subunit type (Gαs, Gαi/o, Gαq/11, Gα12/13).
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