LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 36

Search options

  1. Article ; Online: Dynamics of Ubiquitin Pools in Developing Sea Urchin Embryos: (ubiquitin/embryogenesis/proteolysis).

    Pickart, Cecile M / Summers, Robert G / Shim, Hyunbo / Kasperek, Eileen M

    Development, growth & differentiation

    2023  Volume 33, Issue 6, Page(s) 587–598

    Abstract: The sea urchin embryo is a closed metabolic system in which embryogenesis is accompanied by significant protein degradation. We report results which are consistent with a function for the ubiquitinmediated proteolytic pathway in selective protein ... ...

    Abstract The sea urchin embryo is a closed metabolic system in which embryogenesis is accompanied by significant protein degradation. We report results which are consistent with a function for the ubiquitinmediated proteolytic pathway in selective protein degradation during embryogenesis in this system. Quantitative solid- and solution-phase immunochemical assays, employing anti-ubiquitin antibodies, showed that unfertilized eggs of Strongylocentrotus purpuratus have a high content of unconjugated ubiquitin (ca. 8 × 10
    Language English
    Publishing date 2023-06-06
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 280433-5
    ISSN 1440-169X ; 0012-1592
    ISSN (online) 1440-169X
    ISSN 0012-1592
    DOI 10.1111/j.1440-169X.1991.00587.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 194: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Back to the future with ubiquitin.

    Pickart, Cecile M

    Cell

    2004  Volume 116, Issue 2, Page(s) 181–190

    Abstract: Two papers published in 1984 by the Varshavsky laboratory revealed that the ubiquitin/proteasome pathway is the principal system for degradation of short-lived proteins in mammalian cells, setting the stage for future demonstrations of this pathway's ... ...

    Abstract Two papers published in 1984 by the Varshavsky laboratory revealed that the ubiquitin/proteasome pathway is the principal system for degradation of short-lived proteins in mammalian cells, setting the stage for future demonstrations of this pathway's many regulatory roles. This perspective discusses the impact of those papers and highlights some of the subsequent insights that have led to our current appreciation of the breadth of ubiquitin-mediated signaling.
    MeSH term(s) Animals ; Cysteine Endopeptidases/metabolism ; Histones/metabolism ; Humans ; Lysosomes/physiology ; Models, Biological ; Multienzyme Complexes/metabolism ; Phenotype ; Proteasome Endopeptidase Complex ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin/physiology
    Chemical Substances Histones ; Multienzyme Complexes ; Ubiquitin ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2004-01-23
    Publishing country United States
    Document type Comment ; Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(03)01074-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 58: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: DNA repair: right on target with ubiquitin.

    Pickart, Cecile M

    Nature

    2002  Volume 419, Issue 6903, Page(s) 120–121

    MeSH term(s) DNA/genetics ; DNA/metabolism ; DNA Damage ; DNA Repair ; Humans ; Ligases/metabolism ; Models, Biological ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Saccharomyces cerevisiae Proteins/metabolism ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes
    Chemical Substances Proliferating Cell Nuclear Antigen ; Saccharomyces cerevisiae Proteins ; Small Ubiquitin-Related Modifier Proteins ; Ubiquitin ; DNA (9007-49-2) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ligases (EC 6.-)
    Language English
    Publishing date 2002-09-12
    Publishing country England
    Document type News ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/419120a
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 26: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: Beginning at the end with SUMO.

    Matunis, Michael J / Pickart, Cecile M

    Nature structural & molecular biology

    2005  Volume 12, Issue 7, Page(s) 565–566

    MeSH term(s) Catalysis ; GTPase-Activating Proteins/metabolism ; Models, Molecular ; Multiprotein Complexes/metabolism ; SUMO-1 Protein ; Small Ubiquitin-Related Modifier Proteins/chemistry ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Substrate Specificity ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances GTPase-Activating Proteins ; Multiprotein Complexes ; SUMO-1 Protein ; SUMO1 protein, human ; Small Ubiquitin-Related Modifier Proteins ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; ubiquitin-conjugating enzyme UBC9 (EC 6.3.2.-)
    Language English
    Publishing date 2005-07
    Publishing country United States
    Document type News ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/nsmb0705-565
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4101: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 56: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Ubiquitin chain synthesis.

    Raasi, Shahri / Pickart, Cecile M

    Methods in molecular biology (Clifton, N.J.)

    2005  Volume 301, Page(s) 47–55

    Abstract: Several important signaling processes depend on the tagging of cellular proteins with "polyubiquitin chains"-ubiquitin polymers whose building blocks are connected by isopeptide bonds between G76 of one ubiquitin and a specific lysine residue of the next ...

    Abstract Several important signaling processes depend on the tagging of cellular proteins with "polyubiquitin chains"-ubiquitin polymers whose building blocks are connected by isopeptide bonds between G76 of one ubiquitin and a specific lysine residue of the next one. Here we describe procedures for the synthesis of polyubiquitin chains of defined lengths that are linked through the K48 or K63 side chains. The method involves a series of enzymatic reactions in which proximally and distally blocked monoubiquitins (or chains) are conjugated to produce a particular chain in high yield. Individual chains are then deblocked and joined in another round of reaction. Successive rounds of deblocking and synthesis can give rise to a chain of any desired length.
    MeSH term(s) Animals ; Humans ; Polyubiquitin/chemical synthesis ; Polyubiquitin/chemistry ; Ubiquitin-Conjugating Enzymes/chemistry ; Ubiquitin-Protein Ligases/chemistry
    Chemical Substances Polyubiquitin (120904-94-1) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2005
    Publishing country United States
    Document type Journal Article
    ISSN 1064-3745
    ISSN 1064-3745
    DOI 10.1385/1-59259-895-1:047
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article: Controlled synthesis of polyubiquitin chains.

    Pickart, Cecile M / Raasi, Shahri

    Methods in enzymology

    2005  Volume 399, Page(s) 21–36

    Abstract: Many intracellular signaling processes depend on the modification of proteins with polymers of the conserved 76-residue protein ubiquitin. The ubiquitin units in such polyubiquitin chains are connected by isopeptide bonds between a specific lysine ... ...

    Abstract Many intracellular signaling processes depend on the modification of proteins with polymers of the conserved 76-residue protein ubiquitin. The ubiquitin units in such polyubiquitin chains are connected by isopeptide bonds between a specific lysine residue of one ubiquitin and the carboxyl group of G76 of the next ubiquitin. Chains linked through K48-G76 and K63-G76 bonds are the best characterized, signaling proteasome degradation and nonproteolytic outcomes, respectively. The molecular determinants of polyubiquitin chain recognition are under active investigation; both the chemical structure and the length of the chain can influence signaling outcomes. In this article, we describe the protein reagents necessary to produce K48- and K63-linked polyubiquitin chains and the use of these materials to produce milligram quantities of specific-length chains for biochemical and biophysical studies. The method involves reactions catalyzed by linkage-specific conjugating factors, in which proximally and distally blocked monoubiquitins (or chains) are joined to produce a particular chain product in high yield. Individual chains are then deblocked and joined in another round of reaction. Successive rounds of deblocking and synthesis give rise to a chain of the desired length.
    MeSH term(s) Electrophoresis, Polyacrylamide Gel ; Polyubiquitin/chemical synthesis ; Polyubiquitin/chemistry ; Polyubiquitin/isolation & purification
    Chemical Substances Polyubiquitin (120904-94-1)
    Language English
    Publishing date 2005
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 0076-6879
    ISSN 0076-6879
    DOI 10.1016/S0076-6879(05)99002-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis.

    Wang, Min / Pickart, Cecile M

    The EMBO journal

    2005  Volume 24, Issue 24, Page(s) 4324–4333

    Abstract: Individual ubiquitin (Ub)-protein ligases (E3s) cooperate with specific Ub-conjugating enzymes (E2s) to modify cognate substrates with polyubiquitin chains. E3s belonging to the Really Interesting New Gene (RING) and Homologous to E6-Associated Protein ( ... ...

    Abstract Individual ubiquitin (Ub)-protein ligases (E3s) cooperate with specific Ub-conjugating enzymes (E2s) to modify cognate substrates with polyubiquitin chains. E3s belonging to the Really Interesting New Gene (RING) and Homologous to E6-Associated Protein (E6AP) C-Terminus (HECT) domain families utilize distinct molecular mechanisms. In particular, HECT E3s, but not RING E3s, form a thiol ester with Ub before transferring Ub to the substrate lysine. Here we report that different HECT domain E3s can employ distinct mechanisms of polyubiquitin chain synthesis. We show that E6AP builds up a K48-linked chain on its HECT cysteine residue, while KIAA10 builds up K48- and K29-linked chains as free entities. A small region near the N-terminus of the conserved HECT domain helps to bring about this functional distinction. Thus, a given HECT domain can specify both the linkage of a polyubiquitin chain and the mechanism of its assembly.
    MeSH term(s) Binding Sites ; Blotting, Western ; Cloning, Molecular ; Cysteine/chemistry ; DNA, Complementary/metabolism ; Escherichia coli/metabolism ; Glutathione Transferase/metabolism ; Humans ; Lysine/chemistry ; Multienzyme Complexes/chemistry ; Plasmids/metabolism ; Polyubiquitin/chemistry ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Time Factors ; Ubiquitin/chemistry ; Ubiquitin-Conjugating Enzymes/chemistry ; Ubiquitin-Protein Ligase Complexes/chemistry ; Ubiquitin-Protein Ligases/chemistry
    Chemical Substances DNA, Complementary ; Multienzyme Complexes ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; Ubiquitin ; Polyubiquitin (120904-94-1) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; UBE3A protein, human (EC 2.3.2.26) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Glutathione Transferase (EC 2.5.1.18) ; Lysine (K3Z4F929H6) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2005-12-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7600895
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 100: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article: Proteasomes and their kin: proteases in the machine age.

    Pickart, Cecile M / Cohen, Robert E

    Nature reviews. Molecular cell biology

    2004  Volume 5, Issue 3, Page(s) 177–187

    MeSH term(s) Bacterial Proteins/physiology ; Cysteine Endopeptidases/metabolism ; Cysteine Endopeptidases/physiology ; Endopeptidases/metabolism ; Fungal Proteins/physiology ; Microscopy, Electron ; Models, Biological ; Multienzyme Complexes/metabolism ; Multienzyme Complexes/physiology ; Peptide Hydrolases/physiology ; Peptides/chemistry ; Proteasome Endopeptidase Complex ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Protein Transport ; Signal Transduction ; Structure-Activity Relationship ; Ubiquitin/metabolism
    Chemical Substances Bacterial Proteins ; Fungal Proteins ; Multienzyme Complexes ; Peptides ; Ubiquitin ; Endopeptidases (EC 3.4.-) ; Peptide Hydrolases (EC 3.4.-) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-)
    Language English
    Publishing date 2004-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm1336
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5446: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 26: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article: Ubiquitin: structures, functions, mechanisms.

    Pickart, Cecile M / Eddins, Michael J

    Biochimica et biophysica acta

    2004  Volume 1695, Issue 1-3, Page(s) 55–72

    Abstract: Ubiquitin is the founding member of a family of structurally conserved proteins that regulate a host of processes in eukaryotic cells. Ubiquitin and its relatives carry out their functions through covalent attachment to other cellular proteins, thereby ... ...

    Abstract Ubiquitin is the founding member of a family of structurally conserved proteins that regulate a host of processes in eukaryotic cells. Ubiquitin and its relatives carry out their functions through covalent attachment to other cellular proteins, thereby changing the stability, localization, or activity of the target protein. This article reviews the basic biochemistry of these protein conjugation reactions, focusing on ubiquitin itself and emphasizing recent insights into mechanism and specificity.
    MeSH term(s) Animals ; Binding Sites ; Cell Cycle Proteins/physiology ; F-Box Proteins/physiology ; F-Box-WD Repeat-Containing Protein 7 ; Humans ; Protein Structure, Tertiary ; Signal Transduction/physiology ; Substrate Specificity ; Ubiquitin/chemistry ; Ubiquitin/physiology ; Ubiquitin-Protein Ligases/physiology
    Chemical Substances Cell Cycle Proteins ; F-Box Proteins ; F-Box-WD Repeat-Containing Protein 7 ; FBXW7 protein, human ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2004-11-29
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2004.09.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article: The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases.

    Ross, Christopher A / Pickart, Cecile M

    Trends in cell biology

    2004  Volume 14, Issue 12, Page(s) 703–711

    Abstract: During the past decade, it has become apparent that a set of ostensibly unrelated neurodegenerative diseases, including Parkinson's disease and Huntington's disease, shares striking molecular and cell biology commonalities. Each of the diseases involves ... ...

    Abstract During the past decade, it has become apparent that a set of ostensibly unrelated neurodegenerative diseases, including Parkinson's disease and Huntington's disease, shares striking molecular and cell biology commonalities. Each of the diseases involves protein misfolding and aggregation, resulting in inclusion bodies and other aggregates within cells. These aggregates often contain ubiquitin, which is the signal for proteolysis by the 26S proteasome, and chaperone proteins that are involved in the refolding of misfolded proteins. The link between the ubiquitin-proteasome system and neurodegeneration has been strengthened by the identification of disease-causing mutations in genes coding for several ubiquitin-proteasome pathway proteins in Parkinson's disease. However, the exact molecular connections between these systems and pathogenesis remain uncertain and controversial. In this article, we summarize the state of current knowledge, focusing on important unresolved questions.
    MeSH term(s) Animals ; Humans ; Models, Biological ; Mutation ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/physiopathology ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/physiopathology ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2004-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2004.10.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.MG 25: Show issues
    Zs.MO 113: Show issues
    Zs.A 3410: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top