Erscheinungsjahr
Fach
Sprache
Synonyme wurden verwendet für: Picture • Picture archiving • Picture archiving and communication systems • archiving • communication • communication systems • in • medicine
Suche ohne Synonyme: keywords:(Picture archiving and communication systems in medicine)
Verwendete Synonyme:
- bild
- image
Verwendete Synonyme:
- bildarchivierung
- picture storage
Verwendete Synonyme:
- bildarchivierungs und kommunikationssystem
- pacs
- picture archiving and communication system
Verwendete Synonyme:
- archivierung
Verwendete Synonyme:
- informationsprozess
- kommunikation
- kommunikationsprozess
- kommunikationsverhalten
- kommunikationswissenschaft
- kommunikationswissenschaften
- kommunikatives verhalten
- nachricht
Verwendete Synonyme:
- kommunikationssystem
Verwendete Synonyme:
- intelligent network
- intelligentes netz
Verwendete Synonyme:
- heilkunst
- humanmedizin
- medizin
-
3 Tesla MRI surface coil: Is it sensitive for prostatic imaging??
Freier ZugriffTaylor & Francis Verlag | 2015|Schlagwörter: PACS, Picture archiving and communication system -
Cpmputer assistance in medical imaging
Tema Archiv | 1992|Schlagwörter: PACS (Bildarchivierung), Datenverarbeitung in der Medizin, Bildarchivierung -
3-D correlative imaging and segmentation of cerebral anatomy, function and vasculature
Tema Archiv | 1992|Schlagwörter: Datenverarbeitung in der Medizin, Bildarchivierung, PACS (Bildarchivierung) -
Computers and networks in medical and healthcare systems
Tema Archiv | 1995|Schlagwörter: Datenverarbeitung in der Medizin, PACS (Bildarchivierung) -
Diagnostic imaging over the last 50 years: research and development in medical imaging science and technology
Tema Archiv | 2006|Schlagwörter: PACS (Bildarchivierung), Datenverarbeitung in der Medizin, Bildgebung in der Medizin -
Fused images add value to treatment planning
Tema Archiv | 1996|Schlagwörter: Datenverarbeitung in der Medizin, PACS (Bildarchivierung) -
Predicting PACS loading and performance metrics using Monte Carlo and queuing methods
Tema Archiv | 2003|Schlagwörter: PACS (Bildarchivierung), Datenverarbeitung in der Medizin -
Using mobile wireless devices for interactive visualization and analysis of DICOM data
Tema Archiv | 2003|Schlagwörter: PACS (Bildarchivierung), Datenverarbeitung in der Medizin, medizinisches Bild -
The Practice and Practitioners of Pharmaceutical Medicine
Wiley | 2007|Schlagwörter: Diploma in Pharmaceutical Medicine (DipPharmMed), pharmaceutical medicine practice and practitioners, organizations and educational systems, pharmaceutical medicine and educational backgrounds, versatility, adaptability, communication skills, teamwork -
Automated bone density calculation using feature extraction by deformable templates
Tema Archiv | 1990|Schlagwörter: PACS (BILDARCHIVIERUNG), DATENVERARBEITUNG IN DER MEDIZIN -
Expert System of Image Processing-Applications to the Reconstruction of 3D Images from 2D Images
Springer Verlag | 1996|Schlagwörter: Image processing, 3D image reconstruction, Documentation and Information in Chemistry, Computer Applications in Chemistry, Geographical Information Systems/Cartography, Information Systems and Communication Service -
Thermal decomposition of solid phase nitromethane under various heating rates and target temperatures based on ab initio molecular dynamics simulations
Springer Verlag | 2014|Schlagwörter: PACS, 71.15.Pd Molecular dynamics calculations (Car-Parrinello) and other numerical simulations, 82.30.Cf Atom and radical reactions, Computer Applications in Chemistry, Molecular Medicine, Computer Appl. in Life Sciences, Characterization and Evaluation of Materials, Theoretical and Computational Chemistry -
Fractal Shape Description using Compact Data Sets
Springer Verlag | 1996|Schlagwörter: image compression, Documentation and Information in Chemistry, Computer Applications in Chemistry, Geographical Information Systems/Cartography, Information Systems and Communication Service -
2001 Congress on In Vitro Biology
NTIS | 2002|Schlagwörter: Clinical Medicine, In vitro analysis, Clinical medicine, Communication and radio systems -
TSC Regulates Oligodendroglial Differentiation and Myelination in the CNS
NTIS | 2011|Schlagwörter: Clinical Medicine, Signs and symptoms, Communication and radio systems, In vitro analysis -
Metabolic Signaling and Therapy of Lung Cancer
NTIS | 2013|Schlagwörter: Clinical Medicine, Communication and radio systems, Pgam1 in regulation of lung cancer metabolism, Molecular mechanisms underlying pgam1 activation in lung cancer -
Microarray‐Based Comparative Genomic Hybridization
Wiley | 2009|Schlagwörter: targeted therapy ‐ rational design and therapeutic agent development, oncogenes and tumour‐suppressor genes ‐ cell proliferation and cell fate determination, data integration and genomic data integration, bacterial artificial chromosomes (BACs), P1‐derived artificial chromosomes (PACs) and yeast artificial chromosomes (YACs) ‐ large insert genomic clones aCGH studies, identification of novel amplicons and tumour‐suppressor genes by aCGH ‐ step forward in unravelling cancer complexity, understanding complexity of cancers at genomic and transcriptomic level ‐ step towards goal of individualized medicine -
Structure, Function and Regulation of the Hsp90 Machinery
Freier ZugriffDOAJ | 2013|Schlagwörter: Function and Regulation of the Hsp90 Machinery Jing Li1, and protein degradation, Hsp90 is a flexible dimeric protein composed of three different domains which adopt structurally distinct conformations. ATP binding triggers directionality in these conformational changes and leads to a more compact state. To achieve its function, which facilitate the maturation of client proteins. In addition, such as phosphorylation and acetylation, and inter-domain communications. In this review, one of the most abundant and conserved molecular chaperones, is essential in eukaryotic cells. [1], [2] Different from other well-known molecular chaperone like Hsp70 and GroEL/ES, and steroid hormone receptors (SHRs). [4], Hsp90 does not only function in protein folding but also contribute to various cellular processes including signal transduction, and protein degradation. Interestingly, called HtpG in Escherichia More Details coli, no Hsp90 gene has been found in archea. [8], bacterial Hsp90 is not essential and its precise function remains to be investigated. Recent studies suggest that it collaborates with the DnaK (Hsp70) system in substrate remodeling and may function against oxidative stress. [11], [12] In yeast, there are two Hsp90 isoforms in the cytosol, Hsc82 and Hsp82, of which Hsp82 is up-regulated up to 20 times under heat stress. [2] Hsp90α and Hsp90β are the two major isoforms in the cytoplasm of mammalian cells. Hsp90α is inducible under stress conditions, while Hsp90β is constitutively expressed. [13] Hsp90 analogues also exist in other cellular compartments such as Grp94 in the endoplasmic reticulum, Trap-1 in the mitochondrial matrix, and ch-Hsp90 in the chloroplast. [14], Hsp90 can be secreted as well and it promotes tumor invasiveness. Blocking the secreted Hsp90 led to a significant inhibition of tumor metastasis. [17] Structure of Hsp90 Top Structurally, Hsp90 is a homodimer and each protomer contains three flexibly linked regions, and a C-terminal dimerization domain (C-domain) [Figure 1]. [18] Except for the charged linker located between the N- and M-domains in eukaryotic Hsp90, which contain a Bergerat ATP-binding fold. [19] Another interesting feature of the ATP binding region is that several conserved amino acid residues form a "lid" that closes over the nucleotide binding pocket in the ATP-bound state but is open during the ADP-bound state. [18] The M-domain of Hsp90 is involved in ATP hydrolysis, the M-domain contributes to the interaction sites for client proteins and some co-chaperones. [20] The C-domain is essential for the dimerization of Hsp90. Interestingly, in eukaryotic Hsp90, PDB 2IOQ) and nucleotide-bound yeast Hsp90 in the closed conformation (right, PDB 2CG9). The N-domain is depicted in green, the M-domain in blue, and the C-domain in orange. Click here to view Conformational dynamics of Hsp90 Top Hsp90 is a weak ATPase and the turnover rates are very low, with 1 min–1 for yeast Hsp90 and 0.1 min–1 for human Hsp90. [23], which seem to be in a dynamic equilibrium [Figure 1]. [9], [26] Nucleotide binding induces directionality and a conformational cycle. [9], [28] In the apo state, termed "open conformation" [Figure 1]. ATP binding triggers a series of conformational changes including repositioning of the N-terminal lid region and a dramatic change in the N-M domain orientation. Finally, termed "closed conformation" in which the N-domains are dimerized [Figure 1]. [9], [18] Recent biophysical studies using ensemble and single molecule fluorescence resonance energy transfer (FRET) assays allowed to further dissect the ATP-induced conformational changes [Figure 2]. [26], in which the ATP lid is closed but the N-domains are still open. The N-terminal dimerization leads to the formation of the second intermediate state (I2), in which the M-domain repositions and interacts with the N-domain. Then Hsp90 reaches a fully closed state in which ATP hydrolysis occurs. After ATP is hydrolyzed, in which the ATP lid is closed but the N-domains are still open. Then, in which the M-domain repositions and interacts with the N-domain. Then, Hsp90 reaches a fully closed state in which ATP hydrolysis occurs. After ATP is hydrolyzed, release ADP and Pi, and Hsp90 returns to the open conformation. Click here to view Notably, nucleotide binding is not the only determinant for Hsp90 conformation. The interaction with co-chaperones and client protein also influences the conformational rearrangement of Hsp90. [29], [30] These results suggest that there may be a dynamic equilibrium between the different conformations of Hsp90 and this conformational plasticity is functionally important since it may allow Hsp90 to adapt to different client proteins. Co-chaperone regulation of Hsp90 Top Co-chaperone regulation is a conserved feature of the eukaryotic Hsp90 system. To date, [31] They regulate the function of Hsp90 in different ways such as inhibition and activation of the ATPase of Hsp90 as well as recruitment of specific client proteins to the cycle. Interestingly, [33] The maturation of most SHRs strictly depends on the interaction with Hsp90. Co-chaperones such as Hop/Sti1 and the large peptidylprolyl isomerase (PPIase) have strong influences on the activation. [32], SHRs must pass through three complexes with different co-chaperone compositions chronologically to reach their active conformation. Hsp70/Hsp40 were identified as components in the "early complex." [32] After association with Hsp90 through the adaptor protein Hop, [38] In addition to the intermediate complex, a third complex that contains a PPIase and the co-chaperone p23 had been found as the last step of the cycle. [39], similar heterocomplexes can be found from yeast to man even in the absence of client protein. [32] Recent studies [using FRET, and electron microscopy] provided insight into how the exchange of co-chaperones is regulated. [42], in which first one Hop/Sti1 binds to the Hsp90 dimer and stabilizes its open conformation. As a result, leading to an asymmetric Hsp90 intermediate complex. After the binding of ATP and p23/Sba1, Hsp90 adopts the "closed" conformation which weakens the binding of Hop/Sti1 and therefore promotes its exit. Another PPIase or TPR co-chaperone can potentially bind to form the final complex together with Hsp90 and p23/Sba1. Following ATP hydrolysis, and a client protein form an "early complex." The client protein is transferred from Hsp70 to Hsp90 through the adaptor protein Hop/Sti1. One Hop/Sti1 bound is sufficient to stabilize the open conformation of Hsp90. The other TPR-acceptor site is preferentially occupied by a PPIase, which weakens the binding of Hop/Sti1 and promotes its exit from the complex. Potentially another PPIase (dashed line) associates to form the "late complex" together with Hsp90 and p23/Sba1. After the hydrolysis of ATP, p23/Sba1 and the folded client are released from Hsp90. (B) Hsp90 chaperone cycle for kinases. In the early stage, Hsp70 and Hsp40 interact with newly synthesized kinases. Protein kinases are recruited to Hsp90 though the action of Hop/Sti1 and the kinase-specific co-chaperone Cdc37. Both are able to stabilize the Hsp90/kinase complex. Protein phosphatase Pp5 and the ATPase activator Aha1 release Hop/Sti1 from Hsp90. At a later stage, Aha1 can release Cdc37 from Hsp90 together with nucleotides. (C) Hsp90 chaperone cycle for NLRs. Rar1 binds to the N-domain of Hsp90 through its Chord1 domain and prevents the formation of the closed conformation. This interaction supports the binding of Rar1-Chord2 to the N-domain in the other protomer. With the association of Rar1-Chord2, Sgt1 interacts with Hsp90 as well as with an NLR protein. In the stable ternary complex, and the NLR protein may dissociate from Hsp90. (D) Hsp90-R2TP complex. Model of the R2TP complex in yeast. Pih1 interacts with Rvb1/2, and the C-domain of Tah1. Tah1 binds to the C-terminal MEEVD motif of Hsp90 through its TPR domain. Click here to view Hop/Sti1 serves as an adaptor protein between Hsp70 and Hsp90 and facilitates the transfer of client protein. [37], it is indispensable for maintaining the hormone binding activity of the glucocorticoid receptor (GR) and progesterone receptor (PR). [45], which consists of three TPR motifs and recognizes the C-terminal MEEVD motif in Hsp90. [22] Besides Hop/Sti1, and members of the PPIase family, and Cyp40 (yeast homologues Cpr6/Cpr7), which catalyzes the interconversion of the cis-trans isomerization of peptide bonds prior to proline residues [47] and a TPR domain for the interaction with Hsp90. Most of these large PPIases show independent chaperone activity. [48], the function of PPIases in SHR complexes is not well understood. They may be selected by specific client proteins. For example, Cyp40 is most abundant in estrogen receptor (ER) complexes [51] and Fkbp52 mediates potentiation of GR through increasing GR hormone-binding affinity. [34] Interestingly, which suggests a noncatalytic role of PPIases in the regulation of SHR signaling. [52] In contrast to Hop/Sti1 and the TPR-PPIases, [56] p23 was identified as a component in SHR complexes, together with Hsp90 and a PPIase. [57] It facilitates the maturation of client proteins by stabilizing the closed conformation of Hsp90. [58] As a result, [61] is partially inhibited in the presence of p23/Sba1. [41], the maturation of protein kinases also requires the Hsp70 chaperone machinery [Figure 3]B. [63] In the early stage, Hsp70 and Hsp40 interact with newly synthesized kinases. Protein kinases are recruited to Hsp90 through the action of Hop/Sti1 and the kinase-specific co-chaperone Cdc37. Both are able to stabilize the Hsp90/kinase complex. [64] At a later stage, [67] It was originally identified in Saccharomyces cerevisiae as a gene essential for cell cycle progression. [68], [69] Cdc37 interacts with kinases through its N-terminal domain and binds to the N-domain of Hsp90 via its C-terminal part. Similar to Hop/Sti1, the interaction of Cdc37 with Hsp90 leads to the stabilization of the open conformation and the inhibition of Hsp90 ATPase activity. [70] In contrast to the co-chaperones discussed above, Aha1 is the most powerful ATPase activator of Hsp90. [71] It binds the N- and M-domains of Hsp90. [20], [30] Binding of Aha1 induces a partially closed Hsp90 conformation and accelerates the progression of the ATPase cycle dramatically. [28], [30] The presence of Aha1 enables Hsp90 to bypass the I1 state and to directly reach I2 in the ATPase cycle. [28] The activation of specific clients such as viral Src kinase (v-Src) and SHRs is severely affected in Aha1 knockout cells. [72] Moreover, Aha1 plays a critical role in the inherited misfolding disease cystic fibrosis (CF) through participating in the quality control pathway of the cystic fibrosis transmembrane conductance regulator (CFTR). Down-regulation of Aha1 could rescue the phenotype caused by misfolded CFTR. [73] Recent research highlighted the function of Aha1 in the progression of the Hsp90 cycle. It efficiently displaces Hop/Sti1 from Hsp90 and promotes the transition from the open to closed conformation together with a PPIase in a synergistic manner. [74] Pp5/Ppt1 is a protein phosphatase which is involved in this cycle through regulating the phosphorylation states of Cdc37. It associates with Hsp90 through its N-terminal TPR domain. Binding to Hsp90 results in the abrogation of the intrinsic inhibition of Pp5/Ppt1. [75] Pp5/Ppt1 specifically dephosphorylates Hsp90 and Cdc37 in Hsp90 complexes. [76], [77] In Ppt1 knockout strains, which implies that the tight regulation of the Hsp90 phosphorylation state is necessary for the efficient processing of client proteins. [76] Chaperone cycle for nucleotide-binding site and leucine-rich repeat domain containing (NLR) proteins NLRs are conserved immune sensors which recognize pathogens. [78] Accumulating evidence indicates that Hsp90 and its co-chaperones Sgt1 and Rar1 are involved in the maturation of these proteins. [79] Sgt1 interacts with the N-domain of Hsp90 through its CS domain, Sgt1 has no inherent Hsp90 ATPase regulatory activity due to differences in interaction. [81] Interestingly, although a TPR domain is present in Sgt1 as well, it is not involved in the interaction with Hsp90. [82] Functionally, Hsp90 and Sgt1 form a ternary complex with the co-chaperone Rar1, which acts as a core modulator in plant immunity. [78] During the recruitment and activation of NLRs, Rar1 binds to the N-domain of Hsp90 through its Chord1 domain and prevents the formation of the closed conformation [Figure 3]C. This interaction supports the binding of Rar1-Chord2 to the N-domain in the other protomer. With the association of Rar1-Chord2, Sgt1 is promoted to interact with Hsp90 as well as with an NLR protein. In the stable ternary complex, thus permitting access by a catalytic arginine residue of the M-domain to the ATP binding site and promoting ATP hydrolysis. Once ATP is hydrolyzed, and the NLR protein may dissociate from Hsp90. [83] Hsp90 complexes in RNA processing Recent studies showed that Hsp90 is also involved in the assembly of small nucleolar ribonucleoproteins (snoRNPs) and RNA polymerase. [84], the central player in this process, and the AAA+ ATPase Rvb1 and Rvb2) has been extensively investigated [Figure 3]D. [86], [87] The co-chaperone Tah1 interacts with Hsp90 through its TPR domain and its C-terminal region binds Pih1, the Hsp90-Tah1 complex stabilizes Pih1 in vivo and prevents its aggregation in vitro. [84] The Tah1-Pih1 heterodimer is able to inhibit the ATPase activity of Hsp90. [88] Tah1 and Pih1 are then transferred to the Rvb1/2 complex leading to the formation of the R2TP complex [Figure 3]D. Together, Hsp90 and the R2TP complex are involved in the biogenesis and assembly of snoRNPs. Notably, neither Hsp90 nor R2TP are components of the mature snoRNP complex. The R2TP-Hsp90 complex works together with a prefoldin-like complex in RNA polymerase II assembly. This complex interacts with unassembled Rpb1 and promotes its cytoplasmic assembly and translocation to the nucleus. [85] In addition to the activation of client protein, co-chaperones are also involved in other physiological processes, [91] and melanoma progression (TTC4). [92] The above examples provide a glimpse on Hsp90 co-chaperone cycles. For some cycles, we have obtained a full picture with detailed information; for others, and methylation tightly control the function of Hsp90 and thus influence the maturation of client proteins. [93] Phosphorylation Phosphorylation is the most frequently detected posttranslational modification of Hsp90. A number of different tyrosine or serine phosphorylation sites have been identified and investigated for their impact on Hsp90's chaperone function. [94] For example, hyperphosphorylation also leads to a decreased Hsp90 activity. In yeast, the phosphorylation states of Hsp90 must be precisely regulated in order to maintain the proper function of Hsp90. In addition, phosphorylation also modulates the interaction with co-chaperones and thus exerts further influence on the Hsp90 machinery. [96] For example, tyrosine phosphorylation on Hsp90 disrupts the interaction with Cdc37 and promotes the recruitment of Aha1. [97] C-terminal phosphorylation of Hsp90 regulates alternate binding to co-chaperones Chip and Hop, and inter-domain communication. [96], and Swe1Wee1 kinase. [100], many of them are at the same time Hsp90 client proteins. This indicates that the change of phosphorylation states of Hsp90 may influence the folding and activation of certain groups of client proteins. Acetylation Acetylation is a reversible modification mediated by opposing actions of acetyltransferases and deacetylases. [104] Hsp90 acetylation and its influence on the chaperone machinery have been extensively investigated in recent years. In the case of Hsp90, p300 was reported to be the acetyltransferase and HDAC6 acts as a deacetylase which removes the acetyl group from the protein. [105], [106] Deacetylation of Hsp90 drives the formation of Hsp90 client complexes and promotes the maturation of the client protein GR. Hsp90 can be acetylated at different sites. [107] A study from Necker's lab pointed out that K294, an acetylation site in the M-domain, strongly influences the binding between Hsp90 and its client protein. In general, and thus, Hsp90 fails to support the activation of the client protein. [108] Nitrosylation S-nitrosylation is a reversible covalent modification of reactive cysteine thiols in proteins by nitric oxide (NO). [109], endothelial nitric oxide synthase (eNOS). [111] S-nitrosylation was reported as a negative regulator which inhibits the ATPase activity of Hsp90. [111] In addition, was also reduced consistent with the notion thatHsp90 acts as an NO sensor. [111] This provides a feedback mechanism to inhibit further eNOS activation. Nitrosylation or mutation of the modified C-terminal cysteine residue in Hsp90 led to an ATPase-incompetent state in which the N-terminal domains are kept in the open conformation. [112] The result indicates that nitrosylation has a profound impact on the inter-domain communication in the Hsp90 dimer. Hsp90 client protein recognition Top To date, and RNA modification, have been discovered in recent years. [84], and even degradation. [89], such as the location of the client-binding sites on Hsp90. Current evidence suggests that binding sites could be localized in each of the domains of Hsp90. [8] Another intriguing question unsolved so far is how Hsp90 recognizes its clients. Hsp90 clients belong to different families and do not share common sequences or structural motifs. Although some regions were identified which are important for the recognition of certain group of clients, the αC-β4 loop in kinases, [121] It is reasonable to assume that Hsp90 recognizes certain conformations or the stability of the client protein rather than its primary sequence. Src kinase is a prominent example here. The v-Src and its cellular counterpart (c-Src) share 95% sequence identity but distinct Hsp90 dependency. [122] The activation of v-Src strictly depends on Hsp90, v-Src is an aggregation-prone protein and much more sensitive to thermal and heat denaturation than c-Src. [123] In the case of p53, biochemical experiments suggest that p53 interacts with Hsp90 in a rather folded state. [124], [127] and NMR-based approaches suggested that for heat-treated p53, proposed that Hsp90-bound p53 is in a molten globule state. [129] In contrast, Hagn et al. reported a native-like structure of p53 interaction with Hsp90. [130] Further analysis seems to be required to resolve this conundrum and to determine the molecular mechanism for client recognition. Hsp90 and protein degradation Top Although in general, Hsp90 stabilizes and promotes the correct folding of its client proteins, it was also found to facilitate protein degradation. In addition to soluble cytosolic proteins, and apolipoprotein B. [131], [133] Another aspect which supports the idea that Hsp90 may be involved in the ubiquitin-proteasome pathway is the discovery of a protein called carboxyl terminus of Hsp70-interacting protein (CHIP). [134] As an E3 ubiquitin ligase, CHIP can ubiquitinate unfolded proteins. It also interacts with the C-terminus of Hsp70 and Hsp90 through its TPR domain. [135], Medicine (General)
- ««
- «
- 1
- »»
Meine Suche schicken an (beta)
Schicken Sie ihre Suchanfrage (Suchterm ohne Filter) an andere Datenbanken, Portale und Kataloge, um ggf. weitere interessante Treffer zu finden:
Dimensions ist eine Datenbank für Abstracts und Zitate, die Informationen zu Forschungsförderungen mit daraus resultierenden Veröffentlichungen, Studien und Patenten verknüpft.
Im TIB AV-Portal können audiovisuelle Medien aus Wissenschaft und Lehre recherchiert und eigene wissenschaftliche Videos publiziert werden.
Im FID move kann nach fachspezifischer Literatur, Forschungsdaten und weitere Informationen aus der Mobilitäts- und Verkehrsforschung gesucht werden.
Der Open Research Knowledge Graph liefert strukturiert beschriebene Forschungsinhalte und macht diese vergleichbar.
Frei zugänglicher Ausschnitt der Verbunddatenbank K10plus des GBV und des SWB mit für die Fernleihe und Direktlieferdienste relevanten Materialien.