LIVIVO - Search results -

Search results

Result 1 - 10 of total 46

Search options

Article ; Online: Selective activation of distinct Orai channels by STIM1.

Shuttleworth, Trevor J

2016 Volume 63, Page(s) 40–42

MeSH term(s)	Calcium/metabolism ; Humans ; Neoplasm Proteins/metabolism ; ORAI1 Protein/metabolism ; Stromal Interaction Molecule 1/metabolism
Chemical Substances	Neoplasm Proteins ; ORAI1 Protein ; ORAI1 protein, human ; STIM1 protein, human ; Stromal Interaction Molecule 1 ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-11-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2016.11.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1596: 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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Orai channels - new insights, new ideas.

Shuttleworth, Trevor J

The Journal of physiology

2012 Volume 590, Issue 17, Page(s) 4155–4156

MeSH term(s)	Animals ; Biophysical Phenomena ; Calcium Channels/immunology ; Calcium Channels/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Membrane Glycoproteins/metabolism
Chemical Substances	Calcium Channels ; Membrane Glycoproteins
Language	English
Publishing date	2012-09-07
Publishing country	England
Document type	Editorial ; Review
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.2012.237552
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: 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

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: STIM and Orai proteins and the non-capacitative ARC channels.

Shuttleworth, Trevor J

Frontiers in bioscience (Landmark edition)

2012 Volume 17, Issue 3, Page(s) 847–860

Abstract: The ARC channel is a small conductance, highly Ca²⁺-selective ion channel whose activation is specifically dependent on low concentrations of arachidonic acid acting at an intracellular site. They are widely distributed in diverse cell types where they ... ...

Abstract	The ARC channel is a small conductance, highly Ca²⁺-selective ion channel whose activation is specifically dependent on low concentrations of arachidonic acid acting at an intracellular site. They are widely distributed in diverse cell types where they provide an alternative, store-independent pathway for agonist-activated Ca²⁺ entry. Although biophysically similar to the store-operated CRAC channels, these two conductances function under distinct conditions of agonist stimulation, with the ARC channels providing the predominant route of Ca²⁺ entry during the oscillatory signals generated at low agonist concentrations. Despite these differences in function, like the CRAC channel, activation of the ARC channels is dependent on STIM1, but it is the pool of STIM1 that constitutively resides in the plasma membrane that is responsible. Similarly, both channels are formed by Orai proteins but, whilst the CRAC channel pore is a tetrameric assembly of Orai1 subunits, the ARC channel pore is formed by a heteropentameric assembly of three Orai1 subunits and two Orai3 subunits. There is increasing evidence that the activity of these channels plays a critical role in a variety of different cellular activities.
MeSH term(s)	Animals ; Calcium Channels/chemistry ; Calcium Channels/metabolism ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Molecular ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/metabolism ; ORAI1 Protein ; Protein Multimerization ; Stromal Interaction Molecule 1
Chemical Substances	Calcium Channels ; Membrane Proteins ; Neoplasm Proteins ; ORAI1 Protein ; ORAI1 protein, human ; STIM1 protein, human ; Stromal Interaction Molecule 1
Language	English
Publishing date	2012-01-01
Publishing country	Singapore
Document type	Journal Article ; Review
ZDB-ID	2704569-9
ISSN	2768-6698 ; 1093-9946
ISSN (online)	2768-6698
ISSN	1093-9946
DOI	10.2741/3960
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Orai3--the 'exceptional' Orai?

Shuttleworth, Trevor J

The Journal of physiology

2011 Volume 590, Issue 2, Page(s) 241–257

Abstract: The field of agonist-activated Ca(2+) entry in non-excitable cells underwent a revolution some 5 years ago with the discovery of the Orai proteins as the essential pore-forming components of the low-conductance, highly Ca(2+)-selective CRAC channels ... ...

Abstract	The field of agonist-activated Ca(2+) entry in non-excitable cells underwent a revolution some 5 years ago with the discovery of the Orai proteins as the essential pore-forming components of the low-conductance, highly Ca(2+)-selective CRAC channels whose activation is dependent on depletion of intracellular stores. Mammals possess three distinct Orai proteins (Orai1, 2 and 3) of which Orai3 is unique to this class, apparently evolving from Orai1. However, the sequence of Orai3 shows marked differences from that of Orai1, particularly in those regions of the protein outside of the essential pore-forming domains. Correspondingly, studies from several different groups have indicated that the inclusion of Orai3 is associated with the appearance of conductances that display unique features in their gating, selectivity, regulation and mode of activation. In this Topical Review, these features are discussed with the purpose of proposing that the evolutionary appearance of Orai3 in mammals, and the consequent development of conductances displaying novel properties - whether formed by Orai3 alone or in conjunction with the other Orai proteins - is associated with the specific role of this member of the Orai family in a unique range of distinct cellular activities.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biological Evolution ; Calcium Channels/chemistry ; Calcium Channels/physiology ; HEK293 Cells ; Humans ; Ion Channel Gating/physiology ; Membrane Proteins/chemistry ; Membrane Proteins/physiology ; Molecular Sequence Data ; ORAI1 Protein
Chemical Substances	Calcium Channels ; Membrane Proteins ; ORAI1 Protein ; ORAI1 protein, human ; Orai3 protein, human
Language	English
Publishing date	2011-10-31
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.2011.220574
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: 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

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Anchoring protein AKAP79-mediated PKA phosphorylation of STIM1 determines selective activation of the ARC channel, a store-independent Orai channel.

Thompson, Jill L / Shuttleworth, Trevor J

The Journal of physiology

2015 Volume 593, Issue 3, Page(s) 559–572

Abstract: Key points: Although both the calcium store-dependent CRAC channels and the store-independent ARC channels are regulated by the protein STIM1, CRAC channels are regulated by STIM1 in the endoplasmic reticulum, whilst ARC channels are regulated by the ... ...

Abstract	Key points: Although both the calcium store-dependent CRAC channels and the store-independent ARC channels are regulated by the protein STIM1, CRAC channels are regulated by STIM1 in the endoplasmic reticulum, whilst ARC channels are regulated by the STIM1 constitutively resident in the plasma membrane. We now demonstrate that activation of the ARC channels, but not CRAC channels, is uniquely dependent on phosphorylation of a single residue (T389) in the extensive cytosolic domain of STIM1 by protein kinase A. We further demonstrate that the phosphorylation of the T389 residue by protein kinase A is mediated by the association of plasma membrane STIM1 with the scaffolding protein AKAP79. Together, these findings indicate that the phosphorylation status of this single residue in STIM1 represents a key molecular determinant of the relative activities of these two co-existing Ca(2+) entry channels that are known to play critical, but distinct, roles in modulating a variety of physiologically relevant activities. Abstract: The low-conductance, highly calcium-selective channels encoded by the Orai family of proteins represent a major pathway for the agonist-induced entry of calcium associated with the generation and modulation of the key intracellular calcium signals that initiate and control a wide variety of physiologically important processes in cells. There are two distinct members of this channel family that co-exist endogenously in many cell types: the store-operated Ca(2+) release-activated CRAC channels and the store-independent arachidonic acid-regulated ARC channels. Although the activities of both channels are regulated by the stromal-interacting molecule-1 (STIM1) protein, two distinct pools of this protein are responsible, with the major pool of STIM1 in the endoplasmic reticulum membrane regulating CRAC channel activity, whilst the minor pool of plasma membrane STIM1 regulates ARC channel activity. We now show that a critical feature in determining this selective activation of the two channels is the phosphorylation status of a single threonine residue (T389) within the extensive (∼450 residue) cytosolic domain of STIM1. Specifically, protein kinase A (PKA)-mediated phosphorylation of T389 of STIM1 is necessary for effective activation of the ARC channels, whilst phosphorylation of the same residue actually inhibits the ability of STIM1 to activate the CRAC channels. We further demonstrate that the PKA-mediated phosphorylation of T389 occurs at the plasma membrane via the involvement of the anchoring protein AKAP79, which is constitutively associated with the pool of STIM1 in the plasma membrane. The novel mechanism we have described provides a means for the cell to precisely regulate the relative activities of these two channels to independently modulate the resulting intracellular calcium signals in a physiologically relevant manner.
MeSH term(s)	A Kinase Anchor Proteins/metabolism ; Amino Acid Sequence ; Calcium Channels/chemistry ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Calcium Signaling ; Cyclic AMP-Dependent Protein Kinases/metabolism ; HEK293 Cells ; Humans ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Stromal Interaction Molecule 1
Chemical Substances	A Kinase Anchor Proteins ; Calcium Channels ; Stim1 protein, mouse ; Stromal Interaction Molecule 1 ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2015-02-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.2014.284182
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: 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

Details ▾

Article ; Online: Arachidonic acid, ARC channels, and Orai proteins.

Shuttleworth, Trevor J

Cell calcium

2009 Volume 45, Issue 6, Page(s) 602–610

Abstract: A critical role for arachidonic acid in the regulation of calcium entry during agonist activation of calcium signals has become increasingly apparent in numerous studies over the past 10 years or so. In particular, low concentrations of this fatty acid, ... ...

Abstract	A critical role for arachidonic acid in the regulation of calcium entry during agonist activation of calcium signals has become increasingly apparent in numerous studies over the past 10 years or so. In particular, low concentrations of this fatty acid, generated as a result of physiologically relevant activation of appropriate receptors, induces the activation of a unique, highly calcium-selective conductance now known as the ARC channel. Activation of this channel is specifically dependent on arachidonic acid acting at the intracellular surface of the membrane, and is entirely independent of any depletion of internal calcium stores. Importantly, a specific role of this channel in modulating the frequency of oscillatory calcium signals in various cell types has been described. Recent studies, subsequent to the discovery of STIM1 and the Orai proteins and their role in the store-operated CRAC channels, have revealed that these same proteins are also integral components of the ARC channels and their activation. However, unlike the CRAC channels, activation of the ARC channels depends on the pool of STIM1 that is constitutively resident in the plasma membrane, and the pore of these channels is comprised of both Orai1 and Orai3 subunits. The clear implication is that CRAC channels and ARC channels are closely related, but have evolved to play unique roles in the modulation of calcium signals-largely as a result of their entirely distinct modes of activation. Given this, although the precise details of how arachidonic acid acts to activate the channels remain unclear, it seems likely that the specific molecular features of these channels that distinguish them from the CRAC channels--namely Orai3 and/or plasma membrane STIM1--will be involved.
MeSH term(s)	Arachidonic Acid/metabolism ; Arachidonic Acid/pharmacology ; Arachidonic Acid/physiology ; Calcium/metabolism ; Calcium Channels/metabolism ; Calcium Signaling/physiology ; Cell Line ; Fatty Acids/metabolism ; Fatty Acids/pharmacology ; Humans
Chemical Substances	Calcium Channels ; Fatty Acids ; Arachidonic Acid (27YG812J1I) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2009-03-17
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2009.02.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1596: 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

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: How many Orai's does it take to make a CRAC channel?

Thompson, Jill L / Shuttleworth, Trevor J

Scientific reports

2013 Volume 3, Page(s) 1961

Abstract: CRAC (Calcium Release-Activated Calcium) channels represent the primary pathway for so-called "store-operated calcium entry" - the cellular entry of calcium induced by depletion of intracellular calcium stores. These channels play a key role in diverse ... ...

Abstract	CRAC (Calcium Release-Activated Calcium) channels represent the primary pathway for so-called "store-operated calcium entry" - the cellular entry of calcium induced by depletion of intracellular calcium stores. These channels play a key role in diverse cellular activities, most noticeably in the differentiation and activation of Tcells, and in the response of mast cells to inflammatory signals. CRAC channels are formed by members of the recently discovered Orai protein family, with previous studies indicating that the functional channel is formed by a tetramer of Orai subunits. However, a recent report has shown that crystals obtained from the purified Drosophila Orai protein display a hexameric channel structure. Here, by comparing the biophysical properties of concatenated hexameric and tetrameric human Orai1 channels expressed in HEK293 cells, we show that the tetrameric channel displays the highly calcium-selective conductance properties consistent with endogenous CRAC channels, whilst the hexameric construct forms an essentially non-selective cation channel.
MeSH term(s)	Calcium Channels/metabolism ; HEK293 Cells ; Humans
Chemical Substances	Calcium Channels
Language	English
Publishing date	2013-06-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep01961
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Exploring the unique features of the ARC channel, a store-independent Orai channel.

Thompson, Jill L / Shuttleworth, Trevor J

Channels (Austin, Tex.)

2013 Volume 7, Issue 5, Page(s) 364–373

Abstract: The discovery of the Orai proteins, and the identification of STIM1 as the molecule that regulates them, was based on their role in the agonist-activated store-operated entry of calcium via the CRAC channels. However, these same proteins are also ... ...

Abstract	The discovery of the Orai proteins, and the identification of STIM1 as the molecule that regulates them, was based on their role in the agonist-activated store-operated entry of calcium via the CRAC channels. However, these same proteins are also essential components of the ARC channels responsible for a similar agonist-activated, but store-independent, arachidonic acid-regulated entry of calcium. The fact that these 2 biophysically similar calcium entry pathways frequently co-exist in the same cells suggests that they must each possess different features that allow them to function in distinct ways to regulate specific cellular activities. This review begins to address this question by describing recent findings characterizing the unique features of the ARC channels--their molecular composition, STIM1-dependent activation, and physiological activities--and the importance of defining such features for the accurate therapeutic targeting of these 2 Orai channel subtypes.
MeSH term(s)	Arachidonic Acid/metabolism ; Calcium/metabolism ; Calcium Channels/metabolism ; Humans ; Membrane Proteins/metabolism ; Neoplasm Proteins/metabolism ; ORAI1 Protein ; Stromal Interaction Molecule 1
Chemical Substances	Calcium Channels ; Membrane Proteins ; Neoplasm Proteins ; ORAI1 Protein ; ORAI1 protein, human ; STIM1 protein, human ; Stromal Interaction Molecule 1 ; Arachidonic Acid (27YG812J1I) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-09-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2262854-X
ISSN	1933-6969 ; 1933-6969
ISSN (online)	1933-6969
ISSN	1933-6969
DOI	10.4161/chan.26156
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Molecular basis of activation of the arachidonate-regulated Ca2+ (ARC) channel, a store-independent Orai channel, by plasma membrane STIM1.

Thompson, Jill L / Shuttleworth, Trevor J

The Journal of physiology

2013 Volume 591, Issue 14, Page(s) 3507–3523

Abstract: Currently, Orai proteins are known to encode two distinct agonist-activated, highly calcium-selective channels: the store-operated Ca(2+) release-activated Ca(2+) (CRAC) channels, and the store-independent, arachidonic acid-activated ARC channels. ... ...

Abstract	Currently, Orai proteins are known to encode two distinct agonist-activated, highly calcium-selective channels: the store-operated Ca(2+) release-activated Ca(2+) (CRAC) channels, and the store-independent, arachidonic acid-activated ARC channels. Surprisingly, whilst the trigger for activation of these channels is entirely different, both depend on stromal interacting molecule 1 (STIM1). However, whilst STIM1 in the endoplasmic reticulum membrane is the critical sensor for the depletion of this calcium store that triggers CRAC channel activation, it is the pool of STIM1 constitutively resident in the plasma membrane that is essential for activation of the ARC channels. Here, using a variety of approaches, we show that the key domains within the cytosolic part of STIM1 identified as critical for the activation of CRAC channels are also key for activation of the ARC channels. However, examination of the actual steps involved in such activation reveal marked differences between these two Orai channel types. Specifically, loss of calcium from the EF-hand of STIM1 that forms the key initiation point for activation of the CRAC channels has no effect on ARC channel activity. Secondly, in marked contrast to the dynamic and labile nature of interactions between STIM1 and the CRAC channels, STIM1 in the plasma membrane appears to be constitutively associated with the ARC channels. Finally, specific mutations in STIM1 that induce an extended, constitutively active, conformation for the CRAC channels actually prevent activation of the ARC channels by arachidonic acid. Based on these findings, we propose that the likely role of arachidonic acid lies in inducing the actual gating of the channel.
MeSH term(s)	Arachidonic Acid/physiology ; Calcium Channels/physiology ; Cell Membrane/physiology ; HEK293 Cells ; Humans ; Membrane Proteins/physiology ; Neoplasm Proteins/physiology ; Stromal Interaction Molecule 1
Chemical Substances	Calcium Channels ; Membrane Proteins ; Neoplasm Proteins ; STIM1 protein, human ; Stromal Interaction Molecule 1 ; Arachidonic Acid (27YG812J1I)
Language	English
Publishing date	2013-05-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.2013.256784
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: 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

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Phosphorylation-mediated structural changes within the SOAR domain of stromal interaction molecule 1 enable specific activation of distinct Orai channels.

Thompson, Jill L / Lai-Zhao, Yue / Stathopulos, Peter B / Grossfield, Alan / Shuttleworth, Trevor J

The Journal of biological chemistry

2018 Volume 293, Issue 9, Page(s) 3145–3155

Abstract: Low-conductance, highly calcium-selective channels formed by the Orai proteins exist as store-operated CRAC channels and store-independent, arachidonic acid-activated ARC channels. Both are activated by stromal interaction molecule 1 (STIM1), but CRAC ... ...

Abstract	Low-conductance, highly calcium-selective channels formed by the Orai proteins exist as store-operated CRAC channels and store-independent, arachidonic acid-activated ARC channels. Both are activated by stromal interaction molecule 1 (STIM1), but CRAC channels are activated by STIM1 located in the endoplasmic reticulum membrane, whereas ARC channels are activated by the minor plasma membrane-associated pool of STIM1. Critically, maximally activated CRAC channel and ARC channel currents are completely additive within the same cell, and their selective activation results in their ability to each induce distinct cellular responses. We have previously shown that specific ARC channel activation requires a PKA-mediated phosphorylation of a single threonine residue (Thr
MeSH term(s)	Biological Transport ; Calcium/metabolism ; Calcium Release Activated Calcium Channels/metabolism ; HEK293 Cells ; Humans ; Phosphorylation ; Protein Domains ; Stromal Interaction Molecule 1/chemistry ; Stromal Interaction Molecule 1/metabolism
Chemical Substances	Calcium Release Activated Calcium Channels ; Stromal Interaction Molecule 1 ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-01-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M117.819078
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: 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

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito