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Browse Books Site Directory Site Language: English Change Language English Change Language Quick navigation Home Books Audiobooks Documents, active Collapse section Rate Useful 0 0 found this document useful, Mark this document as useful Not useful 100 100 found this document not useful, Mark this document as not useful Collapse section Share Share on Facebook, opens a new window Facebook Share on Twitter, opens a new window Twitter Share on LinkedIn, opens a new window LinkedIn Copy Link to clipboard Copy Link Share with Email, opens mail client Email. And by having access to our ebooks online or by storing it on your computer, you have convenient answers with Cryptography Theory And Practice Solutions Manual. To get started finding Cryptography Theory And Practice Solutions Manual, you are right to find our website which has a comprehensive collection of manuals listed. Doug Stinson was published in February 2002, by The third edition will be published in 2005.G. Avoine and P. Junod, was publishedCopies of the solution manual can be obtained CRC Press has a web page. The site may not work properly if you don't update your browser. If you do not update your browser, we suggest you visit old reddit. Press J to jump to the feed. Press question mark to learn the rest of the keyboard shortcuts Log In Sign Up User account menu 2 Exercise solutions to book:?Cryptography: Theory and Practice by Douglas Stimson. ? But I can't find the one that I need. I heard of this book has been elected as official textbook for many universities worldwide, so why the solutions resource is so few. Does anyone who had an experience on this book and solutions? 2 comments share save hide report 100 Upvoted This thread is archived New comments cannot be posted and votes cannot be cast Sort by best I have no other tips other than that, sorry. 1 share Report Save level 2 Original Poster 1 year ago yeah, thx for the info though I already got it.
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Cryptography lives at an intersection of math and computer science. All rights reserved Back to Top. Theory and Practice. Second Edition. Solution Manual. Douglas R. Stinson Contents 0 Introduction 1 1 Classical Cryptography. Exercises........................... 2Exercises........................... 15Exercises........................... 25Exercises........................... 37Exercises........................... 50Problem. Exercises........................... 66Exercises........................... 78I provide “final answers” to computationalI obtained mostComputer programsThis solution manual refers to the first printing of the book. Several exercisesThese errors will be fixed in later printings of the book. I would appreciate any comments or feedback about this solution manual andI hope that this solution manual will be a useful resource for instructors teaching courses in cryptography. Please try to prevent the distribution of this manualDouglas R. Stinson. Waterloo, Ontario. June, 2002 1 1. Classical Cryptography ExercisesLook, up in the air, it’s a bird, it’s a plane, it’s Superman!Prove that theIn the third case. Use the fact that a matrix over a fieldHence, the total number of invertibleAnswer: The inverse matrix is. The plaintext is the following. Gentlemen do not read each other’s mail. Answer: An involutory permutation must consist of fixed points and cyclesThe total number of involutory. The total number. The total number of involutoryIn each case, the task is to determine the plaintext. Give a clearly written description of the steps you followed to decrypt each ciphertext. This should include all statistical analysis and computations you performed. The first two plaintexts were taken from “The Diary of Samuel Marchbanks,” by. Robertson Davies, Clarke Irwin, 1947; the fourth was taken from “Lake Wobegon. Days,” by Garrison Keillor, Viking Penguin, Inc., 1985.
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I may not be able to grow flowers, but my garden produces justI have always loved and respected theYou multiply the square footage of the wallsThen you double the whole thing again to give a margin of error,Ton front est ceint. De fleurons glorieux. Car ton bras. Sait porter l’?ep?ee. Il sait porter la croix. Ton histoire est une e? pop?ee, 8 1.22 Classical Cryptography des plus brillants exploits. Et ta valeur,I grew up among slow talkers, men in particular, who droppedSo I enrolled in a speech courseBy a sequence of exchanges of this type, we see that the sum attains itsAssuming that this is the case, we proceed.Answer: There is an error in the statement of this question; the plaintext does notThe ciphertext should be as follows:Answer: We are given the following. Break the ciphertext into blocks of length twoPick out the most frequent ciphertext digram andFor each such guess, proceed as in the known-plaintextHere is a sample of ciphertext for you to decrypt using this method: Exercises 11 LMQETXYEAGTXCTUIEWNCTXLZEWUAISPZYVAPEWLMGQWYAThe plaintext is the following. The king was in his counting house, counting out his money. TheThen form the ciphertext byThe ci.
Almost all signals that lead to activation of NF-kB converge on the activation of a high molecular weight complex that contains a serine-specific IkB kinase (IKK). IKK is an unusual kinase in that in most cells IKK contains (at least) three distinct subunits: IKKalpha, IKKbeta and IKKgamma. IKKa and IKKb are related catalytic kinase subunits, and IKKg (aka NEMO) is a regulatory subunit that serves as a sensing scaffold and integrator of upstream signals for activation of the catalytic subunits. In the classical or canonical pathway, activation of IKK complex leads to the phosphorylation by IKKb of two specific serines near the N terminus of IkBa, which targets IkBa for ubiquitination (generally by a complex called beta-TrCP) and degradation by the 26S proteasome. In the non-canonical (or alternative) pathway, the p100-RelB complex is activated by phosphorylation of the C-terminal region of p100 by an IKKa homodimer (lacking IKKgamma), which leads to ubiquitination followed by degradation of the p100 IkB-like C-terminal sequences to generate p52-RelB. In either pathway, the unmasked NF-kB complex can then enter the nucleus to activate target gene expression. In the classical pathway, one of the target genes activated by NF-kB is that which encodes IkBa. Newly-synthesized IkBa can enter the nucleus, remove NF-kB from DNA, and export the complex back to the cytoplasm to restore the original latent state. Thus, the activation of the NF-kB pathway is generally a transient process, lasting from 30-60 minutes in most cells. Finally, proteins in the NF-kB signaling pathway participate in a number of protein-protein interactions with non-NF-kB proteins (see PROTEIN-PROTEIN INTERACTIONS link). In addition, in many cancer cells (including breast cancer, colon cancer, prostate cancer, lymphoid cancers, and probably many others; see DISEASES link) NF-kB is constitutively active and located in the nucleus.
In some cancers, this is due to chronic stimulation of the IKK pathway, while in other cases (such as some Hodgkin’s and diffuse large B-cell lymphoma cells) the gene encoding IkB can be mutated and defective. Therefore, many current anti-tumor therapies seek to block NF-kB activity as a means to inhibit tumor growth or to sensitize the tumor cells to more conventional therapies, such as chemotherapy. We still have very little understanding of the complex in vivo dynamics of this pathway.Over-expression studies in tissue culture almost certainly do not accurately reflect physiological signaling events. Similarly, what controls the balance between the levels of the various heterodimeric complexes in vivo is not known. In all cases, these structures have been derived from molecules that contain almost exclusively residues from the RH domain. As such, these studies provide rather static glimpses of these factors at work. Several molecular and biochemical studies indicate that Rel dimers assume distinct conformations when bound to DNA versus as free or IkB-bound dimers or when bound to different kB sites. Moreover, such studies have also indicated that C-terminal residues influence sequences within the RH domain. Therefore, we cannot accurately simulate the dynamic nature of the complex as it releases from IkB, enters the nucleus, binds to DNA, and enhances gene expression; however, mathematical and computational modeling of the NF-kB pathway is beginning to address the dynamics of the pathway in response to various signals. In addition, recent studies suggest that NF-kB complexes bind to specific promoters in a dynamic on-off manner, with occupancy of a specific promoter sequence by an individual NF-kB dimer lasting on the order of seconds.
For example, the following issues remain murky: 1) precisely which proteins are in the IKK complex in all cell types; 2) the exact size of the complex in all cell types; 3) what is the physiological relevance of phosphorylation by the IKK complex of substrates other than IkB; 4) how the various NF-kB and non-NF-kB activation pathways converge on IKK (for example, what and how many upstream kinases can activate IKK); 5) how is IKK activated by what appears to be induced clustering; 6) how is it that one subunit of this complex (IKKa) controls a specific developmental process, namely keratinocyte differentiation; 7) all of the other signaling pathways that crosstalk via or to IKK; 8) how do the two catalytic kinases within the IKK complex act on substrate proteins; and 9) how do reactive oxygen species and reactive Cysteine residues impact IKK activity. Recent X-ray crystal structural information on the IKK protein and components of the IKK complex may help answer some of these questions. However, v-Rel has accumulated so many activating mutations that it may not be a precise model for the role of these transcription factors in human cancers, where a single mutation (or gene amplification event) has occurred. However, there are over 800 compounds that have been shown to inhibit NF-kB signaling (see INHIBITORS at this site), and thus, the physiological or pharmacological utility of using any single compound for inhibition of NF-kB activity is a bit muddled. Nevertheless, our knowledge of the molecular details of this pathway is enabling the development of more specific and potent inhibitors of NF-kB signaling, and indeed, some NF-kB signaling inhibitors are entering clinical trials. The revised nomenclature reflects the new members of this pathway, common usage over the past several years, and at times my own judgment. In most cases, the choice was quite simple, although the p65 vs. RelA decision continues to be a thorny one.
For more information on the Gilmore lab, go to the link for THE LAB. Nuclear Factor-kappaB: Regulation and Role in Disease. Kluwer Academic Publishes, Dordrecht, The Netherlands. 426 pages NF-kB: from basic research to human disease. Oncogene (Reviews) 51: 6679-6899 Nature Reviews Molecular Cell Biology 8: 40-62 Shown are the generalized structures of the two classes of Rel transcription factors. Class I proteins have additional inserted sequences in the RH domain. The C-terminal halves of the class I Rel proteins have ankyrin repeat-containing inhibitory domains, which can be removed by proteasome-mediated proteolysis (PROTEASE). The C-terminal halves of the class II Rel proteins have transcriptional activation domains. IKK then phosphorylates IkB at 2 N-terminal serines, which signals it for ubiquitination and proteolysis. Freed NF-kB (p50-RelA, in this case) enters the nucleus and activates gene expression. One NF-kB target gene encodes IkB. The newly synthesized IkB can enter the nucleus, pull NF-kB off DNA, and export NF-kB back to its resting state in the cytoplasm. Thick lines indicate the activating pathway; thin lines indicate the inactivating pathway. These stimuli may trigger inflammation, innate immune responses, adaptive immune responses, secondary lymphoid organ development and osteoclastogenesis. In principle, every isoform of one molecule type can interact with every member of the adjacent family, but differential affinities make some interactions much more likely than others (see text). As a consequence, this is commonly referred to as the DimD. Structural studies have revealed three primary mechanisms that regulate the assembly of monomers into active dimers. The contribution made by each amino-acid position has been studied by alanine scanning mutagenesis and by in vivo selection for p50 ( Sengchanthalangsy et al., 1999; Hart et al., 2001 ).
Results from these experiments reveal that only a few of these interfacial residues (Y267, L269, D302 and V310; murine p50 numbering) contribute energy to the p50 homodimer formation. Involvement of the hydroxyl groups of tyrosine in cross-subunit hydrogen bonding may explain why the phenylalanine-containing RelA and c-Rel homodimers are weaker than the p50 homodimer. Alteration of this residue to an alanine enhances stability, whereas an asparagine at this position further destabilizes p50 homodimer. Another important dimer regulatory residue is alanine at position 307. Substitution of this residue with any other amino acid destabilizes the p50 homodimer. For example, although the subunit interfaces of RelA and c-Rel homodimers appear identical and all 12 subunit-contacting residues are in common, RelA and c-Rel display differences in their ability to heterodimerize with p50; the c-Rel homodimer appears to be more stable than the RelA homodimer.Although these observations are made qualitatively from in vitro co-refolding experiments, they are not inconsistent with in vivo results. From a vast body of work in many cell types, one can say with some confidence that the p50:RelA heterodimer is much more abundant than the RelA:RelA homodimer, with the abundance of the c-Rel:c-Rel homodimer and p50:c-Rel heterodimer being intermediate. However, RelB is unable to form a stable homodimer in vivo and forms a domain swapped, or intertwined homodimer in vitro ( Figure 3a ) ( Huang et al., 2005b ). Substitution of N287 to D or A does not alter the fate of the RelB homodimer in vitro, eliminating this residue as the sole determinant of RelB's unusual dimerization properties. Thus, RelB is capable of two alternate conformations and dimerization behaviors, one that allows for DNA binding and one that does not. What may be the biological significance of these two dimer forms?
Although the intertwined dimer has low affinity and is unstable, such interactions may occur transiently within the dynamic molecular events of gene regulation. Intriguingly, RelB has been reported to have both positive and negative transcriptional activities ( Saccani et al., 2003; Bonizzi et al., 2004; Jacque et al., 2005 ), but the molecular basis for alternate activities remains unknown. The AT-rich sequence is known to possess a higher propensity for bending, with longer stretches being more prone to bending. The N-terminal domain (NTD) of the RHD, which like the DimD folds into an Ig-like domain, makes both base-specific and non-specific contacts with the DNA. The DimD also makes DNA contacts, but these contacts are sequence non-specific. In addition, the linker peptide connecting the two domains also makes both specific and non-specific contacts with the DNA. The most significant contribution is made by loop L1, which is located near the start of the NTD ( Figure 3b ). This loop encompasses five base-contacting residues in murine p50 (R54, R56, Y57, E60 and H64) and four base-contacting residues in murine RelA (R33, R35, Y36 and E39) and c-Rel (R21, R23, Y24 and E27). The conserved tyrosine residue in loop L1, in addition to making van der Waals contacts with two central pyrimidines (preferably thymines), also interacts with the DNA phosphate backbone. The results of such studies generally correlate with in vitro binding data by EMSA, but as others have observed this experimental approach may not allow for conclusions of transcriptional specificity of the endogenous gene. The transfected reporter gene is in molecular excess over cooperating endogenous molecules, is not wrapped in nucleosomes or within its native chromatin environment. Therefore, recent studies have attempted to determine the transcriptional specificity rules of endogenous genes.
To characterize the molecular basis of the narrowly defined immunological phenotypes associated with c-Rel deficiency, several genes have been identified as specifically requiring c-Rel for activation. In a subsequent study ( Leung et al., 2004 ) the specific dimer requirement was further found to be stimulus-dependent. Interestingly, chromatin immunoprecipitation (ChIP) analysis revealed that RelA was bound to the IP-10 promoter even when the RelA homodimer did not allow for gene activation ( Leung et al., 2004 ), indicating that the interaction with presumed co-activators did not result in cooperativity at the level of DNA binding, but possibly at the level of downstream core promoter activation events. Indeed, the transient nature of gene expression is the basis for the resolution of inflammation and so the molecular attenuation mechanisms that limit inflammatory signaling have received attention ( Han and Ulevitch, 2005 ). Typical representatives TNF-R1 and TLR4, which mediate TNF and LPS signaling, respectively, were found to produce remarkably different IKK induction profiles ( Werner et al., 2005 ), which in the case of TNF are independent of the stimulus concentration ( Cheong et al., 2006 ). A current research focus is the elucidation of the mechanisms that produce stimulus-specific IKK activities. This may correlate with the distinct physiological functions in inflammation and immune signaling versus development and homeostasis of secondary lymphoid structures or control of bone homeostasis. Cellular stimulation may be thought of to result in a dozen distinct (although partially overlapping) waves of different dimers, a subset of which may contact or probe the regulatory region of a particular gene, resulting in transcriptionally active or inactive complexes. These events must be coordinated to produce specific regulation.
In this model, two different but coordinated signaling inputs must act in a defined temporal sequence on a promoter; stimulus specificity in gene expression could be achieved by triggering the same signaling pathways in an alternate sequence. An additional interesting aspect of this model is that it provides an example of how nucleosomes can act as mediators of transcription factor cooperativity. Current and future work may not only involve studies of single model promoters, but may benefit from systematic approaches that will identify groups of co-regulated genes and reveal basic regulatory principles. Multiple levels of analysis and investigation will be required. However, applying these models to in vivo regulation will be a challenge. Defined genetic perturbation (e.g., knockouts) and a panel of well-defined stimulation conditions will prove useful. Third, high throughput measurements of coordinated signaling pathways, secondary and tertiary signaling events will be required.Gilmore TD. (2006). Oncogene (this issue). Linnell J, Mott R, Field S, Kwiatkowski DP, Ragoussis J, Udalova IA. (2004). Nucleic Acids Res 32: e44. Perkins ND. (2006). Oncogene (this issue). Scheidereit C. (2006). Oncogene (this issue). Download references Acknowledgements In the interest of clarity, we have narrowly focused this review and apologize for not citing many important contributions. We thank Amanda Fusco, Soumen Basak, and Shannon Werner for reading the manuscript, and laboratory members and colleagues for interesting discussions. Work on related topics in our laboratories is funded by NIH GM72024 and GM071573 (AH), NIH CA71718 and GM071862 (GG), and the Human Frontier Science Program and Italian Association for Research on Cancer (GN). Download citation Published: 30 October 2006 Issue Date: 30 October 2006 DOI: Keywords NF-kappaB IkappaB transcription signal transduction combinatorial control dynamic control. Please consider upgrading your browser.
UniProtKB - Q04206This score cannot be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein. More. - Experimental evidence at protein level i Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. More. Select a section on the left to see content. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.
Essential for cytokine gene expression in T-cells (PubMed: 15790681 ). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. 8 Publications GO - Molecular function i actinin binding Source: UniProtKB Complete GO annotation on QuickGO. GO - Biological process i acetaldehyde metabolic process Source: Ensembl aging Source: Ensembl animal organ morphogenesis Source: Ensembl cellular defense response Source: UniProtKB Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest. More. Keywords i Molecular function Activator, DNA-binding Biological process Host-virus interaction, Transcription, Transcription regulation Enzyme and pathway databases Pathway Commons web resource for biological pathway data More. PathwayCommons i Q04206 Reactome - a knowledgebase of biological pathways and processes More. SABIO-RK i Q04206 SignaLink: a signaling pathway resource with multi-layered regulatory networks More. SignaLink i Q04206 SIGNOR Signaling Network Open Resource More. SIGNOR i Q04206 Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'. More. Gene names i Name: RELA Synonyms: NFKB3 The component name refers to the genomic component encoding a set of proteins. More. Component i: Chromosome 11 Organism-specific databases Eukaryotic Pathogen and Host Database Resources More. EuPathDB i HostDB:ENSG00000173039.18 Human Gene Nomenclature Database More. HGNC i HGNC:9955 ?, RELA Online Mendelian Inheritance in Man (OMIM) More. MIM i 164014 ?, gene neXtProt; the human protein knowledge platform More. Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B) (PubMed: 1493333 ). Colocalized with DDX1 in the nucleus upon TNF-alpha induction (PubMed: 19058135 ). Colocalizes with GFI1 in the nucleus after LPS stimulation (PubMed: 20547752 ).