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Items 1 to 10 of about 3316
1. Evans BJ, Kwon T: Molecular Polymorphism and Divergence of Duplicated Genes in Tetraploid African Clawed Frogs (Xenopus). Cytogenet Genome Res; 2015;145(3-4):243-52
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Molecular Polymorphism and Divergence of Duplicated Genes in Tetraploid African Clawed Frogs (Xenopus).
  • Genome duplication creates redundancy in proteins and their interaction networks, and subsequent smaller-scale gene duplication can further amplify genetic redundancy.
  • Mutations then lead to the loss, maintenance or functional divergence of duplicated genes.
  • Genome duplication occurred many times in African clawed frogs (genus Xenopus), and almost all extant species in this group evolved from a polyploid ancestor.
  • To better understand the nature of selective constraints in a polyploid genome, we examined molecular polymorphism and divergence of duplicates and single-copy genes in 2 tetraploid African clawed frog species, Xenopus laevis and X. victorianus.
  • We found that molecular polymorphism in the coding regions of putative duplicated genes was higher than in singletons, but not significantly so.
  • Our findings also suggest that transcriptome evolution in polyploids is influenced by variation in the genome-wide mutation rate, and do not reject the hypothesis that gene dosage balance is also important.
  • [MeSH-major] Evolution, Molecular. Gene Duplication. Polymorphism, Genetic / genetics. Tetraploidy. Xenopus / genetics
  • [MeSH-minor] Animals. Chromosome Mapping. Gene Dosage. Models, Genetic. Open Reading Frames / genetics. Phylogeny. Untranslated Regions / genetics

  • figshare. supplemental materials - Supporting Data and Materials for the article .
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  • (PMID = 26066830.001).
  • [ISSN] 1424-859X
  • [Journal-full-title] Cytogenetic and genome research
  • [ISO-abbreviation] Cytogenet. Genome Res.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Review
  • [Publication-country] Switzerland
  • [Chemical-registry-number] 0 / Untranslated Regions
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2. Kwon T, Cho SH: Draft Genome Sequence of Enterohemorrhagic Escherichia coli O157 NCCP15739, Isolated in the Republic of Korea. Genome Announc; 2015;3(3)
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  • [Title] Draft Genome Sequence of Enterohemorrhagic Escherichia coli O157 NCCP15739, Isolated in the Republic of Korea.
  • Enterohemorrhagic Escherichia coli (EHEC) is the main cause of the recent outbreaks of diarrhea, hemolytic-uremic syndrome (HUS), and hemorrhagic colitis worldwide.
  • Herein, we present the draft genome sequence of the NCCP15739 isolate from a patient in the Republic of Korea.

  • REBASE - The Restriction Enzyme Database. gene/protein/disease-specific - REBASE ref# 19865 .
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  • [Copyright] Copyright © 2015 Kwon and Cho.
  • (PMID = 26021919.001).
  • [ISSN] 2169-8287
  • [Journal-full-title] Genome announcements
  • [ISO-abbreviation] Genome Announc
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Other-IDs] NLM/ PMC4447904
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3. Vogel C, Marcotte EM: Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat Rev Genet; 2012 Apr;13(4):227-32
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  • [Title] Insights into the regulation of protein abundance from proteomic and transcriptomic analyses.
  • Recent advances in next-generation DNA sequencing and proteomics provide an unprecedented ability to survey mRNA and protein abundances.
  • Such proteome-wide surveys are illuminating the extent to which different aspects of gene expression help to regulate cellular protein abundances.
  • Current data demonstrate a substantial role for regulatory processes occurring after mRNA is made - that is, post-transcriptional, translational and protein degradation regulation - in controlling steady-state protein abundances.
  • Intriguing observations are also emerging in relation to cells following perturbation, single-cell studies and the apparent evolutionary conservation of protein and mRNA abundances.
  • Here, we summarize current understanding of the major factors regulating protein expression.
  • [MeSH-major] Proteins / genetics. Proteins / metabolism. RNA, Messenger / metabolism
  • [MeSH-minor] Gene Expression Profiling. Proteome / metabolism. Proteomics / methods

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  • [Cites] Mol Cell Proteomics. 2002 May;1(5):376-86 [12118079.001]
  • [Cites] Yeast. 2000 Sep 15;16(12):1131-45 [10953085.001]
  • [Cites] Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6940-5 [12771378.001]
  • [Cites] Nature. 2003 Oct 16;425(6959):737-41 [14562106.001]
  • [Cites] PLoS Biol. 2004 Jun;2(6):e137 [15124029.001]
  • [Cites] Mol Cell Proteomics. 2004 Dec;3(12):1154-69 [15385600.001]
  • [Cites] J Mass Spectrom. 2005 Apr;40(4):430-43 [15838939.001]
  • [Cites] J Proteome Res. 2005 Jul-Aug;4(4):1073-85 [16083256.001]
  • [Cites] Cell. 2005 Dec 16;123(6):1025-36 [16360033.001]
  • [Cites] Nature. 2006 Jun 15;441(7095):840-6 [16699522.001]
  • [Cites] Cell Cycle. 2006 Jul;5(14):1503-5 [16861887.001]
  • [Cites] Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13004-9 [16916930.001]
  • [Cites] PLoS Biol. 2006 Oct;4(10):e309 [17048983.001]
  • [Cites] Nat Biotechnol. 2007 Jan;25(1):117-24 [17187058.001]
  • [Cites] Anal Bioanal Chem. 2007 Oct;389(4):1017-31 [17668192.001]
  • [Cites] PLoS One. 2008;3(5):e2097 [18461186.001]
  • [Cites] Science. 2008 Jun 20;320(5883):1643-7 [18566288.001]
  • [Cites] Nature. 2008 Sep 4;455(7209):64-71 [18668037.001]
  • [Cites] Nature. 2008 Sep 4;455(7209):58-63 [18668040.001]
  • [Cites] Nature. 2008 Oct 30;455(7217):1251-4 [18820680.001]
  • [Cites] Science. 2008 Nov 7;322(5903):918-23 [18988847.001]
  • [Cites] DNA Res. 2009 Feb;16(1):45-58 [19001483.001]
  • [Cites] PLoS Biol. 2009 Mar 3;7(3):e48 [19260763.001]
  • [Cites] Science. 2009 Apr 10;324(5924):218-23 [19213877.001]
  • [Cites] Bioinformatics. 2009 Jun 1;25(11):1397-403 [19318424.001]
  • [Cites] Nature. 2009 Aug 6;460(7256):762-5 [19606093.001]
  • [Cites] Cell. 2009 Aug 21;138(4):673-84 [19703394.001]
  • [Cites] FEBS Lett. 2009 Dec 17;583(24):3966-73 [19850042.001]
  • [Cites] Mol Biosyst. 2009 Dec;5(12):1512-26 [20023718.001]
  • [Cites] Mol Cell Proteomics. 2010 Feb;9(2):271-84 [19955083.001]
  • [Cites] Proteomics. 2010 Mar;10(6):1297-306 [20077411.001]
  • [Cites] Nat Biotechnol. 2010 Jul;28(7):695-709 [20622844.001]
  • [Cites] Science. 2010 Jul 30;329(5991):533-8 [20671182.001]
  • [Cites] Mol Syst Biol. 2010 Aug 24;6:400 [20739923.001]
  • [Cites] Mol Syst Biol. 2010 Aug 24;6:406 [20739928.001]
  • [Cites] Proteomics. 2010 Dec;10(23):4209-12 [21089048.001]
  • [Cites] Mol Syst Biol. 2010 Dec 21;6:450 [21179022.001]
  • [Cites] Nat Struct Mol Biol. 2011 Jan;18(1):27-34 [21131977.001]
  • [Cites] Science. 2011 Feb 11;331(6018):764-8 [21233346.001]
  • [Cites] Nature. 2011 May 19;473(7347):337-42 [21593866.001]
  • [Cites] Mol Syst Biol. 2011;7:497 [21654674.001]
  • [Cites] Mol Syst Biol. 2011;7:511 [21772259.001]
  • [Cites] Mol Syst Biol. 2011;7:514 [21772262.001]
  • [Cites] Nature. 2011 Jul 21;475(7356):308-15 [21776076.001]
  • [Cites] Trends Genet. 2011 Aug;27(8):316-22 [21763027.001]
  • [Cites] Methods Mol Biol. 2011;759:407-25 [21863500.001]
  • [Cites] Nat Genet. 2011 Sep;43(9):854-9 [21857679.001]
  • [Cites] Nat Rev Genet. 2011 Oct;12(10):671-82 [21897427.001]
  • [Cites] Cell. 2011 Nov 11;147(4):789-802 [22056041.001]
  • [Cites] Mol Cell Proteomics. 2011 Dec;10(12):M111.009217 [21933953.001]
  • [Cites] J Biol Chem. 2010 Jan 22;285(4):2221-6 [19955182.001]
  • [Cites] Genome Res. 2003 Feb;13(2):216-23 [12566399.001]
  • (PMID = 22411467.001).
  • [ISSN] 1471-0064
  • [Journal-full-title] Nature reviews. Genetics
  • [ISO-abbreviation] Nat. Rev. Genet.
  • [Language] eng
  • [Grant] United States / NIGMS NIH HHS / GM / DP1 GM106408; United States / NIGMS NIH HHS / GM / R01 GM076536
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Proteins; 0 / Proteome; 0 / RNA, Messenger
  • [Other-IDs] NLM/ NIHMS395043; NLM/ PMC3654667
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4. Choi H: Cultural marginality: a concept analysis with implications for immigrant adolescents. Issues Compr Pediatr Nurs; 2001 Jul-Sep;24(3):193-206
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Cultural marginality: a concept analysis with implications for immigrant adolescents.
  • Society in the United States is becoming increasingly culturally diverse.
  • In 1996, almost 1 in 10 people living in the United States was a foreign-born immigrant and the number of foreign-born in the population exceeded 25 million.
  • However, the lack of mutual understanding between health care providers and immigrants, particularly children and adolescents, has impeded progress in research and practice for this population.
  • To facilitate nurses' understanding of immigrant adolescents' unique experiences, this article explores the concept of cultural marginality.
  • Cultural margin ality is defined by the author as "situations and feelings of passive betweeness when people exist between two different cultures and do not yet perceive themselves as centrally belonging to either one."
  • Using Walker and Avant's (1995) method as a framework, my article identifies attributes, antecedents, and consequences of cultural marginality in the context of immigrant adolescents' experiences.
  • To clarify the abstract concept, cases are provided that distill meanings of the concept in life.
  • A conceptual model has been synthesized to illustrate relationships among attributes, antecedents, and consequences and to highlight areas for further inquiry.
  • Concept analysis is a critical step for the develop ment of nursing knowledge.
  • The process of concept analysis is demonstrated through clarification of the concept of cultural marginality, which offers guidance for nursing research and practice within the immigrant adolescent population.
  • [MeSH-major] Cultural Diversity
  • [MeSH-minor] Adolescent. Concept Formation / physiology. Emigration and Immigration. Humans. United States / epidemiology

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  • (PMID = 12141837.001).
  • [ISSN] 0146-0862
  • [Journal-full-title] Issues in comprehensive pediatric nursing
  • [ISO-abbreviation] Issues Compr Pediatr Nurs
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] United States
  • [Number-of-references] 50
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5. Kwon T, Kim SW: Fiber-optic interferometer for surface profile measurement with vibration suppression. Opt Express; 2011 Feb 28;19(5):4223-30
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Fiber-optic interferometer for surface profile measurement with vibration suppression.
  • We describe an improved design of fiber-optic interferometer intended to measure surface profiles with enhanced capability of vibration suppression.
  • The reference wavefront is generated directly from the measurement wave using a multi-mode fiber that eliminates only the spatial wavefront distortion by means of bend loss.
  • The temporal fluctuation caused by vibration is consequently cancelled out in the process of interference since it becomes to exist in both the measurement and reference waves.
  • Further, an injection locking technique is incorporated to stabilize the reference wave intensity and hence make stable the interferometric fringe intensity.
  • Experimental result proves that the proposed fiber-optic interferometer is capable of producing sub-wavelength measurement precision even in the presence of severe vibration with 100-μm amplitude.
  • [MeSH-major] Artifacts. Fiber Optic Technology / instrumentation. Interferometry / instrumentation. Materials Testing / instrumentation. Photometry / instrumentation
  • [MeSH-minor] Equipment Design. Equipment Failure Analysis. Surface Properties. Vibration

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  • (PMID = 21369252.001).
  • [ISSN] 1094-4087
  • [Journal-full-title] Optics express
  • [ISO-abbreviation] Opt Express
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
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6. Vogel C, Marcotte EM: Label-free protein quantitation using weighted spectral counting. Methods Mol Biol; 2012;893:321-41
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  • [Title] Label-free protein quantitation using weighted spectral counting.
  • Mass spectrometry (MS)-based shotgun proteomics allows protein identifications even in complex biological samples.
  • Protein abundances can then be estimated from the counts of MS/MS spectra attributable to each protein, provided that one corrects for differential MS-detectability of the contributing peptides.
  • We describe the use of a method, APEX, which calculates Absolute Protein EXpression levels based on learned correction factors, MS/MS spectral counts, and each protein's probability of correct identification.The APEX-based calculations consist of three parts:.
  • (1) Using training data, peptide sequences and their sequence properties, a model is built that can be used to estimate MS-detectability (O (i)) for any given protein. (2) Absolute abundances of proteins measured in an MS/MS experiment are calculated with information from spectral counts, identification probabilities and the learned O (i)-values. (3) Simple statistics allow for significance analysis of differential expression in two distinct biological samples, i.e., measuring relative protein abundances.
  • APEX-based protein abundances span more than four orders of magnitude and are applicable to mixtures of hundreds to thousands of proteins from any type of organism.
  • [MeSH-major] Peptide Mapping / methods. Software
  • [MeSH-minor] Algorithms. Amino Acid Sequence. Animals. Cell Extracts / chemistry. Fungal Proteins / chemistry. Fungal Proteins / metabolism. Humans. Molecular Sequence Data. Peptide Fragments / chemistry. Proteome / chemistry. Proteome / metabolism. Proteomics. Tandem Mass Spectrometry

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  • [Cites] Nat Biotechnol. 2004 Feb;22(2):214-9 [14730315.001]
  • [Cites] J Proteome Res. 2003 Nov-Dec;2(6):643-9 [14692458.001]
  • [Cites] Anal Chem. 2004 Jul 15;76(14):4193-201 [15253663.001]
  • [Cites] J Theor Biol. 1968 Nov;21(2):170-201 [5700434.001]
  • [Cites] J Biol Chem. 1971 Apr 10;246(7):2211-7 [5555568.001]
  • [Cites] Macromolecules. 1978 Jan-Feb;11(1):9-15 [621952.001]
  • [Cites] Adv Enzymol Relat Areas Mol Biol. 1978;47:45-148 [364941.001]
  • [Cites] Biochim Biophys Acta. 1984 Jun 28;787(3):221-6 [6547351.001]
  • [Cites] Biophys J. 1985 Jan;47(1):61-70 [3978191.001]
  • [Cites] Proteins. 1994 Jun;19(2):141-9 [8090708.001]
  • [Cites] Mol Cell Biol. 1999 Mar;19(3):1720-30 [10022859.001]
  • [Cites] Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6591-6 [10359756.001]
  • [Cites] Mol Cell Biol. 1999 Nov;19(11):7357-68 [10523624.001]
  • [Cites] J Proteome Res. 2004 Nov-Dec;3(6):1138-48 [15595722.001]
  • [Cites] Rapid Commun Mass Spectrom. 2005;19(13):1844-50 [15945033.001]
  • [Cites] Mol Cell Proteomics. 2005 Jul;4(7):887-901 [15824125.001]
  • [Cites] J Am Soc Mass Spectrom. 2005 Aug;16(8):1231-8 [15978832.001]
  • [Cites] Nat Rev Mol Cell Biol. 2005 Jul;6(7):577-83 [15957003.001]
  • [Cites] Mol Cell Proteomics. 2005 Aug;4(8):1205-9 [15911532.001]
  • [Cites] Mol Cell Proteomics. 2005 Sep;4(9):1265-72 [15958392.001]
  • [Cites] Mol Cell Proteomics. 2006 Jan;5(1):144-56 [16219938.001]
  • [Cites] Nat Chem Biol. 2005 Oct;1(5):252-62 [16408053.001]
  • [Cites] Nat Biotechnol. 2006 Mar;24(3):333-8 [16525410.001]
  • [Cites] Cell. 2006 Apr 7;125(1):173-86 [16615898.001]
  • [Cites] Nature. 2006 Jun 15;441(7095):840-6 [16699522.001]
  • [Cites] Bioinformatics. 2006 Jul 15;22(14):e481-8 [16873510.001]
  • [Cites] Nat Biotechnol. 2007 Jan;25(1):117-24 [17187058.001]
  • [Cites] Nat Biotechnol. 2007 Jan;25(1):125-31 [17195840.001]
  • [Cites] Mol Syst Biol. 2007;3:79 [17299416.001]
  • [Cites] J Proteome Res. 2008 Mar;7(3):855-65 [18275136.001]
  • [Cites] Science. 2008 May 16;320(5878):938-41 [18436743.001]
  • [Cites] Nat Protoc. 2008;3(9):1444-51 [18772871.001]
  • [Cites] BMC Bioinformatics. 2008;9:529 [19068132.001]
  • [Cites] PLoS Biol. 2009 Mar 3;7(3):e48 [19260763.001]
  • [Cites] Nature. 2009 Aug 6;460(7256):762-5 [19606093.001]
  • [Cites] Mol Syst Biol. 2010 Aug 24;6:400 [20739923.001]
  • [Cites] Proteomics. 2010 Dec;10(23):4209-12 [21089048.001]
  • [Cites] Nature. 1986 Jan 16-22;319(6050):199-203 [3945310.001]
  • [Cites] Int J Pept Protein Res. 1988 Oct;32(4):269-78 [3209351.001]
  • [Cites] Mol Cell Proteomics. 2002 May;1(5):376-86 [12118079.001]
  • [Cites] Trends Biotechnol. 2002 Sep;20(9):361-4 [12175758.001]
  • [Cites] Nature. 2002 Oct 3;419(6906):520-6 [12368866.001]
  • [Cites] Anal Chem. 2002 Oct 15;74(20):5383-92 [12403597.001]
  • [Cites] Proteomics. 2002 Oct;2(10):1374-91 [12422355.001]
  • [Cites] Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6940-5 [12771378.001]
  • [Cites] Nature. 2003 Oct 16;425(6959):737-41 [14562106.001]
  • [Cites] Anal Chem. 2003 Sep 1;75(17):4646-58 [14632076.001]
  • [Cites] Nucleic Acids Res. 2004 Jan 1;32(Database issue):D293-5 [14681416.001]
  • [Cites] Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3833-8 [15007177.001]
  • (PMID = 22665309.001).
  • [ISSN] 1940-6029
  • [Journal-full-title] Methods in molecular biology (Clifton, N.J.)
  • [ISO-abbreviation] Methods Mol. Biol.
  • [Language] eng
  • [Grant] United States / NIGMS NIH HHS / GM / R01 GM076536
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Cell Extracts; 0 / Fungal Proteins; 0 / Peptide Fragments; 0 / Proteome
  • [Other-IDs] NLM/ NIHMS395003; NLM/ PMC3654649
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7. Choi H, Scholl BJ: Perceiving causality after the fact: postdiction in the temporal dynamics of causal perception. Perception; 2006;35(3):385-99
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Perceiving causality after the fact: postdiction in the temporal dynamics of causal perception.
  • In simple dynamic events we can easily perceive not only motion, but also higher-level properties such as causality, as when we see one object collide with another.
  • Several researchers have suggested that such causal perception is an automatic and stimulus-driven process, sensitive only to particular sorts of visual information, and a major research project has been to uncover the nature of these visual cues.
  • Here, rather than investigating what information affects causal perception, we instead explore the temporal dynamics of when certain types of information are used.
  • Surprisingly, we find that certain visual events can determine whether we perceive a collision in an ambiguous situation even when those events occur after the moment of potential 'impact' in the putative collision has already passed.
  • This illustrates a type of postdictive perception: our conscious perception of the world is not an instantaneous moment-by-moment construction, but rather is formed by integrating information presented within short temporal windows, so that new information which is obtained can influence the immediate past in our conscious awareness.
  • Such effects have been previously demonstrated for low-level motion phenomena, but the present results demonstrate that postdictive processes can influence higher-level event perception.
  • These findings help to characterize not only the 'rules' of causal perception, but also the temporal dynamics of how and when those rules operate.
  • [MeSH-major] Causality. Motion Perception / physiology
  • [MeSH-minor] Cues. Humans. Judgment. Photic Stimulation / methods. Psychological Tests. Time Factors. Vision, Ocular / physiology

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  • (PMID = 16619953.001).
  • [ISSN] 0301-0066
  • [Journal-full-title] Perception
  • [ISO-abbreviation] Perception
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
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8. Land M, Vogel C, Gefeller O: Partitioning methods for multifactorial risk attribution. Stat Methods Med Res; 2001 Jun;10(3):217-30
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] Partitioning methods for multifactorial risk attribution.
  • The epidemiological problem of risk attribution in the framework of multiple exposures has been the subject of intensive research activities in the last decade.
  • In particular, partitioning methods have been developed to define new multidimensional measures of attributable risk putting the task of quantifying a proportion of disease events in a population that can be ascribed to the adverse health effects of certain risk factors into a multifactorial perspective.
  • The parameters generalize the concept of attributable risk to different multifactorial frameworks in which multiple exposures might be arranged in hierarchically ordered classes or in equally ranking groups.
  • Partitioning methods are reviewed and differences between the multifactorial variants of attributable risk are illustrated by a component causes model.
  • [MeSH-major] Algorithms. Risk Assessment / methods
  • [MeSH-minor] Causality. Epidemiologic Methods. Epidemiologic Studies. Humans

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  • (PMID = 11446149.001).
  • [ISSN] 0962-2802
  • [Journal-full-title] Statistical methods in medical research
  • [ISO-abbreviation] Stat Methods Med Res
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
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9. Chun J, Kwon T, Lee EJ, Hyun S, Hong SK, Kang SS: The subcellular localization of 3-phosphoinositide-dependent protein kinase is controlled by caveolin-1 binding. Biochem Biophys Res Commun; 2005 Jan 7;326(1):136-46
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] The subcellular localization of 3-phosphoinositide-dependent protein kinase is controlled by caveolin-1 binding.
  • 3-Phosphoinositide-dependent protein kinase 1 (PDK1), a member of the serine/threonine kinase family, has been demonstrated to be crucial for cellular survival, differentiation, and metabolism.
  • Here, we present evidence that PDK1 is associated with caveolin-1, a 22-kDa integral membrane protein, which is the principal structural and regulatory component of the caveolae membranes in COS-1.
  • First, we noted the presence of two potential caveolin-1 binding motifs ((141)FFVKLYFTF(149) and (299)YDFPEKFF(306)) in the PDK1 catalytic domain.
  • Using a pull-down approach, we observed that PDK1 interacts physically with caveolin-1 both in vivo and in vitro.
  • Second, we detected the co-localization of PDK1 and caveolin-1 via confocal microscopy.
  • The localization of PDK1 to the plasma membrane was disrupted by caveolin binding.
  • Third, in transient transfection assays, interaction with caveolin-1 induced a substantial reduction in the in vivo serine/threonine phosphorylation of PDK1, whereas the caveolin-1 binding site mutant ((141)FFVKLYFTF(149) and (299)YDFPEKFF(306) change to (141)AFVKLAFTA(149) and (299)ADAPEFLA(306)) did not.
  • Furthermore, a caveolin-1 scaffolding peptide (amino acids 82-101) functionally suppressed the self-phosphorylation and kinase activities of purified recombinant PDK1 protein.
  • Thus, our observations indicated that PDK1 binds to caveolin-1 through its caveolin-binding motifs, and also that the protein-protein interaction between PDK1 and caveolin-1 regulates PDK1 self-phosphorylation, kinase activity, and subcellular localization.
  • [MeSH-major] Caveolins / metabolism. Protein-Serine-Threonine Kinases / chemistry. Protein-Serine-Threonine Kinases / metabolism. Subcellular Fractions / metabolism
  • [MeSH-minor] 3-Phosphoinositide-Dependent Protein Kinases. Amino Acid Sequence. Animals. Binding Sites. CHO Cells. Caveolin 1. Cricetinae. Cricetulus. Enzyme Activation. Humans. Molecular Sequence Data. Protein Binding. Protein Structure, Tertiary. Structure-Activity Relationship. Substrate Specificity

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  • (PMID = 15567163.001).
  • [ISSN] 0006-291X
  • [Journal-full-title] Biochemical and biophysical research communications
  • [ISO-abbreviation] Biochem. Biophys. Res. Commun.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / CAV1 protein, human; 0 / Caveolin 1; 0 / Caveolins; EC 2.7.11.1 / 3-Phosphoinositide-Dependent Protein Kinases; EC 2.7.11.1 / PDPK1 protein, human; EC 2.7.11.1 / Protein-Serine-Threonine Kinases
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10. Silva GM, Finley D, Vogel C: K63 polyubiquitination is a new modulator of the oxidative stress response. Nat Struct Mol Biol; 2015 Feb;22(2):116-23
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • [Title] K63 polyubiquitination is a new modulator of the oxidative stress response.
  • Ubiquitination is a post-translational modification that signals multiple processes, including protein degradation, trafficking and DNA repair.
  • Polyubiquitin accumulates globally during the oxidative stress response, and this has been mainly attributed to increased ubiquitin conjugation and perturbations in protein degradation.
  • Here we show that the unconventional Lys63 (K63)-linked polyubiquitin accumulates in the yeast Saccharomyces cerevisiae in a highly sensitive and regulated manner as a result of exposure to peroxides.
  • We demonstrate that hydrogen peroxide inhibits the deubiquitinating enzyme Ubp2, leading to accumulation of K63 conjugates assembled by the Rad6 ubiquitin conjugase and the Bre1 ubiquitin ligase.
  • Using linkage-specific isolation methods and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics, we identified >100 new K63-polyubiquitinated targets, which were substantially enriched in ribosomal proteins.
  • Finally, we demonstrate that impairment of K63 ubiquitination during oxidative stress affects polysome stability and protein expression, rendering cells more sensitive to stress, and thereby reveal a new redox-regulatory role for this modification.
  • [MeSH-major] Oxidative Stress / physiology. Ubiquitination / physiology
  • [MeSH-minor] Endopeptidases / metabolism. Lysine / chemistry. Lysine / metabolism. Polyubiquitin / metabolism. Protein Processing, Post-Translational. Proteolysis. Saccharomyces cerevisiae / metabolism. Saccharomyces cerevisiae Proteins / metabolism. Ubiquitin-Conjugating Enzymes / metabolism

  • Gene Ontology. gene/protein/disease-specific - Gene Ontology annotations from this paper .
  • Hazardous Substances Data Bank. L-Lysine .
  • Saccharomyces Genome Database. Saccharomyces Genome Database .
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  • [Cites] Nature. 2001 Aug 2;412(6846):553-7 [11484057.001]
  • [Cites] Nature. 2003 Dec 18;426(6968):895-9 [14685250.001]
  • [Cites] Nature. 2010 Sep 9;467(7312):179-84 [20829789.001]
  • [Cites] Nat Cell Biol. 2010 Dec;12(12):1177-85 [21076411.001]
  • [Cites] Cell. 2007 Dec 14;131(6):1084-96 [18083099.001]
  • [Cites] Genetics. 2012 Oct;192(2):319-60 [23028185.001]
  • [Cites] Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17394-9 [23045643.001]
  • [Cites] Nat Commun. 2013;4:1568 [23463011.001]
  • [Cites] EMBO Rep. 2009 May;10(5):466-73 [19373254.001]
  • [Cites] Mol Cell Proteomics. 2011 Dec;10(12):M111.009217 [21933953.001]
  • [Cites] Proc Natl Acad Sci U S A. 2012 Jul 3;109(27):10837-42 [22699496.001]
  • [Cites] Biochem Soc Trans. 2009 Oct;37(Pt 5):937-53 [19754430.001]
  • [Cites] Genetics. 2012 Apr;190(4):1157-95 [22209905.001]
  • [Cites] J Biol Chem. 2006 Dec 1;281(48):36724-31 [17028178.001]
  • [Cites] Cell. 2000 Jul 7;102(1):67-76 [10929714.001]
  • [Cites] Cell Rep. 2012 Dec 27;2(6):1475-84 [23219552.001]
  • [Cites] Antioxid Redox Signal. 2011 Jul 1;15(1):191-203 [21126188.001]
  • [Cites] Mol Cell. 2008 Jul 11;31(1):57-66 [18614047.001]
  • [Cites] Mol Cell. 2009 Feb 13;33(3):275-86 [19217402.001]
  • [Cites] Mol Cell Proteomics. 2012 Nov;11(11):1475-88 [22865924.001]
  • [Cites] Nature. 2000 Nov 9;408(6809):239-47 [11089981.001]
  • [Cites] Hum Mol Genet. 2008 Feb 1;17(3):431-9 [17981811.001]
  • [Cites] Annu Rev Plant Biol. 2004;55:373-99 [15377225.001]
  • [Cites] Nat Rev Mol Cell Biol. 2009 Aug;10(8):550-63 [19626045.001]
  • [Cites] J Biol Chem. 2006 Sep 29;281(39):29011-21 [16849329.001]
  • [Cites] J Cell Biol. 2008 Aug 25;182(4):663-73 [18725537.001]
  • [Cites] Cell. 2009 Apr 3;137(1):133-45 [19345192.001]
  • [Cites] EMBO J. 2009 Feb 18;28(4):359-71 [19153599.001]
  • [Cites] Mol Cell. 2003 Jan;11(1):267-74 [12535539.001]
  • [Cites] Nature. 2002 Sep 12;419(6903):135-41 [12226657.001]
  • [Cites] Annu Rev Pharmacol Toxicol. 2004;44:239-67 [14744246.001]
  • [Cites] J Biol Chem. 2005 Mar 18;280(11):9879-86 [15632126.001]
  • [Cites] Biochim Biophys Acta. 2008 Nov;1780(11):1217-35 [18178164.001]
  • [Cites] Microbiology. 2007 Jan;153(Pt 1):247-53 [17185553.001]
  • [Cites] J Biol Chem. 2003 Sep 12;278(37):34739-42 [12876294.001]
  • [Cites] J Cell Biol. 2009 May 4;185(3):493-502 [19398763.001]
  • [Cites] Mol Cell. 2010 Aug 13;39(3):477-84 [20655260.001]
  • [Cites] Cell. 2000 Oct 13;103(2):351-61 [11057907.001]
  • [Cites] Curr Opin Microbiol. 2002 Dec;5(6):602-7 [12457705.001]
  • [Cites] Mol Cell. 2011 Oct 21;44(2):325-40 [21906983.001]
  • [Cites] Nat Cell Biol. 2005 Aug;7(8):750-7 [16056266.001]
  • [Cites] J Biol Chem. 2010 Jan 22;285(4):2361-7 [19923226.001]
  • [Cites] Biochem J. 2010 Dec 15;432(3):585-94 [20919990.001]
  • [Cites] FASEB J. 2005 Oct;19(12):1707-9 [16099947.001]
  • [Cites] Physiol Rev. 2002 Jan;82(1):47-95 [11773609.001]
  • [Cites] Nature. 2004 Jan 8;427(6970):167-71 [14695475.001]
  • [Cites] Annu Rev Biochem. 2009;78:363-97 [19489724.001]
  • [Cites] Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7351-5 [1651502.001]
  • [Cites] Genes Cells. 2009 Feb;14(2):271-80 [19170772.001]
  • [Cites] Biotechniques. 2007 Feb;42(2):158, 160, 162 [17373478.001]
  • [Cites] J Cell Biol. 2008 Apr 21;181(2):293-307 [18426977.001]
  • [Cites] EMBO Rep. 2012 Apr;13(4):331-8 [22370727.001]
  • [Cites] Nat Commun. 2014;5:4763 [25159004.001]
  • [Cites] J Biol Chem. 2003 Jan 3;278(1):311-8 [12401807.001]
  • [Cites] Nat Biotechnol. 2003 Aug;21(8):921-6 [12872131.001]
  • [Cites] Front Plant Sci. 2014 Jan 31;5:15 [24550925.001]
  • [Cites] Comp Biochem Physiol C Toxicol Pharmacol. 2007 Jul-Aug;146(1-2):180-93 [17045551.001]
  • [Cites] Mol Cell Biol. 1995 Mar;15(3):1265-73 [7862120.001]
  • [Cites] Physiol Rev. 2002 Apr;82(2):373-428 [11917093.001]
  • [Cites] Proc Natl Acad Sci U S A. 1980 Apr;77(4):1783-6 [6990414.001]
  • [Cites] Science. 2010 Nov 26;330(6008):1203-9 [21109664.001]
  • (PMID = 25622294.001).
  • [ISSN] 1545-9985
  • [Journal-full-title] Nature structural & molecular biology
  • [ISO-abbreviation] Nat. Struct. Mol. Biol.
  • [Language] eng
  • [Grant] United States / NIGMS NIH HHS / GM / R01 GM043601; United States / NIGMS NIH HHS / GM / R01 GM113237; United States / NIGMS NIH HHS / GM / GM43601
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bre1 protein, S cerevisiae; 0 / Saccharomyces cerevisiae Proteins; 120904-94-1 / Polyubiquitin; EC 2.3.2.23 / RAD6 protein, S cerevisiae; EC 2.3.2.23 / Ubiquitin-Conjugating Enzymes; EC 3.4.- / Endopeptidases; EC 3.4.99.- / ubiquitin-Nalpha-protein hydrolase; K3Z4F929H6 / Lysine
  • [Other-IDs] NLM/ NIHMS649187; NLM/ PMC4318705
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