As of November 2017, 22 states require licensure to genetic counselors. These states are California, Connecticut, Delaware, Idaho, Illinois, Indiana, Kentucky, Massachusetts, Minnesota, Nebraska, New Hampshire, New Jersey, New Mexico, North Dakota, Ohio, Oklahoma, Pennsylvania, South Dakota, Tennessee, Utah, Virginia, and Washington. As of that time all other states besides Wyoming and Vermont were in progress of getting licensure and/ or in the rule making stage[1].

  1. ^ "States Issuing Licenses for Genetic Counselors". National Society of Genetic Counselors. Retrieved 29 January 2018.

A genetic counselor is an expert with a Master of Science degree in genetic counseling. There are currently 37 accredited programs in the United States, four accredited programs in Canada, and six programs with the intent to become accredited [1]. In the United States they are certified by the American Board of Genetic Counseling.[1] In Canada, genetic counselors are certified by the Canadian Association of Genetic Counsellors. Most enter the field from a variety of disciplines, including biology/ biological sciences and social sciences such as psychology [2]. Genetic counselors should be expert educators, skilled in translating the complex language of genomic medicine into terms that are easy to understand. Genetic counseling helps one to know the chances of inheritance of a genetic disorder so that people can make informed decisions.

  1. ^ "Accredited Programs". gceducation.org. Retrieved 2018-01-30.
  2. ^ "National Society of Genetic Counselors : Interested in Becoming a Genetic Counselor". www.nsgc.org. Retrieved 2018-01-30.

The goals of genetic counseling are to increase understanding of genetic diseases, discuss disease management options, and explain the risks and benefits of testing.[1] Counseling sessions focus on giving vital, unbiased information and non-directive assistance in the patient's decision-making process. Seymour Kessler, in 1979, first categorized sessions in five phases: an intake phase, an initial contact phase, the encounter phase, the summary phase, and a follow-up phase.[2] The intake and follow-up phases occur outside of the actual counseling session. The initial contact phase is when the counselor and families meet and build rapport. The encounter phase includes dialogue between the counselor and the client about the nature of screening and diagnostic tests. The summary phase provides all the options and decisions available for the next step. If patients wish to go ahead with testing, an appointment is organized and the genetic counselor acts as the person to communicate the results. Result delivery can happen both in person or via phone. Often counselors will call out results to avoid patients having to come back in as results can take weeks to be processed. If further counseling is needed in a more personal setting, or it is determined that additional family members should be tested, a secondary appointment can be made.

A round, moist, lumpy clump of clay body is thrown at a wheelhead or a bat attached to it. The term "bat" refers to a secondary disc or square, made of wood – or more recently plastic – to which the lump of clay is attached instead of the wheel head, thereby permitting the finished piece to be more easily lifted from the wheel. The clump is made even and forced to the center of the wheel by applying pressure with the hands. Often the best way to muscle it towards the center is to hold one hand with the palm facing away from you and the other at an approximate 90 degrees to the first hand. This makes it easier to push the clay away from your torso and towards the center of the wheel. The thrower finds the center of the clay by moving a thumb across the lump until no more friction is felt. The thumb is pressed into the centre of the lump, stopping about 5 mm (14 inch) from the wheel head. The hole made is widened by slowly pulling your hands toward your body. The sides are then pulled up and made thinner by pressure between the hands. This can be done simply with wet hands or by using a wet sponge for a smoother surface. The vessel is shaped, and the mouth is smoothed. The vessel is cut from the wheelhead or bat with a cheese wire and left to stiffen. Sometimes the stiffened vessel is inverted on the wheel and trimmed with a sharp tool.

The thickness or weight of the yarn is a significant factor in determining how many stitches and rows are required to cover a given area for a given stitch pattern. This is also termed the gauge. Thicker yarns generally require large-diameter crochet hooks, whereas thinner yarns may be crocheted with thick or thin hooks. Hence, thicker yarns generally require fewer stitches, and therefore less time, to work up a given project. The recommended gauge for a given ball of yarn can be found on the label that surrounds the skein when buying in stores. Patterns and motifs are coarser with thicker yarns and produce bold visual effects, whereas thinner yarns are best for refined or delicate pattern-work. Yarns are standardly grouped by thickness into six categories: superfine, fine, light, medium, bulky and superbulky. Quantitatively, thickness is measured by the number of wraps per inch (WPI). The related weight per unit length is usually measured in tex or denier.

  1. ^ Genetic Alliance Site [Internet]. [cited 2010 Oct 29]. Available from: http://www.geneticalliance.org/.
  2. ^ Hodgson, JM; Gillam, LH; Sahhar, MA; Metcalfe, SA (Feb 2010). ""Testing times, challenging choices": an Australian study of prenatal genetic counseling". Journal of Genetic Counseling. 19 (1): 22–37. doi:10.1007/s10897-009-9248-6. PMID 19798554.

C1orf27

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Uncharacterized protein Chromosome 1 Open Reading Frame 27 is a protein in humans, encoded by the C1orf27 gene. It is accession number NM_017847[1]. This is a membrane protein that is 3926 base pairs long with the most extensive string of amino acids being 454aa long. C1orf27 exhibits cytoplasmic expression in epidermal tissues.[2] Predicted associated biological processes of the gene include cell fate specification and developmental properties.[3]

Gene

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Locus

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This gene is located on chromosome 1 at 1q31.1.[4] It is encoded on the plus strand of DNA from 186,344,406 to 186,390,514.

 
Diagram of C1orf27 and nearby genes on human chromosome 1.[4]

mRNA

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Alternative Splicing

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There appear to be four isoforms due to splicing[5]. Two of those are truncated on the 3' end of the protein from 266aa and 396aa. Additional location of alternative splicing are from 79aa to 102aa and 246aa to 260aa.

Protein

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General Properties

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The primary encoded protein consists of 454 amino acid residues and is 3926 base pairs long.[1] It consists of 14 total exons. The predicted molecular weight of the primary, unmodified protein is approximately 51.1 kdal.

Aliases

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As with many other genes, there are some common aliases found with this gene.[6] Those aliases are Lymphocyte-activation gene-1 (LAG1) Interacting Protein, Transparent Testa Glabra 1 (TTG1), and Odorant Response Abnormal 4 (ODR4). The most common alias for C1orf27 is ODR4, and this is what most readily appears when searching the gene.

Composition[7]

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Computational analysis revealed the most abundant amino acid to be leucine at 10.1% of the total protein. The second most abundant was serine which contributes to 8.6% of the total protein. Glutamic acid was third most abundant and contributes to 7.7% of the protein. Based on the distribution of other amino acid types, there were five high scoring hydrophobic segments. There were also two transmembrane domains located at 82-98aa and432-449aa.

Post-Translational Modifications

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Interactor Number of Predicted Sites Function
N-myristoylation 8 Key components of signaling pathways, and typically promotes membrane binding essential for protein localization and/ or biological function[8]
N-glycosylation 4 Increase protein stability by decreasing protein dynamics[9].
Protein Kinase C Phosphorylation 7 Enzymatic activityy regulation[10].
Casein Kinase II Phosphorylation 7 Epidermal growth factor role[11].
Tyrosine Kinase Phosphorylation 2 Alterations to the structural conformation[12].
cAMP and cGMP Dependent Phosphorylation 2 Coordination of the active site conformation and enzymatic activity[13].

C1orf27 is predicted to undergo multiple post translational modifications such as glycosylation, myristoylation, and phosphorylation[14].

Interactions

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There were eight interactions identified by Mentha[15]. The first one was UFSP2 which hydrolyzes the peptide bond at the C-term gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. The second one was HSCB which acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. The third was GRB2 which is an adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway. The fourth was CYLD which is a protease that cleaves Lys-63-linked polyubiquitin chains, controls regulation of cell survival, proliferation, and differentiation, and is required for normal cell cycle progress. The fifth was ATM which activates checkpoint signaling upon double strand breaks, apaptosis, and genotoxic stress. The sixth was FAM177A1, the function of which is unknown. The last two were THID2 and Q81kP6 which are both in bacillus anthracis.

Subcellular Localization

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The c1orf27 protein is likely cytoplasmic[16]. This was found with 55.5 reliability. The K-NN prediction was k=9/23 and the protein was found to be 55.6% cytoplasmic, 11.1% mitochondrial, 11.1% vacuolar, 11.1% cytoskeletal, and 11.1% golgi.

Structure

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Predicted tertiary structure of c1orf27[17].

Alpha helices predicted in the c1orf27 protein are colored blue in the above picture. Beta sheets are pictured by the red arrows. Random coils are the purple strands between structures.

Expression

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Tissue Expression Pattern

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Overall, expression of c1orf27 seems to be ubiquitous. Highest expression body sites (>50 TPM) were bladder, bone marrow, kidney, liver, pancreas, parathyroid, and vascular. Highest expression health sites (>50 TPM) were adrenal tumors, cervical tumors, and liver tumors. This makes sense because of the tissues that it is expressed in. There was moderate expression (>25 TPM) in the human fetus, and expression increased with age. Expression was completely absent in the ears, esophagus, lymph, nerve, salivary glands, thyroid, tonsils, and umbilical cord. Interestingly enough, there was no expression in bladder carcinoma despite expression being elevated in the bladder itself. There was high expression in endothelial cells and neuronal cells but was undetectable in glial cells and neuropil cells. Expression was also localized to the nucleoplasm and plasma membrane in humans but is localized to the cytosol in mice.

Homology

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Paralogs

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There were no paralogs of C1orf27 identified in the human genome.[5]

Orthologs

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There were orthologs identified in most animals for which there were complete genome data.[5] The most distant, yet still relevant, orthologs identified were invertebrates from phylum Cnidaria.

Molecular Evolution

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The m value, or number of corrected amino acid changes per 100 residues, for the C1orf27 gene was graphed against the species divergence in millions of years. When compared to divergence graphs of fibrinogen and cytochrome C, it was determined that this gene closely resembles the evolutionary pattern observed in fibrinogen, suggesting a more rapid rate of evolution. M values for C1orf27 were calculated using the percentage of identity, when compared to humans, observed in the mRNA sequences of the orthologs using the formula derived from the Molecular Clock Hypothesis.

References

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  1. ^ a b "Homo sapiens odr-4 GPCR localization factor homolog (ODR4), transcript - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-02-05.
  2. ^ "Tissue expression of C1orf27 - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2018-02-05.
  3. ^ Makar, A. B.; McMartin, K. E.; Palese, M.; Tephly, T. R. (June 1975). "Formate assay in body fluids: application in methanol poisoning". Biochemical Medicine. 13 (2): 117–126. ISSN 0006-2944. PMID 1.
  4. ^ a b "ODR4 odr-4 GPCR localization factor homolog [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-02-19.
  5. ^ a b c "Protein BLAST: search protein databases using a protein query". blast.ncbi.nlm.nih.gov. Retrieved 2018-02-25.
  6. ^ Makar, A. B.; McMartin, K. E.; Palese, M.; Tephly, T. R. (June 1975). "Formate assay in body fluids: application in methanol poisoning". Biochemical Medicine. 13 (2): 117–126. ISSN 0006-2944. PMID 1.
  7. ^ EMBL-EBI. "SAPS < Sequence Statistics < EMBL-EBI". www.ebi.ac.uk. Retrieved 2018-04-22.
  8. ^ Wright, Megan H.; Heal, William P.; Mann, David J.; Tate, Edward W. (2009-11-07). "Protein myristoylation in health and disease". Journal of Chemical Biology. 3 (1): 19–35. doi:10.1007/s12154-009-0032-8. ISSN 1864-6158. PMC 2816741. PMID 19898886.{{cite journal}}: CS1 maint: PMC format (link)
  9. ^ "Proteomics/Post-translational Modification/Glycosylation - Wikibooks, open books for an open world". en.wikibooks.org. Retrieved 2018-05-06.
  10. ^ "Posttranslational modifications on protein kinase c isozymes. Effects of epinephrine and phorbol esters". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1783 (5): 695–712. 2008-05-01. doi:10.1016/j.bbamcr.2007.07.011. ISSN 0167-4889.
  11. ^ Siomi, Mikiko C.; Higashijima, Kyoko; Ishizuka, Akira; Siomi, Haruhiko (December 2002). "Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties". Molecular and Cellular Biology. 22 (24): 8438–8447. ISSN 0270-7306. PMID 12446764.
  12. ^ Rahimi, Nader; Costello, Catherine E. (2015-1). "Emerging Roles of Post-translational Modifications in Signal Transduction and Angiogenesis". Proteomics. 15 (0): 300–309. doi:10.1002/pmic.201400183. ISSN 1615-9853. PMC 4297243. PMID 25161153. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  13. ^ "CGMP-dependent protein kinase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2018-05-06.
  14. ^ "ExPASy - PROSITE". prosite.expasy.org. Retrieved 2018-04-22.
  15. ^ "mentha: the interactome browser". mentha.uniroma2.it. Retrieved 2018-04-22.
  16. ^ "PSORT II Prediction". psort.hgc.jp. Retrieved 2018-04-22.
  17. ^ Kelley, Lawrence. "PHYRE2 Protein Fold Recognition Server". www.sbg.bio.ic.ac.uk. Retrieved 2018-05-06.

Although animal crackers are made with a layered dough like crackers, they tend to be sweet in flavor, but still technically a cracker and not a cookie[1].

  1. ^ "FAQs | Stauffer's Animal Crackers". www.stauffers.com. Retrieved 2018-02-05.

Either way, the portrayal has worked; it is favored in 54% of states in the United States[1].

  1. ^ "8 Things You Should Know Before You Buy Cinnamon Toast Crunch". Delish. 2016-05-12. Retrieved 2018-02-05.

the colors of his bill correspond to the three original froot loop colors[1].

The company was founded in 1993 by Donald Gary Young[1]

Goals

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Young Living is one of the top leaders in essential oils and wellness solutions. The overall goal of the company is to provide a pure essential oil product to help customers discover lifelong transitions into wellness[1].