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I've noticed the data on CUDO seems to show that cutoffs for all university engineering programs are increasing? Yet our demographics show less students applying and going to university. Does anyone know when all the 2015 or possibly 2016 data will be out on this? Do you think the 2017 cutoffs will be even higher?
My main goal is to get into the DD program for Math at Waterloo and business at Laurier. What average do you think I'll need to get accepted? I'm not really too picky about which side I want to enter the program through, cause I like both universities. Would a 92 or 93 (with OK extra curriculars) be enough?
Mature and active TGF-β ligands are formed by much larger precursor molecules. The active precursors include two of the carboxy-terminal mature domains in either homo- or heterodimer conformations. The amino-terminal signal peptide is cleaved at a conserved Arg-X-Arg-Arg site when translocated into the lumen of the rough endoplasmic reticulum, leaving the carboxy-terminal TGF-β superfamily mature monomer polypeptide. For TGF-β superfamily members, the mature domain is related to a latency associated peptide (LAP) which helps the protein move toward sites of activation or storage.
The critical difference to distinguish the subfamilies is the number and location of the cysteines, whose spacing and conservation are the hallmark of the TGF-β family members. The three TGF-β isoforms contain nine cysteines. Four cysteine pairs with each other intramolecularly and the other five cysteine forms a disulfide bridge with a nearby monomer which leads a dimer formation. All other TGF-β superfamily members contain seven or five cysteines. For seven cysteines TGF-β molecules, they share a common pattern. Six cysteines form a “cystine knot” which holds each monomer subunit together. The fourth cysteine in each monomer forms Disulfide Bridge in a covalently linked with an adjacent monomer. Many of these seven cysteine-containing ligands are classified into bone morphogenetic proteins (BMPs) or growth differentiation factors (GDFs). The five cysteines TGF beta molecules are Lefty A, Lefty B, BMP-15, GDF-3 and GDF-9. These ligands are biologically active in non-covalent dimers formation.
“Transforming growth factors” (TGFs) superfamily members are responsible for causing normal fibroblasts to undergo anchorage-independent growth, a property closely associated with the transformed, or malignant, phenotype in vivo. TGF-α is originally thought to be expressed solely by tumor cells, and TGF-β is thought to be expressed in normal tissues and served to modulate the transforming process. TGF-β1 was found and charactered in the early 1980’s and this leads to the identification of two TGF-β isoforms (TGF-β2, TGF-β3) and a large family of growth factors that are essential regulators of developmental processes, physiology and disease pathogenesis.
The TGF-β Superfamily members are secreted cell-regulatory proteins which play biologically diverse roles in embryonic development, tissue differentiation and proliferation, body patterning, maintenance of pluripotency, and also can influence of cell fate in stem cell systems.
There are nearly forty TGF-β Superfamily proteins in mammalian genome which all share sequence and structural similarities. They share the same family of receptors and signaling intermediates. Subfamilies within the TGF-β superfamily are organized based on structural and sequence similarities of the mature monomer.
The TGF-β superfamily consists of over 30 structurally related members. The proteins encoded by TGF-β superfamily genes are processed to produce mature peptides by proteolytic cleavage. The TGF-β superfamily signaling begins with the secretion of TGF-β ligand peptides. These peptides are dimerized into homodimers or heterodimers and are secreted from the cell. Secreted dimers bind to their respective type I and type II serine/threonine kinase receptors and elicit transcriptional responses through phosphorylation of the receptors-regulated Smad proteins (R-Smads). In vertebrates, the type I receptors for bone morphogenetic proteins (BMPs) phosphorylate Smad1 or the closely related Smad5 and Smad8; whereas the type I receptors for TGF-βs, Activins and Nodal signal through Smad2 and Smad3. Phosphorylated R-Smads form heteromeric complexes with a common Smad, Smad4, and translocate into the nucleus to regulate target gene expression. Diverse nuclear DNA binding proteins interact with R-Smad/Smad4 complexes in the nucleus, mediating cell type-specific responses to TGF-β signaling.
There are three types of TGF-β superfamily receptors on the surface of cell membrane: type I receptor, type II receptor, and co-receptor. In TGF-β superfamily signaling, there are 3 models of ligand binding to receptors:
1. Ligand binds to the co-receptor, which presents the ligand to the type II receptor. The type II receptor then activates the type I receptor. This model has been found in TGF-β subfamily signaling.
2. Ligand binds to the type II receptor and then activates the type I receptor to the signaling complex. This model has been found in TGF-β subfamily and Activins signaling.
3. The type I and type II receptors bind ligand in a cooperative manner, meaning the two receptors have a much higher affinity when together than they do individually. This model has been found in BMPs signaling.
Tumor necrosis factors secreted by hematopoietic or non-hematopoietic cells are involved with inflammation and immunity as one kind of cytokines, as well as cell death and proliferation, differentiation, migration, phagocytosis, and survival.
However, aberrant TNF proteins can lead to a variety of disease states, including cancer, diabetes, atherosclerosis, and autoimmune disorders such as inflammatory bowel disease (IBD) and rheumatoid arthritis (RA). Furthermore, the connection between bacterial infection and autoimmune disorders resulting from TNF misregulation is reported. Although the pathogenic cause of most chronic inflammatory diseases is unknown, the classic inflammatory responses promoted by TNF are thought to account for them.
Since 1998, anti-TNF therapy has been used successfully for the treatment of inflammatory disease such as RA and IBD. The use of infliximab or adalimumab (two anti-TNF antibodies) and soluble TNF receptor fusion proteins fuel a major part of the global market as TNF inhibitors. Certolizumab pegol and golimumab are also used to treat crohn’s disease and RA later. However, the inhibition of TNF will lead an increased risk for bacterial infections. So people try to selectively inhibit TNF secreted from specific cell types. The strategy is to primary inhibit the pathogenic TNF but sparing essential TNF in the host defence.
The intracellular regions of tumor necrosis factors receptors (TNFR) associate with either of two adapter protein types. One is death domain (DD) adapter proteins and another is TNF receptor-associated factors (TRAF).
TNF receptors that directly recruit TRAFs involve a TRAF interaction motif (TIM), a short cytoplasmic sequence with an extended conformation. In humans, TRAF2 is the best characterized one of TRAF. Once TNFR and TRAF2 combine, the Jun N-terminal kinases (JNK) pathway and NF-KB pathway is triggered, leading to diverse functions including cell differentiation, proliferation and inflammatory response. Structural studies about TRAF2 reveal that the molecule forms a stable trimer in solution. Therefore, it is likely that upon engagement with ligands, the trimerized TNF receptors bind a trimeric intracellular TRAF adapter protein with high avidity. After recruitment by the TNF receptors, TRAF2 activates protein kinases that start the JNK pathway or the NF-KB pathway. TRAFs are major signal transducers for the TNF superfamily as well as the IL-1 family proteins.
Tumor necrosis factor ligands (TNF) family named by the first identified members TNFα and TNFβ is consisting of 19 ligands on the basis of sequence, functional, and structural similarities. All TNF ligands cytokines seem to form homotrimeric with exception of heterotrimeric by Lymphotoxin-alpha/beta (LTα/β). Some of the TNF family members and their functions are listed as following:
TNFα which is also named cachectin is a cytokine with variety of functions. It is involved in apoptosis of some tumor cells, induction of cachexia, causing fever, stimulation of interleukin-1 secretion, cell proliferation and cell differentiation.
LTα and LTβ are cytotoxic for a wide range of tumor cells and they induce cell apoptosis both in vitro and in vivo.
CD40L plays a key role in the development and activation of B-cell.
FASL is a protein on cell surface regulating of the immune system and the progression of cancer.
TNFSF9/4-1BBL is a bidirectional signal transducer that acts as a ligand for TNFRSF9/4-1BB and also contributes to T-cell stimulation.
TNFSF4/OX40L is important in the interaction between T cell and antigen-presenting cell (APC) and also mediates adhesion of activated T cells to endothelial cells.
TNFSF10/TNF-related apoptosis inducing ligand (TRAIL) induces apoptosis of transformed cells and tumor cells, but not normal cells.
Tumor necrosis factors (TNF) receptor (TNFR) family is consisting of a group of proteins with an extracellular domain rich in cysteine residues. These receptors are activated by specific TNF ligands. There are about 30 TNF receptors having been reported in humans.
Most TNF receptors form trimeric complexes in the plasma membrane as the active form and these receptors bind to TNF ligands as multimeric entities. Signaling through these receptors involves with cytoplasmic adaptor proteins (such as TRADD and TRAF1) as downstream. TNF receptors not only play a key role in apoptosis and inflammation but also involve in other signal transduction pathways, for example, survival, proliferation and differentiation. Some TNF receptors contain a ‘death domains’ which is crucial for the initiation of an apoptotic response.
TNFR1 is found ubiquitously throughout every cell in the body, while its counterpart TNFR2 is more restrictively expressed on certain immune subpopulations. Normally, TNFα signaling through TNFR1 pathway will lead to apoptosis through the caspase system. On the other hand TNFα signaling through TNFR2 will lead to cell survival through activation of NF-κB pathway. However, it has been found that autoreactive T Cells have a defective immuno-proteasome which causes the inability to activate the NF-κB pathway when stimulated through TNFR2.
I will finish only Pre-cal 12 and Physics before I apply to university. Pre-cal12 is 82(tough teacher) at last year. But, now I am in 96 in Physics12, also I can maintain or upgrade my grade. I will take calculus AP physics Chemistry12 and english 12 on second semester. I will apply UBC mechanical engineering and UT aerospace engineering. Do you guys think is this posible to get admission.
I'm currently in Grade 12 and I'm interested in going into the Dental Hygiene Program @ UBC (first choice). My second choice is most likely Vancouver Community College (bc parents want me to stay local) or else, I wanna go to University of Alberta.
- Which university would you recommend?
- What is the average to get into the Dental Hygiene Program @ UBC??
- What allows one applicant to be "better" than another?
- How is the interview process?
- Anything you would recommend me to do (courses to take in high school/ extra curriculum/ volunteer events to take on)
Exactly one year ago I was in many of your positions, struggling to find the perfect university for my wants/needs and praying my midterm marks and first sem. final grades were on fleek.
Now that I'm in uni, I have decided to return the favour and give any tips or advice to anyone applying this year.
A little bit about me:
I got into the McMaster life sciences program around March (first round) with a 91% average. I also applied to UTM and UTSG and got in around February. I initially wanted to go to UTM, but my gut feeling chose Mac. Let me just say, your gut feeling never lets you down!
Hey, I'm a grade 12 student thats thinking about going into psychology at UofT next year.
I was wonder what was the average marks of people that have been accepted past year. Also, when the website says the english mark needs to be "low to mid 80s", does that mean it can be anywhere from 80-85?
Finally, are any M courses accepted for my top 6 choices? Thank you!
I'm a student athlete (football) and looking to attend a great university academically, athletically, and socially, with a nice atmosphere (average is 85+). From what I've seen, Queen's, Western, UBC, and Mcmaster seem awesome.
So, in your experience and from what you've heard, what school do you think presents the best university experience and why? Try to consider most programs and sports and student life.
*Also, If you have or are applying, 1. program 2. average 3. EC's 4. Reason 5.Province 6. Sport?
I went on a cultural outreach trip through my school to Latin America last spring break. I didn't go on it to boost my résumé or university application; every student at my school has to go on such a trip (although many choose to stay in my city and volunteer here). I absolutely loved the trip and so I would like to write about it in my supplementary applications.
I am well aware of the stigma attached to these volunteer abroad trips. I know that they're a college essay topic US universities caution people to avoid; however, I've noticed that supplementary application standards for top Canadian schools seem to be lower and people's responses are more cliché imo.
I don't plan on writing something basic like "I realised just how privileged I am" or "they taught me more than I taught them," etc. or making me seem like some saviour. I stayed with a local family on my trip and so I was thinking about writing about that or how the trip made me realise and reaffirm my career goals.
So do you think it would be okay for me to write about my trip?
Hi, I just had the biggest screw-up, i didnt study enough and i ended up getting a total average of 65.5% on my unit 1 in grade 10 math ,this is the lowest mark ive ever gotten, its not coz im dumb but... i didnt work hard enough and now my dad found out. Hes extremely disappointed because of the mark and he knows that I'm capable of much more. So he says i need to get an average of at least 90% now. There 6 units i already finished the first with a 65. I'm not stupid but I'm also not sure if i can pull that off. More than for my dad, i want to be able to do this for myself.
Any advice on how i can get there?
I guess i can start by actually doing the homework and paying a bit more attention in class.
I'm really worried, coz its never happened to me , any help would be really appreciated
Thanks in advance
BTW this is my first post on this website, i just made an account, so im not too sure how everything works
I'm in my final year of high school (grade 12) and have been very stressed due to my low English mark of 74%. I have 90's in my other classes but I know this English mark will hold me back. I tried dropping my in-class English course so I could take online English (VHS), but my guidance counsellor refused as she would not let me be a part-time student without a "valid reason".
Could I upgrade my mark next semester through the VHS online English private school and have my marks uploaded for midterms?
If I upgraded my mark this means I would be in 4 courses in a single semester.. is it doable?
Am I screwed?
[And of course I will try my best to improve my mark over this semester so I don't have to 100% retake the course]
I am a grade 12 student planning to apply to Life Sciences at U of T. As I was browsing through the programs that one could possibly specialize in after first year, I noticed that different campuses have different programs offered. For example, the St. George campus offers Pharmacology, while UTM does not. So I was wondering, if I have more that one program in mind right now that are offered at different campuses, how would that work? How would I chose which campus to apply to? I'm very confused...