Acta Biologica et Medica Germanica. / Band 36, Heft 11/12, : 3rd Symposium Intracellular Protein Catabolism / / hrsg. von R. Baumann.
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Place / Publishing House: | Berlin ;, Boston : : De Gruyter, , [2022] ©1977 |
Year of Publication: | 2022 |
Edition: | Reprint 2022 |
Language: | German |
Series: | Acta Biologica et Medica Germanica ;
Band 36, Heft 11/12 |
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Physical Description: | 1 online resource (476 p.) |
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Acta Biologica et Medica Germanica. Band 36, Heft 11/12, 3rd Symposium Intracellular Protein Catabolism / hrsg. von R. Baumann. Reprint 2022 Berlin ; Boston : De Gruyter, [2022] ©1977 1 online resource (476 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier text file PDF rda Acta Biologica et Medica Germanica ; Band 36, Heft 11/12 Frontmatter -- Preface -- Intracellular proteinase of Bacillus subtilis -- Relationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium -- Characterization and function of intracellular proteinases and proteinase inhibitors from yeast -- Protein 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 -- Studies on bovine spleen cathepsin D -- Intracellular protein catabolism and new serine proteases -- Cathepsin H: An endoaminopeptidase -- The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea -- The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen -- Protein cleavage in virus-infected cells -- Peptidases of the kidney microvillus membrane -- Degradation of myofibrillar proteins by cathepsins B and D -- Degradation of myones as a consequence of disuse and denervation -- The influence of immobilization on soluble proteins of muscle -- A neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes -- The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- Studies on the possible physiological controls of skeletal muscle proteases -- Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- Acetyl glutamate — a model of signals for intracellular proteolysis -- Flow and shuttle of plasma membrane during endocytosis -- Inhibition by insulin of the physiological autophagic breakdown of cell organelles -- Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- Studies on the relationship between the molecular structure and the catabolism of insulin -- Insulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- Presence of an endopeptidase activity in rat liver ribosomes -- Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- The role of lysosomal enzymes in protein degradation in different types of rat liver cells -- Uptake and degradation of asialo-fetuin by isolated rat hepatocytes -- Endocytosis and breakdown of proteins by sinusoidal liver cells -- The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- Protein degradation in isolated rat hepatocytes -- Attempts to relate enzyme inactivation to degradation in vivo -- Lysosomes and protein degradation -- Protein degradation in rat liver cells -- Intracellular protein catabolism -- Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- Turnover of lipogenic enzymes of rat liver in dependence on age -- Aging changes in intracellular protein breakdown -- Cooperation of various subcellular fractions in protein degradation in vitro -- Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- Naturally occurring inhibitors of intracellular proteinases -- Isolation and characterization of inhibitors of neutral proteinases from spleen -- Production of rabbit antibodies against active rat cathepsin B -- Role of heparin in the interaction of serine proteinases with antithrombin III -- Protease inhibitors produced by microorganisms -- Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- Studies on the in vivo-action of leupeptin on the nitrogen retention in rats -- Inactivation studies of cathepsin D with diazo compounds -- Inhibition of serine proteinases by benzamidine derivatives -- Studies on some effectors of lysosomal proteinases from rat liver -- Endogenous proteolytic activity of chromatin -- Degradation of phosphorylated chromosomal nonhistone proteins -- Interaction of intracellular proteases and immune mechanisms -- The diversity of cellular proteinases in physiology and pathology -- CONTENTS/ СОДЕРЖАНИЕ/ INHALT restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star Issued also in print. Mode of access: Internet via World Wide Web. In German. Description based on online resource; title from PDF title page (publisher's Web site, viewed 04. Okt 2022) NON-CLASSIFIABLE. bisacsh Abramov, Z. T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Airhart, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Anachkova, B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ansorge, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Aronson jr., N. N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bakay, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ballard, F. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Banno, Yoshiko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Barrett, Alan J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Baumann, R., editor. edt http://id.loc.gov/vocabulary/relators/edt Berg, T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Betz, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Beynon, Robert J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bielka, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bird, J. W. C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bohley, P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Booth, A. G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bouma, J. M. W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Brandenburg, D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Brezesinski, G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bruno, M. K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Brzin, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Carney, Ian T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Chaloupka, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb De La Morena, E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dean, Roger T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dron, D. I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dunn, W. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Duursma, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Etherington, D. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Evans, P. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ferenčik, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Francis, G. L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Friedrich, K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Giraldi, T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Grisolia, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gruber, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Guba, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gubenšek, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hedge, A. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hermann, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Holzer, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hood, W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hopgood, M. F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Iborra, J.-L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Isotova, L. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jahr, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jones, R. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Katunuma, Nobuhiko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kay, John, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Keilová, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kenny, A. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Khairallah, E. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Khairallah, L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kirschke, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Knook, D. L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Knowles, S. E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kobayashi, Keiko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koelsch, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koenig, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kohler, E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kohnert, K.-D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kominami, Eiki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kooistra, T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kopitar, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Korant, B. D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kotulová, D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kovačič, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kregar, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Langner, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lapanje, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lasch, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lindigkeit, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lu, C. Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Macnair, R. D. C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Markwardt, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Murgašová, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mészáros, Magda G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nisi, C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ohkuma, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Papachristodoulou, D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pfeifer, U., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Philippová, L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pierart-Gallois, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Poole, B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Puchalsky, D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Reglero, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Richter, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Riemann, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rivas, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Romer, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rubio, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Russev, G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Römer, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Salama, Z. B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sanada, Yukihiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schmidt, G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schmidt, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schneider, Y. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schottelius, B. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schwartz, W. N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Schön, E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Seglen, P. O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Simon, O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sohár, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Solheim, A. E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Spanier, A. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Stanovnik, B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Starkey, Phyllis M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Stauber, W. T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Steiner, D. F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Stepanov, V. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Strnadová, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Strongin, A. Ya., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Stürzebecher, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Suhar, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Sönksen, P. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Takács, Ö., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Thomas, J. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tišler, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tolleshaug, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tomášek, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Trouet, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tulkens, P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Turk, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Umezawa, Hamao, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Urh, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Walsmann, P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Warburton, M. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Welfle, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Wiederanders, B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Zühlke, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Čechová, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Štefanovič, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb print 9783112650073 https://doi.org/10.1515/9783112650080 https://www.degruyter.com/isbn/9783112650080 Cover https://www.degruyter.com/document/cover/isbn/9783112650080/original |
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German |
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Abramov, Z. T., Abramov, Z. T., Airhart, J., Airhart, J., Anachkova, B., Anachkova, B., Ansorge, S., Ansorge, S., Aronson jr., N. N., Aronson jr., N. N., Bakay, R., Bakay, R., Ballard, F. J., Ballard, F. J., Banno, Yoshiko, Banno, Yoshiko, Barrett, Alan J., Barrett, Alan J., Baumann, R., Baumann, R., Berg, T., Berg, T., Betz, H., Betz, H., Beynon, Robert J., Beynon, Robert J., Bielka, H., Bielka, H., Bird, J. W. C., Bird, J. W. C., Bohley, P., Bohley, P., Booth, A. G., Booth, A. G., Bouma, J. M. W., Bouma, J. M. W., Brandenburg, D., Brandenburg, D., Brezesinski, G., Brezesinski, G., Bruno, M. K., Bruno, M. K., Brzin, J., Brzin, J., Carney, Ian T., Carney, Ian T., Chaloupka, J., Chaloupka, J., De La Morena, E., De La Morena, E., Dean, Roger T., Dean, Roger T., Dron, D. I., Dron, D. I., Dunn, W. A., Dunn, W. A., Duursma, A., Duursma, A., Etherington, D. J., Etherington, D. J., Evans, P. J., Evans, P. J., Ferenčik, M., Ferenčik, M., Francis, G. L., Francis, G. L., Friedrich, K., Friedrich, K., Giraldi, T., Giraldi, T., Grisolia, S., Grisolia, S., Gruber, M., Gruber, M., Guba, F., Guba, F., Gubenšek, F., Gubenšek, F., Hedge, A. M., Hedge, A. M., Hermann, V., Hermann, V., Holzer, H., Holzer, H., Hood, W., Hood, W., Hopgood, M. F., Hopgood, M. F., Iborra, J.-L., Iborra, J.-L., Isotova, L. S., Isotova, L. S., Jahr, H., Jahr, H., Jones, R. H., Jones, R. H., Katunuma, Nobuhiko, Katunuma, Nobuhiko, Kay, John, Kay, John, Keilová, H., Keilová, H., Kenny, A. J., Kenny, A. J., Khairallah, E. A., Khairallah, E. A., Khairallah, L., Khairallah, L., Kirschke, H., Kirschke, H., Knook, D. L., Knook, D. L., Knowles, S. E., Knowles, S. E., Kobayashi, Keiko, Kobayashi, Keiko, Koelsch, R., Koelsch, R., Koenig, H., Koenig, H., Kohler, E., Kohler, E., Kohnert, K.-D., Kohnert, K.-D., Kominami, Eiki, Kominami, Eiki, Kooistra, T., Kooistra, T., Kopitar, M., Kopitar, M., Korant, B. D., Korant, B. D., Kotulová, D., Kotulová, D., Kovačič, M., Kovačič, M., Kregar, I., Kregar, I., Langner, J., Langner, J., Lapanje, S., Lapanje, S., Lasch, J., Lasch, J., Lindigkeit, R., Lindigkeit, R., Lu, C. Y., Lu, C. Y., Macnair, R. D. C., Macnair, R. D. C., Markwardt, F., Markwardt, F., Murgašová, I., Murgašová, I., Mészáros, Magda G., Mészáros, Magda G., Nisi, C., Nisi, C., Ohkuma, S., Ohkuma, S., Papachristodoulou, D., Papachristodoulou, D., Pfeifer, U., Pfeifer, U., Philippová, L., Philippová, L., Pierart-Gallois, M., Pierart-Gallois, M., Poole, B., Poole, B., Puchalsky, D., Puchalsky, D., Reglero, A., Reglero, A., Richter, V., Richter, V., Riemann, S., Riemann, S., Rivas, J., Rivas, J., Romer, I., Romer, I., Rubio, V., Rubio, V., Russev, G., Russev, G., Römer, I., Römer, I., Salama, Z. B., Salama, Z. B., Sanada, Yukihiro, Sanada, Yukihiro, Schmidt, G., Schmidt, G., Schmidt, S., Schmidt, S., Schneider, Y. J., Schneider, Y. J., Schottelius, B. A., Schottelius, B. A., Schwartz, W. N., Schwartz, W. N., Schön, E., Schön, E., Seglen, P. O., Seglen, P. O., Simon, O., Simon, O., Sohár, I., Sohár, I., Solheim, A. E., Solheim, A. E., Spanier, A. M., Spanier, A. M., Stanovnik, B., Stanovnik, B., Starkey, Phyllis M., Starkey, Phyllis M., Stauber, W. T., Stauber, W. T., Steiner, D. F., Steiner, D. F., Stepanov, V. M., Stepanov, V. M., Strnadová, M., Strnadová, M., Strongin, A. Ya., Strongin, A. Ya., Stürzebecher, J., Stürzebecher, J., Suhar, A., Suhar, A., Sönksen, P. H., Sönksen, P. H., Takács, Ö., Takács, Ö., Thomas, J. H., Thomas, J. H., Tišler, M., Tišler, M., Tolleshaug, H., Tolleshaug, H., Tomášek, V., Tomášek, V., Trouet, A., Trouet, A., Tulkens, P., Tulkens, P., Turk, V., Turk, V., Umezawa, Hamao, Umezawa, Hamao, Urh, I., Urh, I., Walsmann, P., Walsmann, P., Warburton, M. J., Warburton, M. J., Welfle, H., Welfle, H., Wiederanders, B., Wiederanders, B., Zühlke, H., Zühlke, H., Čechová, J., Čechová, J., Štefanovič, J., Štefanovič, J., |
author_facet |
Abramov, Z. T., Abramov, Z. T., Airhart, J., Airhart, J., Anachkova, B., Anachkova, B., Ansorge, S., Ansorge, S., Aronson jr., N. N., Aronson jr., N. N., Bakay, R., Bakay, R., Ballard, F. J., Ballard, F. J., Banno, Yoshiko, Banno, Yoshiko, Barrett, Alan J., Barrett, Alan J., Baumann, R., Baumann, R., Berg, T., Berg, T., Betz, H., Betz, H., Beynon, Robert J., Beynon, Robert J., Bielka, H., Bielka, H., Bird, J. W. C., Bird, J. W. C., Bohley, P., Bohley, P., Booth, A. G., Booth, A. G., Bouma, J. M. W., Bouma, J. M. W., Brandenburg, D., Brandenburg, D., Brezesinski, G., Brezesinski, G., Bruno, M. K., Bruno, M. K., Brzin, J., Brzin, J., Carney, Ian T., Carney, Ian T., Chaloupka, J., Chaloupka, J., De La Morena, E., De La Morena, E., Dean, Roger T., Dean, Roger T., Dron, D. I., Dron, D. I., Dunn, W. A., Dunn, W. A., Duursma, A., Duursma, A., Etherington, D. J., Etherington, D. J., Evans, P. J., Evans, P. J., Ferenčik, M., Ferenčik, M., Francis, G. L., Francis, G. L., Friedrich, K., Friedrich, K., Giraldi, T., Giraldi, T., Grisolia, S., Grisolia, S., Gruber, M., Gruber, M., Guba, F., Guba, F., Gubenšek, F., Gubenšek, F., Hedge, A. M., Hedge, A. M., Hermann, V., Hermann, V., Holzer, H., Holzer, H., Hood, W., Hood, W., Hopgood, M. F., Hopgood, M. F., Iborra, J.-L., Iborra, J.-L., Isotova, L. S., Isotova, L. S., Jahr, H., Jahr, H., Jones, R. H., Jones, R. H., Katunuma, Nobuhiko, Katunuma, Nobuhiko, Kay, John, Kay, John, Keilová, H., Keilová, H., Kenny, A. J., Kenny, A. J., Khairallah, E. A., Khairallah, E. A., Khairallah, L., Khairallah, L., Kirschke, H., Kirschke, H., Knook, D. L., Knook, D. L., Knowles, S. E., Knowles, S. E., Kobayashi, Keiko, Kobayashi, Keiko, Koelsch, R., Koelsch, R., Koenig, H., Koenig, H., Kohler, E., Kohler, E., Kohnert, K.-D., Kohnert, K.-D., Kominami, Eiki, Kominami, Eiki, Kooistra, T., Kooistra, T., Kopitar, M., Kopitar, M., Korant, B. D., Korant, B. D., Kotulová, D., Kotulová, D., Kovačič, M., Kovačič, M., Kregar, I., Kregar, I., Langner, J., Langner, J., Lapanje, S., Lapanje, S., Lasch, J., Lasch, J., Lindigkeit, R., Lindigkeit, R., Lu, C. Y., Lu, C. Y., Macnair, R. D. C., Macnair, R. D. C., Markwardt, F., Markwardt, F., Murgašová, I., Murgašová, I., Mészáros, Magda G., Mészáros, Magda G., Nisi, C., Nisi, C., Ohkuma, S., Ohkuma, S., Papachristodoulou, D., Papachristodoulou, D., Pfeifer, U., Pfeifer, U., Philippová, L., Philippová, L., Pierart-Gallois, M., Pierart-Gallois, M., Poole, B., Poole, B., Puchalsky, D., Puchalsky, D., Reglero, A., Reglero, A., Richter, V., Richter, V., Riemann, S., Riemann, S., Rivas, J., Rivas, J., Romer, I., Romer, I., Rubio, V., Rubio, V., Russev, G., Russev, G., Römer, I., Römer, I., Salama, Z. B., Salama, Z. B., Sanada, Yukihiro, Sanada, Yukihiro, Schmidt, G., Schmidt, G., Schmidt, S., Schmidt, S., Schneider, Y. J., Schneider, Y. J., Schottelius, B. A., Schottelius, B. A., Schwartz, W. N., Schwartz, W. N., Schön, E., Schön, E., Seglen, P. O., Seglen, P. O., Simon, O., Simon, O., Sohár, I., Sohár, I., Solheim, A. E., Solheim, A. E., Spanier, A. M., Spanier, A. M., Stanovnik, B., Stanovnik, B., Starkey, Phyllis M., Starkey, Phyllis M., Stauber, W. T., Stauber, W. T., Steiner, D. F., Steiner, D. F., Stepanov, V. M., Stepanov, V. M., Strnadová, M., Strnadová, M., Strongin, A. Ya., Strongin, A. Ya., Stürzebecher, J., Stürzebecher, J., Suhar, A., Suhar, A., Sönksen, P. H., Sönksen, P. H., Takács, Ö., Takács, Ö., Thomas, J. H., Thomas, J. H., Tišler, M., Tišler, M., Tolleshaug, H., Tolleshaug, H., Tomášek, V., Tomášek, V., Trouet, A., Trouet, A., Tulkens, P., Tulkens, P., Turk, V., Turk, V., Umezawa, Hamao, Umezawa, Hamao, Urh, I., Urh, I., Walsmann, P., Walsmann, P., Warburton, M. J., Warburton, M. J., Welfle, H., Welfle, H., Wiederanders, B., Wiederanders, B., Zühlke, H., Zühlke, H., Čechová, J., Čechová, J., Štefanovič, J., Štefanovič, J., |
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author_sort |
Abramov, Z. T., |
title |
Acta Biologica et Medica Germanica. |
spellingShingle |
Acta Biologica et Medica Germanica. Acta Biologica et Medica Germanica ; Frontmatter -- Preface -- Intracellular proteinase of Bacillus subtilis -- Relationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium -- Characterization and function of intracellular proteinases and proteinase inhibitors from yeast -- Protein 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 -- Studies on bovine spleen cathepsin D -- Intracellular protein catabolism and new serine proteases -- Cathepsin H: An endoaminopeptidase -- The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea -- The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen -- Protein cleavage in virus-infected cells -- Peptidases of the kidney microvillus membrane -- Degradation of myofibrillar proteins by cathepsins B and D -- Degradation of myones as a consequence of disuse and denervation -- The influence of immobilization on soluble proteins of muscle -- A neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes -- The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- Studies on the possible physiological controls of skeletal muscle proteases -- Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- Acetyl glutamate — a model of signals for intracellular proteolysis -- Flow and shuttle of plasma membrane during endocytosis -- Inhibition by insulin of the physiological autophagic breakdown of cell organelles -- Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- Studies on the relationship between the molecular structure and the catabolism of insulin -- Insulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- Presence of an endopeptidase activity in rat liver ribosomes -- Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- The role of lysosomal enzymes in protein degradation in different types of rat liver cells -- Uptake and degradation of asialo-fetuin by isolated rat hepatocytes -- Endocytosis and breakdown of proteins by sinusoidal liver cells -- The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- Protein degradation in isolated rat hepatocytes -- Attempts to relate enzyme inactivation to degradation in vivo -- Lysosomes and protein degradation -- Protein degradation in rat liver cells -- Intracellular protein catabolism -- Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- Turnover of lipogenic enzymes of rat liver in dependence on age -- Aging changes in intracellular protein breakdown -- Cooperation of various subcellular fractions in protein degradation in vitro -- Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- Naturally occurring inhibitors of intracellular proteinases -- Isolation and characterization of inhibitors of neutral proteinases from spleen -- Production of rabbit antibodies against active rat cathepsin B -- Role of heparin in the interaction of serine proteinases with antithrombin III -- Protease inhibitors produced by microorganisms -- Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- Studies on the in vivo-action of leupeptin on the nitrogen retention in rats -- Inactivation studies of cathepsin D with diazo compounds -- Inhibition of serine proteinases by benzamidine derivatives -- Studies on some effectors of lysosomal proteinases from rat liver -- Endogenous proteolytic activity of chromatin -- Degradation of phosphorylated chromosomal nonhistone proteins -- Interaction of intracellular proteases and immune mechanisms -- The diversity of cellular proteinases in physiology and pathology -- CONTENTS/ СОДЕРЖАНИЕ/ INHALT |
title_full |
Acta Biologica et Medica Germanica. Band 36, Heft 11/12, 3rd Symposium Intracellular Protein Catabolism / hrsg. von R. Baumann. |
title_fullStr |
Acta Biologica et Medica Germanica. Band 36, Heft 11/12, 3rd Symposium Intracellular Protein Catabolism / hrsg. von R. Baumann. |
title_full_unstemmed |
Acta Biologica et Medica Germanica. Band 36, Heft 11/12, 3rd Symposium Intracellular Protein Catabolism / hrsg. von R. Baumann. |
title_auth |
Acta Biologica et Medica Germanica. |
title_alt |
Frontmatter -- Preface -- Intracellular proteinase of Bacillus subtilis -- Relationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium -- Characterization and function of intracellular proteinases and proteinase inhibitors from yeast -- Protein 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 -- Studies on bovine spleen cathepsin D -- Intracellular protein catabolism and new serine proteases -- Cathepsin H: An endoaminopeptidase -- The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea -- The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen -- Protein cleavage in virus-infected cells -- Peptidases of the kidney microvillus membrane -- Degradation of myofibrillar proteins by cathepsins B and D -- Degradation of myones as a consequence of disuse and denervation -- The influence of immobilization on soluble proteins of muscle -- A neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes -- The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- Studies on the possible physiological controls of skeletal muscle proteases -- Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- Acetyl glutamate — a model of signals for intracellular proteolysis -- Flow and shuttle of plasma membrane during endocytosis -- Inhibition by insulin of the physiological autophagic breakdown of cell organelles -- Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- Studies on the relationship between the molecular structure and the catabolism of insulin -- Insulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- Presence of an endopeptidase activity in rat liver ribosomes -- Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- The role of lysosomal enzymes in protein degradation in different types of rat liver cells -- Uptake and degradation of asialo-fetuin by isolated rat hepatocytes -- Endocytosis and breakdown of proteins by sinusoidal liver cells -- The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- Protein degradation in isolated rat hepatocytes -- Attempts to relate enzyme inactivation to degradation in vivo -- Lysosomes and protein degradation -- Protein degradation in rat liver cells -- Intracellular protein catabolism -- Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- Turnover of lipogenic enzymes of rat liver in dependence on age -- Aging changes in intracellular protein breakdown -- Cooperation of various subcellular fractions in protein degradation in vitro -- Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- Naturally occurring inhibitors of intracellular proteinases -- Isolation and characterization of inhibitors of neutral proteinases from spleen -- Production of rabbit antibodies against active rat cathepsin B -- Role of heparin in the interaction of serine proteinases with antithrombin III -- Protease inhibitors produced by microorganisms -- Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- Studies on the in vivo-action of leupeptin on the nitrogen retention in rats -- Inactivation studies of cathepsin D with diazo compounds -- Inhibition of serine proteinases by benzamidine derivatives -- Studies on some effectors of lysosomal proteinases from rat liver -- Endogenous proteolytic activity of chromatin -- Degradation of phosphorylated chromosomal nonhistone proteins -- Interaction of intracellular proteases and immune mechanisms -- The diversity of cellular proteinases in physiology and pathology -- CONTENTS/ СОДЕРЖАНИЕ/ INHALT |
title_new |
Acta Biologica et Medica Germanica. |
title_sort |
acta biologica et medica germanica. 3rd symposium intracellular protein catabolism / |
series |
Acta Biologica et Medica Germanica ; |
series2 |
Acta Biologica et Medica Germanica ; |
publisher |
De Gruyter, |
publishDate |
2022 |
physical |
1 online resource (476 p.) Issued also in print. |
edition |
Reprint 2022 |
contents |
Frontmatter -- Preface -- Intracellular proteinase of Bacillus subtilis -- Relationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium -- Characterization and function of intracellular proteinases and proteinase inhibitors from yeast -- Protein 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 -- Studies on bovine spleen cathepsin D -- Intracellular protein catabolism and new serine proteases -- Cathepsin H: An endoaminopeptidase -- The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea -- The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen -- Protein cleavage in virus-infected cells -- Peptidases of the kidney microvillus membrane -- Degradation of myofibrillar proteins by cathepsins B and D -- Degradation of myones as a consequence of disuse and denervation -- The influence of immobilization on soluble proteins of muscle -- A neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes -- The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- Studies on the possible physiological controls of skeletal muscle proteases -- Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- Acetyl glutamate — a model of signals for intracellular proteolysis -- Flow and shuttle of plasma membrane during endocytosis -- Inhibition by insulin of the physiological autophagic breakdown of cell organelles -- Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- Studies on the relationship between the molecular structure and the catabolism of insulin -- Insulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- Presence of an endopeptidase activity in rat liver ribosomes -- Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- The role of lysosomal enzymes in protein degradation in different types of rat liver cells -- Uptake and degradation of asialo-fetuin by isolated rat hepatocytes -- Endocytosis and breakdown of proteins by sinusoidal liver cells -- The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- Protein degradation in isolated rat hepatocytes -- Attempts to relate enzyme inactivation to degradation in vivo -- Lysosomes and protein degradation -- Protein degradation in rat liver cells -- Intracellular protein catabolism -- Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- Turnover of lipogenic enzymes of rat liver in dependence on age -- Aging changes in intracellular protein breakdown -- Cooperation of various subcellular fractions in protein degradation in vitro -- Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- Naturally occurring inhibitors of intracellular proteinases -- Isolation and characterization of inhibitors of neutral proteinases from spleen -- Production of rabbit antibodies against active rat cathepsin B -- Role of heparin in the interaction of serine proteinases with antithrombin III -- Protease inhibitors produced by microorganisms -- Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- Studies on the in vivo-action of leupeptin on the nitrogen retention in rats -- Inactivation studies of cathepsin D with diazo compounds -- Inhibition of serine proteinases by benzamidine derivatives -- Studies on some effectors of lysosomal proteinases from rat liver -- Endogenous proteolytic activity of chromatin -- Degradation of phosphorylated chromosomal nonhistone proteins -- Interaction of intracellular proteases and immune mechanisms -- The diversity of cellular proteinases in physiology and pathology -- CONTENTS/ СОДЕРЖАНИЕ/ INHALT |
isbn |
9783112650080 9783112650073 |
url |
https://doi.org/10.1515/9783112650080 https://www.degruyter.com/isbn/9783112650080 https://www.degruyter.com/document/cover/isbn/9783112650080/original |
illustrated |
Not Illustrated |
doi_str_mv |
10.1515/9783112650080 |
work_keys_str_mv |
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3rd Symposium Intracellular Protein Catabolism / |
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Acta Biologica et Medica Germanica. |
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A possible role in the degradation of native enzymes -- </subfield><subfield code="t">The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases -- </subfield><subfield code="t">Studies on the possible physiological controls of skeletal muscle proteases -- </subfield><subfield code="t">Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP -- </subfield><subfield code="t">Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH -- </subfield><subfield code="t">Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis -- </subfield><subfield code="t">Acetyl glutamate — a model of signals for intracellular proteolysis -- </subfield><subfield code="t">Flow and shuttle of plasma membrane during endocytosis -- </subfield><subfield code="t">Inhibition by insulin of the physiological autophagic breakdown of cell organelles -- </subfield><subfield code="t">Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats -- </subfield><subfield code="t">Studies on the relationship between the molecular structure and the catabolism of insulin -- </subfield><subfield code="t">Insulin and glucagon degradation in livers of sand rats (Psammomys obesus) -- </subfield><subfield code="t">Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes -- </subfield><subfield code="t">Presence of an endopeptidase activity in rat liver ribosomes -- </subfield><subfield code="t">Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats -- </subfield><subfield code="t">The role of lysosomal enzymes in protein degradation in different types of rat liver cells -- </subfield><subfield code="t">Uptake and degradation of asialo-fetuin by isolated rat hepatocytes -- </subfield><subfield code="t">Endocytosis and breakdown of proteins by sinusoidal liver cells -- </subfield><subfield code="t">The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation -- </subfield><subfield code="t">Protein degradation in isolated rat hepatocytes -- </subfield><subfield code="t">Attempts to relate enzyme inactivation to degradation in vivo -- </subfield><subfield code="t">Lysosomes and protein degradation -- </subfield><subfield code="t">Protein degradation in rat liver cells -- </subfield><subfield code="t">Intracellular protein catabolism -- </subfield><subfield code="t">Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies -- </subfield><subfield code="t">Turnover of lipogenic enzymes of rat liver in dependence on age -- </subfield><subfield code="t">Aging changes in intracellular protein breakdown -- </subfield><subfield code="t">Cooperation of various subcellular fractions in protein degradation in vitro -- </subfield><subfield code="t">Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors -- </subfield><subfield code="t">Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors -- </subfield><subfield code="t">Naturally occurring inhibitors of intracellular proteinases -- </subfield><subfield code="t">Isolation and characterization of inhibitors of neutral proteinases from spleen -- </subfield><subfield code="t">Production of rabbit antibodies against active rat cathepsin B -- </subfield><subfield code="t">Role of heparin in the interaction of serine proteinases with antithrombin III -- </subfield><subfield code="t">Protease inhibitors produced by microorganisms -- </subfield><subfield code="t">Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver -- </subfield><subfield code="t">Studies on the in vivo-action of leupeptin on the nitrogen retention in rats -- </subfield><subfield code="t">Inactivation studies of cathepsin D with diazo compounds -- </subfield><subfield code="t">Inhibition of serine proteinases by benzamidine derivatives -- </subfield><subfield code="t">Studies on some effectors of lysosomal proteinases from rat liver -- </subfield><subfield code="t">Endogenous proteolytic activity of chromatin -- </subfield><subfield code="t">Degradation of phosphorylated chromosomal nonhistone proteins -- </subfield><subfield code="t">Interaction of intracellular proteases and immune mechanisms -- </subfield><subfield code="t">The diversity of cellular proteinases in physiology and pathology -- </subfield><subfield code="t">CONTENTS/ СОДЕРЖАНИЕ/ INHALT</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="530" ind1=" " ind2=" "><subfield code="a">Issued also in print.</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In German.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 04. Okt 2022)</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">NON-CLASSIFIABLE.</subfield><subfield code="2">bisacsh</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Abramov, Z. 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