degradation RpoS proteolysis forms another level of the sigma factor s regulation. Degradation occurs ... factors known to regulate RpoS proteolysis but via incompletely characterized mechanisms include ... translation, and LrhA and acetyl phosphate affects RpoS proteolysis by possibly acting as a phosphoryl ... more details
Unreferenced date October 2006 Protein turnover is the balance between protein synthesis and Proteolysis protein degradation . More synthesis than breakdown indicates an anabolic state that builds lean tissues, more breakdown than synthesis indicates a catabolic state that burns lean tissues. Protein turnover is believed to decrease with age in all senescence organisms including humans. This results in an increase in the amount of damaged protein within the body. It is unknown if this is a cause or consequence of aging but it seems likely that it is in fact both. The damaged protein results in a slower protein turnover which then results in more damaged protein causing an exponential increase in damage to all protein within the body and to aging. Some bodybuilding supplement s claim to reduce the protein breakdown by reducing or blocking the number of catabolic hormones within the body. This is believed to increase anabolism. However if protein breakdown falls too low then the body would not be able to remove muscle cells that have been damaged during workouts which would in turn prevent the growth of new muscle cells. When older proteins are broken down in the body, they must be replaced. This concept is called protein turnover, and different types of proteins have very different turnover rates. Protein synthesis occurs during the process of Translation biology translation on ribosome s. Protein breakdown occurs generally in two cellular locations br lysosome Lysosomal protease s digest endocytosis endocytosed proteins br cytoplasm Cytoplasmic complexes, called proteasome s, digest older or abnormal proteins that have been tagged with ubiquitin for destruction. DEFAULTSORT Protein Turnover Category Protein biosynthesis Protein stub ... more details
A PEST sequence is a peptide sequence which is rich in proline P , glutamic acid E , serine S , and threonine T . This sequence is associated with protein s that have a short intracellular half life hence, it is hypothesized that the PEST sequence acts as a signal peptide for Proteolysis protein degradation . ref cite journal author Rogers S, Wells R, Rechsteiner M title Amino acid sequences common to rapidly degraded proteins the PEST hypothesis journal Science volume 234 issue 4774 pages 364 8 year 1986 pmid 2876518 doi 10.1126 science.2876518 ref The degradation may be mediated possibly via the proteosome ref cite journal author Reverte CG, Ahearn MD, Hake LE title CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome journal Dev. Biol. volume 231 issue 2 pages 447 58 year 2001 pmid 11237472 doi 10.1006 dbio.2001.0153 ref ref cite journal author Spencer ML, Theodosiou M, Noonan DJ title NPDC 1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin proteasome system through a PEST degradation motif journal J. Biol. Chem. volume 279 issue 35 pages 37069 78 year 2004 pmid 15229225 doi 10.1074 jbc.M402507200 ref or calpain . ref cite journal author Shumway SD, Maki M, Miyamoto S title The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu calpain journal J. Biol. Chem. volume 274 issue 43 pages 30874 81 year 1999 pmid 10521480 doi 10.1074 jbc.274.43.30874 ref References references Category Proteins Category Posttranslational modification molecular cell biology stub es Secuencia PEST ... more details
enzyme Name citryl CoA lyase EC number 4.1.3.34 CAS number 131095 35 7 IUBMB EC number 4 1 3 34 GO code 0008816 image width caption In enzymology , a citryl CoA lyase EC number 4.1.3.34 is an enzyme that catalysis catalyzes the chemical reaction 3S citryl CoA math rightleftharpoons math acetyl CoA oxaloacetate Hence, this enzyme has one substrate biochemistry substrate , 3S citryl CoA , and two product chemistry products , acetyl CoA and oxaloacetate . This enzyme belongs to the family of lyase s, specifically the oxo acid lyases, which cleave carbon carbon bonds . The systematic name of this enzyme class is 3S citryl CoA oxaloacetate lyase acetyl CoA forming . This enzyme is also called 3S citryl CoA oxaloacetate lyase . This enzyme participates in citrate cycle tca cycle . References reflist 1 cite journal author Dimroth P, Loyal R, Eggerer H date 1977 title Characterization of the isolated transferase subunit of citrate lyase as a CoA Transferase. Evidence against a covalent enzyme substrate intermediate journal Eur. J. Biochem. volume 80 pages 479&ndash 88 pmid 336371 doi 10.1111 j.1432 1033.1977.tb11903.x issue 2 cite journal author Lill U, Schreil A, Eggerer H date 1982 title Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase journal Eur. J. Biochem. volume 125 pages 645&ndash 50 pmid 6749502 doi 10.1111 j.1432 1033.1982.tb06731.x issue 3 4.1 enzyme stub Category EC 4.1.3 Category Enzymes of unknown structure ... more details
enzyme Name citrate CoA ligase EC number 6.2.1.18 CAS number 856428 87 0 IUBMB EC number 6 2 1 18 GO code 0047779 image width caption In enzymology , a citrate CoA ligase EC number 6.2.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP citrate CoA math rightleftharpoons math ADP phosphate 3S citryl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , citrate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 3S citryl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is citrate CoA ligase ADP forming . Other names in common use include citryl CoA synthetase , citrate CoA ligase , and citrate thiokinase . This enzyme participates in citric acid cycle . References reflist 1 cite journal author Lill U, Schreil A, Eggerer H date 1982 title Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase journal Eur. J. Biochem. volume 125 pages 645&ndash 50 pmid 6749502 doi 10.1111 j.1432 1033.1982.tb06731.x issue 3 cite journal author Aoshima M, Ishii M, Igarashi Y date 2004 title A novel enzyme, citryl CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK 6 journal Mol. Microbiol. volume 52 pages 751&ndash 61 pmid 15101981 doi 10.1111 j.1365 2958.2004.04009.x issue 3 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name ATP citrate synthase EC number 2.3.3.8 CAS number 9027 95 6 IUBMB EC number 2 3 3 8 GO code 0003878 image width caption In enzymology , an ATP citrate synthase EC number 2.3.3.8 is an enzyme that catalysis catalyzes the chemical reaction ADP phosphate acetyl CoA oxaloacetate math rightleftharpoons math ATP citrate CoA The 4 substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP , phosphate , acetyl CoA , and oxaloacetate , whereas its 3 product chemistry products are adenosine triphosphate ATP , citrate , and coenzyme A CoA . This enzyme belongs to the family of transferase s, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl CoA oxaloacetate C acetyltransferase pro S carboxymethyl forming, ADP phosphorylating . Other names in common use include ATP citric lyase , ATP citrate oxaloacetate lyase pro S CH2COO acetyl CoA , ATP dephosphorylating , acetyl CoA oxaloacetate acetyltransferase isomerizing , ADP phosphorylating , adenosine triphosphate citrate lyase , citrate cleavage enzyme , citrate ATP lyase , citric cleavage enzyme , and ATP citrate pro S lyase . This enzyme participates in citrate cycle tca cycle and reductive carboxylate cycle co2 fixation . References reflist 1 cite journal author Lill U, Schreil A, Eggerer H date 1982 title Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase journal Eur. J. Biochem. volume 125 pages 645&ndash 50 pmid 6749502 doi 10.1111 j.1432 1033.1982.tb06731.x issue 3 cite journal author Srere PA and Lipmann F date 1953 title An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A journal J. Am. Chem. Soc. volume 75 pages 4874 doi 10.1021 ja01115a547 issue 19 transferase stub Category EC 2.3.3 Category Enzymes of unknown structure it ATP citrato sintasi ... more details
protein Name zinc metallopeptidase STE24 homolog, S. cerevisiae caption image width HGNCid 12877 Symbol ZMPSTE24 AltSymbols EntrezGene 10269 OMIM 606480 RefSeq NM 005857 UniProt O75844 PDB ECnumber 3.4.24.84 Chromosome 1 Arm p Band 34 LocusSupplementaryData ZMPSTE24 is a human gene . ref name pmid9700155 cite journal author Tam A, Nouvet FJ, Fujimura Kamada K, Slunt H, Sisodia SS, Michaelis S title Dual roles for Ste24p in yeast a factor maturation NH2 terminal proteolysis and COOH terminal CAAX processing journal J. Cell Biol. volume 142 issue 3 pages 635 49 year 1998 month August pmid 9700155 pmc 2148179 doi 10.1083 jcb.142.3.635 url http www.jcb.org cgi pmidlookup?view long&pmid 9700155 ref ref name pmid10373325 cite journal author Freije JM, Blay P, Pend s AM, Cadi anos J, Crespo P, L pez Ot n C title Identification and chromosomal location of two human genes encoding enzymes potentially involved in proteolytic maturation of farnesylated proteins journal Genomics volume 58 issue 3 pages 270 80 year 1999 month June pmid 10373325 doi 10.1006 geno.1999.5834 url ref The protein encoded by this gene is a metallopeptidase . It is involved in the processing of Lamin A . ref name pmid16207929 cite journal author Young SG, Fong LG, Michaelis S title Prelamin A, Zmpste24, misshapen cell nuclei, and progeria new evidence suggesting that protein farnesylation could be important for disease pathogenesis journal J. Lipid Res. volume 46 issue 12 pages 2531 58 year 2005 month December pmid 16207929 doi 10.1194 jlr.R500011 JLR200 url ref See also progeria References Reflist biochem stub Metalloendopeptidases de CAAX Prenylprotease 1 ... more details
Paul Gr tzner April 30, 1847 July 29, 1919 was a German physiologist who was a native of Twardog ra Festenberg , Silesia present day Twardog ra , Lower Silesian Voivodeship . He studied medicine in W rzburg , Berlin and Breslau , where he was a pupil of Rudolf Heidenhain 1834 1897 . After graduation he was an assistant at the physiological institute in Breslau. In 1881 he became a professor at the University of Bern , and in 1884 succeeded Karl von Vierordt 1818 1884 at the physiological institute at the University of T bingen . Gr tzner performed numerous studies involving the physiology of nerves and muscles, circulatory system circulatory physiology , glandular and gastric secretion s, et al. In the 1870s with Wilhelm Ebstein 1836 1912 he performed important research involving the physiochemical behavior of pepsin in the digestive system digestive tract . Findings from this research were published in an 1874 treatise called Ueber Pepsinbildung im Magen , and is included in Pfl gers Archiv. Gr tzner is credited with introducing a colorimetric method for determining the quantity of pepsin in a solution. Among his numerous written articles was an 1879 physiological study on voice and speech titled Physiologie der Stimme und Sprache . References http translate.google.com translate?hl en&sl de&u http www.zeno.org Pagel 1901 A Gr 25C3 25BCtzner, 2BPaul&sa X&oi translate&resnum 9&ct result&prev search 3Fq 3DGr 25C3 25BCtzner 2B1847 2BT 25C3 25BCbingen 26hl 3Den 26sa 3DG Pagel Biographical Dictionary translated from German http www.biochemj.org bj 071 0384 0710384.pdf Studies on Gastric Proteolysis http jp.physoc.org cgi reprint 3 3 4 269.pdf The Journal of Physiology Persondata Metadata see Wikipedia Persondata . NAME Grutzner, Paul ALTERNATIVE NAMES SHORT DESCRIPTION DATE OF BIRTH April 30, 1847 PLACE OF BIRTH DATE OF DEATH July 29, 1919 PLACE OF DEATH DEFAULTSORT Grutzner, Paul Category German physiologists Category 1847 births Category 1919 deaths Category People fro ... more details
saved book title Biochemistry subtitle An introduction cover image AminoAcidball.svg cover color black Biochemistry An introduction This collection of Wikipedia articles is intended to supplement a standard textbook of biochemistry. Students may find its explanations complement their texts for greater clarity. In some areas its information will extend past their texts. In a few areas, information is still lacking but students are warmly welcomed to make up that deficit Cells and water Biochemistry Cell biology Cells Water Structural Biochemistry Nucleic acids Nucleic acid RNA DNA Proteins and amino acids Protein Amino acid Proteinogenic amino acid Properties of the twenty amino acids Myoglobin Hemoglobin Enzyme mechanisms Enzyme catalysis Enzyme kinetics Enzyme kinetics Lipids and membranes Lipid Biological membrane Membrane protein Cell membrane Carbohydrate structure Carbohydrate Polysaccharide Intermediary metabolism Metabolism Metabolism Overview of metabolism Carbohydrate metabolism Glycolysis Gluconeogenesis Glycogen Pentose phosphate pathway Citric acid cycle Citric acid cycle Oxidative phosphorylation Oxidative phosphorylation Photosynthesis Photosynthesis Lipid metabolism Fatty acid synthesis Lipogenesis Acetyl CoA carboxylase Fatty acid degradation Beta oxidation Nitrogen metabolism Nitrogen fixation Amino acid synthesis Nucleotide Urea cycle Integration of metabolism Hormone Signal transduction Diabetes mellitus Informational Macromolecules DNA synthesis and repair DNA replication DNA repair Oncogene Oncogenes RNA synthesis and processing Transcription genetics Transcription Regulation of gene expression Protein synthesis and modifications Translation biology Translation Posttranslational modification Proteolysis Proteasome Category Wikipedia books on biology Biochemistry an introduction Category Wikipedia books on chemistry Biochemistry an introduction ... more details
orphan date October 2011 Infobox protein family Symbol EcoEI R C Name EcoEI R C image width caption Pfam PF08463 Pfam clan InterPro IPR013670 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the EcoEI R protein C terminal domain is a protein domain found at the C terminus of both the R subunit of type I restriction enzymes and the Res subunit of type III restriction enzymes. The type I enzymes include EcoEI, which recognises 5 GAGN 7 ATGC 3 the R protein HsdR is required for both nuclease and ATPase activity. ref name pmid8412658 cite journal author Murray NE, Daniel AS, Cowan GM, Sharp PM title Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes journal Mol. Microbiol. volume 9 issue 1 pages 133 43 year 1993 month July pmid 8412658 doi 10.1111 j.1365 2958.1993.tb01675.x url ref ref name pmid10449767 cite journal author Makovets S, Doronina VA, Murray NE title Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes journal Proc. Natl. Acad. Sci. U.S.A. volume 96 issue 17 pages 9757 62 year 1999 month August pmid 10449767 pmc 22283 doi 10.1073 pnas.96.17.9757 url ref References reflist InterPro content IPR013670 Category Protein families Category Protein domains ... more details
Infobox protein family Symbol HECT Name HECT domain ubiquitin transferase image PDB 1d5f EBI.jpg width caption structure of an e6ap ubch7 complex insights into the ubiquitination pathway Pfam PF00632 Pfam clan InterPro IPR000569 SMART PROSITE MEROPS SCOP 1d5f TCDB OPM family OPM protein CAZy CDD In molecular biology, the HECT domain is a protein domain found in ubiquitin protein ligases . The name HECT comes from H omologous to the E 6 AP C arboxyl T erminus . ref name pmid7708685 cite journal author Huibregtse JM, Scheffner M, Beaudenon S, Howley PM title A family of proteins structurally and functionally related to the E6 AP ubiquitin protein ligase journal Proc. Natl. Acad. Sci. U.S.A. volume 92 issue 7 pages 2563 7 year 1995 month March pmid 7708685 pmc 42258 doi url ref Protein s containing this domain at the C terminus include ubiquitin protein ligase , which regulates ubiquitination of disambiguation needed CDC25 date October 2011 . Ubiquitin protein ligase accepts ubiquitin from an ubiquitin conjugating enzyme E2 ubiquitin conjugating enzyme in the form of a thioester , and then directly transfers the ubiquitin to targeted substrate biochemistry substrates . A cysteine residue is required for ubiquitin thiolester formation. Human thyroid receptor interacting protein 12 TRIP12 , which also contains this domain, is a component of an Adenosine triphosphate ATP dependent multisubunit protein that Protein protein interaction interact s with the ligand binding domain of the thyroid hormone receptor . It could be an E3 ubiquitin protein ligase. Human UBE3A ubiquitin protein ligase E3A Protein protein interaction interact s with the E6 protein of the cancer associated Human papillomavirus type 16 and Human papillomavirus type 18. The E6 E6 AP Protein complex complex Molecular binding bind s to and targets the P53 Tumour suppressor gene tumour suppressor protein for ubiquitin mediated proteolysis . References reflist InterPro content IPR000569 Category Protein domain ... more details
PBB geneid 8505 Poly ADP ribose glycohydrolase is an enzyme that in humans is encoded by the PARG gene . ref name entrez cite web title Entrez Gene Poly ADP ribose glycohydrolase url http www.ncbi.nlm.nih.gov sites entrez?db gene&cmd retrieve&list uids 8505 accessdate 2011 11 08T12 08 44.097 08 00 ref ref name pmid9115250 cite journal author Lin W, Am JC, Aboul Ela N, Jacobson EL, Jacobson MK title Isolation and characterization of the cDNA encoding bovine poly ADP ribose glycohydrolase journal J. Biol. Chem. volume 272 issue 18 pages 11895 901 year 1997 month May pmid 9115250 doi ref ref name pmid10449915 cite journal author Am JC, Apiou F, Jacobson EL, Jacobson MK title Assignment of the poly ADP ribose glycohydrolase gene PARG to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization journal Cytogenet. Cell Genet. volume 85 issue 3 4 pages 269 70 year 1999 pmid 10449915 doi ref Poly ADP ribose glycohydrolase PARG is the major enzyme responsible for the catabolism of poly adenosine diphosphate ribose ADP ribose , a reversible covalent modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products. ref name entrez cite web title Entrez Gene Poly ADP ribose glycohydrolase url http www.ncbi.nlm.nih.gov sites entrez?db gene&cmd retrieve&list uids 8505 accessdate 2011 11 08T12 08 44.097 08 00 ref References reflist Further reading refbegin 2 Cite pmid 11053413 Cite pmid 12878198 Cite pmid 14527731 Cite pmid 14622405 Cite pmid 15081900 Cite pmid 15212953 Cite pmid 15450800 Cite pmid 15868399 Cite pmid 16117724 refend NLM content gene 10 stub Category EC 3.2.1 ... more details
PBB geneid 834 Caspase 1 is an enzyme that proteolysis proteolytically cleaves other proteins, such as the Protein precursor precursor forms of the inflammatory cytokine s interleukin 1 interleukin 1 and interleukin 18 , into active mature peptides. ref cite journal author Thornberry N, Bull H, Calaycay J, et al. title A novel heterodimeric cysteine protease is required for interleukin 1 beta processing in monocytes journal Nature volume 356 issue 6372 pages 768&ndash 74 year 1992 pmid 1574116 doi 10.1038 356768a0 ref ref cite journal author Cerretti DP, Kozlosky CJ, Mosley B, et al. title Molecular cloning of the interleukin 1 beta converting enzyme journal Science year 1992 volume 256 issue 5053 pages 97&ndash 100 pmid 1373520 doi 10.1126 science.1373520 ref It belongs to a family of cysteine protease s known as caspase s that always cleave proteins following an aspartic acid residue. ref cite journal author Black RA, Kronheim SR, Merriam JE, March CJ, Hopp TP title A pre aspartate specific protease from human leukocytes that cleaves pro interleukin 1 beta journal J Biol Chem volume 264 issue 10 year 1989 pages 5323&ndash 5326 pmid 2784432 ref Caspase 1 is produced as a zymogen that is cleaved into 20 kDa p20 and 10 kDa p10 subunits that become part of the active enzyme. Active caspase 1 contains two heterodimer s of p20 and p10. It interacts with another CARD domain containing protein called PYCARD or ASC and is involved in inflammasome formation and activation of inflammation inflammatory processes. ref cite journal author Mariathasan S, Newton K, Monack D, Vucic D, French D, Lee W, Roose Girma M, Erickson S, Dixit V title Differential activation of the inflammasome by caspase 1 adaptors ASC and Ipaf journal Nature volume 430 issue 6996 pages 213 8 year 2004 pmid 15190255 doi 10.1038 nature02664 ref Caspase 1 has been shown to induce cell necrosis or pyroptosis and may ... laysource laydate quote ref See also The Proteolysis Map Caspase References Reflist External links ... more details
and Michele Pagano 2008 . Deregulated proteolysis by the F box proteins SKP2 and TrCP tipping the scales ... hand, SCF TrCP promotes proteolysis of Emi1, an APC C Cdh1 inhibitor, and Wee1, a Cdk1 inhibitor ... more details
. This causes proteolysis , which is the directed degradation of proteins by cellular enzyme s called .... The problem occurs when the proteins do not dissolve in proteolysis. This happens because the mis folded proteins sometimes become robust enough that they are not dissolved by normal proteolysis. When the fragments do not dissolve, they get spit out of proteolysis and they aggregate to form oligomer s. The reason they aggregate is that the parts of the protein that do not dissolve in proteolysis ... more details
Intramembrane proteolysis of signal peptides an essential step in the generation of HLA E epitopes journal .... title SPPL2a and SPPL2b promote intramembrane proteolysis of TNF in activated dendritic cells to trigger ... methylation and proteolysis prior to secretion as active proteins. Type IV prepilin leader ... more details
rate. ProteolysisProteolysis is the process that breaks down proteins. It is regulated by moisture ... involved in proteolysis and must be broken down by special keratinolytic microorganisms. ref name Gupta ... The Decomposition of Hair in the Buried Body Environment isbn 1420069918 ref Proteolysis products In general, proteolysis breaks down proteins into, ref name Forbes ref name Dent proteoses peptones polypeptides amino acids Continuing proteolysis leads to the production of Phenols phenolic substances ... more details
aggregates by preventing proteolysis proteolytic cleavage and hence inhibiting fibril removal via ... LB, Pepys MB title Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer ... more details
proteolysis of p27 Kip1 at G1 phase. journal Nat. Cell Biol. volume 6 issue 12 pages 1229 35 year ..., the ubiquitin ligase that regulates proteolysis of p27 in G1 phase. journal J. Biol. Chem. volume 280 ... more details
For uses other than abbreviations Rip disambiguation Rip Wiktionary RIP TOC right R.I.P. is an abbreviation for rest in peace Latin requiescat in pace . R.I.P. or RIP may also refer to Biology Regulated intramembrane proteolysis, a biochemical process which regulates a semipermeable membrane Repeat induced point mutation , a process by which DNA in some fungi accumulates mutations Ribosome inactivating protein , a type of protein that controls ribosomes Ramus interventricularis paraconalis, branch of the right coronary artery Mathematics Restricted isometry property Computers Raster image processor , a component used in a printing system which produces a bitmap Real IP address , a term used in load balancing Recovery Is Possible , a Linux distribution Relative Instruction Pointer, an addressing mode peculiar to the X86 64 Architectural features x86 64 architecture Remote Imaging Protocol , a method of using graphics instead of text on a Bulletin Board System Routing Information Protocol , a protocol used in computer networks Row Instruction Pointer, a special purpose processor register in network processors Military R.I.P. cartridge Round, Irritant, Personnel , or tear gas cartridge, a specialist shotgun ammunition Ranger Indoctrination Program , a U.S. Army program requirement for assignment to a Ranger battalion Music RIP band , a punk band from Basque Country Spain R.I.P. Coroner album R.I.P. Coroner album , a 1987 album by thrash metal band Coroner R.I.P. Rocket from the Crypt album R.I.P. Rocket from the Crypt album , a 2008 album of a 2005 live performance by Rocket from the Crypt Rust in Peace , a 1990 album by the band Megadeth Backtracks AC DC album Track listing R.I.P. Rock in Peace , a song by AC DC that originally appeared on the Australian version of Dirty Deeds Done Dirt Cheap , but was released internationally in the 2009 box set Backtracks R.I.P. Rest in Pain , a song by Sepultura from the 1987 Schizophrenia Sepultura album Schizophrenia album Other ... more details
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