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| 003 | IT-RoAPU | ||
| 005 | 20250106152058.0 | ||
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| 008 | 241019t20221977gw fo d z ger d | ||
| 020 |
_a9783112650073 _qprint |
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| 020 |
_a9783112650080 _qPDF |
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| 024 | 7 |
_a10.1515/9783112650080 _2doi |
|
| 035 | _a(DE-B1597)9783112650080 | ||
| 035 | _a(DE-B1597)630442 | ||
| 035 | _a(OCoLC)1347247657 | ||
| 040 |
_aDE-B1597 _beng _cDE-B1597 _erda |
||
| 050 | 4 |
_aQP551 _b.A283 1977 |
|
| 072 | 7 |
_aMED008000 _2bisacsh |
|
| 082 | 0 | 4 |
_a612.3 _223 |
| 084 | _aonline - DeGruyter | ||
| 245 | 0 | 0 |
_aActa Biologica et Medica Germanica. _nBand 36, Heft 11/12, _p3rd Symposium Intracellular Protein Catabolism / _chrsg. von R. Baumann. |
| 250 | _aReprint 2022 | ||
| 264 | 1 |
_aBerlin ; _aBoston : _bDe Gruyter, _c[2022] |
|
| 264 | 4 | _c1977 | |
| 300 | _a1 online resource (476 p.) | ||
| 336 |
_atext _btxt _2rdacontent |
||
| 337 |
_acomputer _bc _2rdamedia |
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| 338 |
_aonline resource _bcr _2rdacarrier |
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| 347 |
_atext file _bPDF _2rda |
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| 490 | 0 |
_aActa Biologica et Medica Germanica ; _vBand 36, Heft 11/12 |
|
| 505 | 0 | 0 |
_tFrontmatter -- _tPreface -- _tIntracellular proteinase of Bacillus subtilis -- _tRelationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium -- _tCharacterization and function of intracellular proteinases and proteinase inhibitors from yeast -- _tProtein degradation during the differentiation of eukaryotic cells : Studies on the sporulation of Saccharomyces cerevisiae and on the formation of the neuromuscular junction in the chick embryo -- _tStudies on bovine spleen cathepsin D -- _tIntracellular protein catabolism and new serine proteases -- _tCathepsin H: An endoaminopeptidase -- _tThe effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea -- _tThe action of cathepsin B and collagenolytic cathepsin in the degradation of collagen -- _tProtein cleavage in virus-infected cells -- _tPeptidases of the kidney microvillus membrane -- _tDegradation of myofibrillar proteins by cathepsins B and D -- _tDegradation of myones as a consequence of disuse and denervation -- _tThe influence of immobilization on soluble proteins of muscle -- _tA neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes -- _tThe susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- _tStudies on the possible physiological controls of skeletal muscle proteases -- _tLysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- _tEvidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- _tIncreased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- _tAcetyl glutamate — a model of signals for intracellular proteolysis -- _tFlow and shuttle of plasma membrane during endocytosis -- _tInhibition by insulin of the physiological autophagic breakdown of cell organelles -- _tProteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- _tStudies on the relationship between the molecular structure and the catabolism of insulin -- _tInsulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- _tConversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- _tPresence of an endopeptidase activity in rat liver ribosomes -- _tImplications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- _tThe role of lysosomal enzymes in protein degradation in different types of rat liver cells -- _tUptake and degradation of asialo-fetuin by isolated rat hepatocytes -- _tEndocytosis and breakdown of proteins by sinusoidal liver cells -- _tThe accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- _tProtein degradation in isolated rat hepatocytes -- _tAttempts to relate enzyme inactivation to degradation in vivo -- _tLysosomes and protein degradation -- _tProtein degradation in rat liver cells -- _tIntracellular protein catabolism -- _tPepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- _tTurnover of lipogenic enzymes of rat liver in dependence on age -- _tAging changes in intracellular protein breakdown -- _tCooperation of various subcellular fractions in protein degradation in vitro -- _tPharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- _tBiochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- _tNaturally occurring inhibitors of intracellular proteinases -- _tIsolation and characterization of inhibitors of neutral proteinases from spleen -- _tProduction of rabbit antibodies against active rat cathepsin B -- _tRole of heparin in the interaction of serine proteinases with antithrombin III -- _tProtease inhibitors produced by microorganisms -- _tInhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- _tStudies on the in vivo-action of leupeptin on the nitrogen retention in rats -- _tInactivation studies of cathepsin D with diazo compounds -- _tInhibition of serine proteinases by benzamidine derivatives -- _tStudies on some effectors of lysosomal proteinases from rat liver -- _tEndogenous proteolytic activity of chromatin -- _tDegradation of phosphorylated chromosomal nonhistone proteins -- _tInteraction of intracellular proteases and immune mechanisms -- _tThe diversity of cellular proteinases in physiology and pathology -- _tCONTENTS/ СОДЕРЖАНИЕ/ INHALT |
| 506 | 0 |
_arestricted access _uhttp://purl.org/coar/access_right/c_16ec _fonline access with authorization _2star |
|
| 530 | _aIssued also in print. | ||
| 538 | _aMode of access: Internet via World Wide Web. | ||
| 546 | _aIn German. | ||
| 588 | 0 | _aDescription based on online resource; title from PDF title page (publisher's Web site, viewed 19. Oct 2024) | |
| 650 | 0 |
_aProteins _xMetabolism. |
|
| 650 | 4 | _aAutophagie. | |
| 650 | 4 | _aBiochemie. | |
| 650 | 4 | _aChromatinabbau. | |
| 650 | 4 | _aDiazo-Verbindungen. | |
| 650 | 4 | _aEndozytose. | |
| 650 | 4 | _aGlykoproteinabbau. | |
| 650 | 4 | _aHefeproteasen. | |
| 650 | 4 | _aImmunmechanismen. | |
| 650 | 4 | _aImmunreaktionen. | |
| 650 | 4 | _aInsulinabbau. | |
| 650 | 4 | _aKollagenabbau. | |
| 650 | 4 | _aLiposomen. | |
| 650 | 4 | _aLysosomen. | |
| 650 | 4 | _aMuskelschwund. | |
| 650 | 4 | _aNukleasen. | |
| 650 | 4 | _aOrganelleabbau. | |
| 650 | 4 | _aProteasen. | |
| 650 | 4 | _aProteinabbau. | |
| 650 | 4 | _aProteininhibition. | |
| 650 | 4 | _aProteolyse. | |
| 650 | 4 | _aStickstoffretention. | |
| 650 | 4 | _aVirusinfektion. | |
| 650 | 4 | _aenzymatische Aktivität. | |
| 650 | 4 | _alysosomale Enzyme. | |
| 650 | 4 | _aphosphorylierte Proteine. | |
| 650 | 7 |
_aMEDICAL / Biochemistry. _2bisacsh |
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| 700 | 1 |
_aAbramov, Z. T. _eautore |
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| 850 | _aIT-RoAPU | ||
| 856 | 4 | 0 | _uhttps://doi.org/10.1515/9783112650080 |
| 856 | 4 | 0 | _uhttps://www.degruyter.com/isbn/9783112650080 |
| 856 | 4 | 2 |
_3Cover _uhttps://www.degruyter.com/document/cover/isbn/9783112650080/original |
| 942 | _cEB | ||
| 999 |
_c280061 _d280061 |
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