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Article: Corrigendum to "Erdheim-Chester disease with tendon and muscle involvement: Reports of a rare presentation" [Radiology Case Reports 19 (2024) 1866-1871].

Golagha, Mahshid / Firouzabadi, Fatemeh Dehghani / Millo, Corina / Nikpanah, Moozhan / Ahlman, Mark A / Dave, Rahul H / Estrada-Veras, Juvianee I / O'Brien, Kevin / Malayeri, Ashkan A

Radiology case reports

2024 Volume 19, Issue 6, Page(s) 2576–2577

Abstract: This corrects the article DOI: 10.1016/j.radcr.2024.02.009.]. ...

Abstract	[This corrects the article DOI: 10.1016/j.radcr.2024.02.009.].
Language	English
Publishing date	2024-03-28
Publishing country	Netherlands
Document type	Published Erratum
ZDB-ID	2406300-9
ISSN	1930-0433
ISSN	1930-0433
DOI	10.1016/j.radcr.2024.02.112
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Article: Erdheim-Chester disease with tendon and muscle involvement: Reports of a rare presentation.

Golagha, Mahshid / Dehghani Firouzabadi, Fatemeh / Millo, Corina / Nikpanah, Moozhan / Ahlman, Mark A / Dave, Rahul H / Estrada-Veras, Juvianee I / O'Brien, Kevin / Malayeri, Ashkan A

Radiology case reports

2024 Volume 19, Issue 5, Page(s) 1866–1871

Abstract: Erdheim-Chester disease (ECD) is a rare histiocytic disease that affects multiple systems in the body. While it typically targets long bones, cardiovascular structures, the retroperitoneum, and the central nervous system, reports of tendon and skeletal ... ...

Abstract	Erdheim-Chester disease (ECD) is a rare histiocytic disease that affects multiple systems in the body. While it typically targets long bones, cardiovascular structures, the retroperitoneum, and the central nervous system, reports of tendon and skeletal muscle involvement are scarce. This review presents 2 cases: a case of ECD involving the left Achilles tendon and left abductor hallucis, as well as an unusual manifestation of ECD in the thigh musculature. In Case 1, studies involved a 39-year-old man who initially presented with bone and pituitary involvement. An order for
Language	English
Publishing date	2024-02-23
Publishing country	Netherlands
Document type	Case Reports
ZDB-ID	2406300-9
ISSN	1930-0433
ISSN	1930-0433
DOI	10.1016/j.radcr.2024.02.009
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Article: Rituximab for Autoimmune Encephalitis with Epilepsy.

Kurukumbi, Mohankumar / Dave, Rahul H / Castillo, Jose / Shah, Tulsi / Lau, Joanne

Case reports in neurological medicine

2020 Volume 2020, Page(s) 5843089

Abstract: Intractable epilepsy remains a significant medical challenge, resulting in recurrent and prolonged intensive care unit (ICU) admissions. Autoimmune encephalitis is emerging as a treatable cause of intractable epilepsy. It is characterized by antibodies ... ...

Abstract	Intractable epilepsy remains a significant medical challenge, resulting in recurrent and prolonged intensive care unit (ICU) admissions. Autoimmune encephalitis is emerging as a treatable cause of intractable epilepsy. It is characterized by antibodies against cerebral antigens, such as potassium channels such as leucine-rich, glioma inactivated 1 (LGI1) and contactin-associated protein 2 (CASPR2), calcium channels such as the voltage-gated calcium channel (VGCC), or neurotransmitter receptors such as the
Language	English
Publishing date	2020-06-23
Publishing country	United States
Document type	Case Reports
ZDB-ID	2629909-4
ISSN	2090-6676 ; 2090-6668
ISSN (online)	2090-6676
ISSN	2090-6668
DOI	10.1155/2020/5843089
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Article: Pituitary Imaging Abnormalities and Related Endocrine Disorders in Erdheim-Chester Disease.

Shekhar, Skand / Irizarry-Caro, Jorge A / Sinaii, Ninet / Gahl, William A / Estrada-Veras, Juvianee I / Dave, Rahul H / Gochuico, Bernadette R / Papadakis, Georgios Z / Patronas, Nicholas / Stratakis, Constantine A / O'Brien, Kevin / Hannah-Shmouni, Fady

Cancers

2021 Volume 13, Issue 16

Abstract: Purpose: We examined abnormal pituitary imaging (API) and associated endocrine dysfunction in subjects with ECD.: Methods: A cross-sectional descriptive examination of a natural history cohort study diagnosed with ECD was conducted at a clinical ... ...

Abstract	Purpose: We examined abnormal pituitary imaging (API) and associated endocrine dysfunction in subjects with ECD. Methods: A cross-sectional descriptive examination of a natural history cohort study diagnosed with ECD was conducted at a clinical research center. Subjects underwent baseline endocrine tests of anterior and posterior pituitary function and dedicated pituitary gland MRI scans. We determined the frequency of various pituitary imaging abnormalities in ECD and assessed its relationships with age, sex, body mass index (BMI), Results: Our cohort included 61 subjects with ECD [age (SD): 54.3 (10.9) y, 46 males/15 females]. API was present in 47.5% (29/61) of ECD subjects. Loss of the posterior pituitary bright spot (36.1%) followed by thickened pituitary stalk (24.6%), abnormal enhancement (18.0%), and pituitary atrophy (14.8%) were the most common abnormalities. DI and panhypopituitarism were more frequent in subjects with API without differences in age, sex distribution, hsCRP, ESR, and Conclusions: We noted a high burden of API and endocrinopathies in ECD. API was highly associated with the presence of panhypopituitarism and DI. Therefore, a thorough assessment of hypothalamic-pituitary integrity should be considered in subjects with ECD.
Language	English
Publishing date	2021-08-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13164126
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Article ; Online: Neurological manifestations of Erdheim-Chester Disease.

Boyd, Louisa C / O'Brien, Kevin J / Ozkaya, Neval / Lehky, Tanya / Meoded, Avner / Gochuico, Bernadette R / Hannah-Shmouni, Fady / Nath, Avindra / Toro, Camilo / Gahl, William A / Estrada-Veras, Juvianee I / Dave, Rahul H

Annals of clinical and translational neurology

2020 Volume 7, Issue 4, Page(s) 497–506

Abstract: Objective: To characterize the spectrum of neurologic involvement in Erdheim-Chester Disease (ECD), a treatable inflammatory neoplasm of histiocytes.: Methods: Sixty-two patients with ECD were prospectively enrolled in a natural history study that ... ...

Abstract	Objective: To characterize the spectrum of neurologic involvement in Erdheim-Chester Disease (ECD), a treatable inflammatory neoplasm of histiocytes. Methods: Sixty-two patients with ECD were prospectively enrolled in a natural history study that facilitated collection of clinical, imaging, laboratory, neurophysiologic, and pathologic data. Results: Ninety-four percent of the patients had neurologic abnormalities on examination or imaging, and 22% had neurologic symptoms as the initial presentation of ECD. The most common neurologic findings were cognitive impairment, peripheral neuropathy, pyramidal tract signs, cranial nerve involvement, and cerebellar ataxia. Imaging revealed atrophy and demyelination along with focal lesions that were located throughout the nervous system, dura, and extra-axial structures. The BRAF V600E variant correlated with cerebral atrophy. Brain pathology revealed lipid-laden, phagocytic macrophages (histiocytes) accompanied by demyelination and axonal degeneration. Interpretation: In patients with ECD, neurologic morbidity is common and contributes significantly to disability. Since neurologic symptoms can be the presenting feature of ECD and, given the mean delay in ECD diagnosis is 4.2 years, it is critical that neurologists consider of ECD and other histiocytosis in patients with inflammatory, infectious, or neoplastic-appearing white matter. Furthermore, given the broad spectrum of neurologic involvement, neurologists have an important role in a team of specialists treating ECD patients.
MeSH term(s)	Adult ; Aged ; Cerebellar Ataxia/diagnosis ; Cerebellar Ataxia/etiology ; Cerebellar Ataxia/physiopathology ; Cognitive Dysfunction/diagnosis ; Cognitive Dysfunction/etiology ; Cognitive Dysfunction/physiopathology ; Erdheim-Chester Disease/complications ; Erdheim-Chester Disease/diagnosis ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; Middle Aged ; Nervous System Diseases/diagnosis ; Nervous System Diseases/etiology ; Nervous System Diseases/pathology ; Nervous System Diseases/physiopathology ; Peripheral Nervous System Diseases/diagnosis ; Peripheral Nervous System Diseases/etiology ; Peripheral Nervous System Diseases/physiopathology ; Prospective Studies ; Young Adult
Language	English
Publishing date	2020-03-29
Publishing country	United States
Document type	Clinical Study ; Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2740696-9
ISSN	2328-9503 ; 2328-9503
ISSN (online)	2328-9503
ISSN	2328-9503
DOI	10.1002/acn3.51014
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Article: A Molecular and Structural Mechanism for G Protein-mediated Microtubule Destabilization

Davé, Rahul H / Saengsawang, Witchuda / Lopus, Manu / Davé, Sonya / Wilson, Leslie / Rasenick, Mark M

Journal of biological chemistry. 2011 Feb. 11, v. 286, no. 6

2011

Abstract: The heterotrimeric, G protein-coupled receptor-associated G protein, Gαs, binds tubulin with nanomolar affinity and disrupts microtubules in cells and in vitro. Here we determine that the activated form of Gαs binds tubulin with a KD of 100 nM, ... ...

Abstract	The heterotrimeric, G protein-coupled receptor-associated G protein, Gαs, binds tubulin with nanomolar affinity and disrupts microtubules in cells and in vitro. Here we determine that the activated form of Gαs binds tubulin with a KD of 100 nM, stimulates tubulin GTPase, and promotes microtubule dynamic instability. Moreover, the data reveal that the α3-β5 region of Gαs is a functionally important motif in the Gαs-mediated microtubule destabilization. Indeed, peptides corresponding to that region of Gαs mimic Gαs protein in activating tubulin GTPase and increase microtubule dynamic instability. We have identified specific mutations in peptides or proteins that interfere with this process. The data allow for a model of the Gαs/tubulin interface in which Gαs binds to the microtubule plus-end and activates the intrinsic tubulin GTPase. This model illuminates both the role of tubulin as an "effector" (e.g. adenylyl cyclase) for Gαs and the role of Gαs as a GTPase activator for tubulin. Given the ability of Gαs to translocate intracellularly in response to agonist activation, Gαs may play a role in hormone- or neurotransmitter-induced regulation of cellular morphology.
Language	English
Dates of publication	2011-0211
Size	p. 4319-4328.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

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Article: Cytosolic Gαs Acts as an Intracellular Messenger to Increase Microtubule Dynamics and Promote Neurite Outgrowth

Yu, Jiang-Zhou / Dave, Rahul H / Allen, John A / Sarma, Tulika / Rasenick, Mark M

Journal of biological chemistry. 2009 Apr. 17, v. 284, no. 16

2009

Abstract: It is now evident that Gαs traffics into cytosol following G protein-coupled receptor activation, and α subunits of some heterotrimeric G-proteins, including Gαs bind to tubulin in vitro. Nevertheless, many features of G-protein-microtubule interaction ... ...

Abstract	It is now evident that Gαs traffics into cytosol following G protein-coupled receptor activation, and α subunits of some heterotrimeric G-proteins, including Gαs bind to tubulin in vitro. Nevertheless, many features of G-protein-microtubule interaction and possible intracellular effects of G protein α subunits remain unclear. In this study, several biochemical approaches demonstrated that activated Gαs directly bound to tubulin and cellular microtubules, and fluorescence microscopy showed that cholera toxin-activated Gαs colocalized with microtubules. The activated, GTP-bound, Gαs mimicked tubulin in serving as a GTPase activator for β-tubulin. As a result, activated Gαs made microtubules more dynamic, both in vitro and in cells, decreasing the pool of insoluble microtubules without changing total cellular tubulin content. The amount of acetylated tubulin (an indicator of microtubule stability) was reduced in the presence of Gαs activated by mutation. Previous studies showed that cholera toxin and cAMP analogs may stimulate neurite outgrowth in PC12 cells. However, in this study, overexpression of a constitutively activated Gαs or activation of Gαs with cholera toxin in protein kinase A-deficient PC12 cells promoted neurite outgrowth in a cAMP-independent manner. Thus, it is suggested that activated Gαs acts as an intracellular messenger to regulate directly microtubule dynamics and promote neurite outgrowth. These data serve to link G-protein signaling with modulation of the cytoskeleton and cell morphology.
Language	English
Dates of publication	2009-0417
Size	p. 10462-10472.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article ; Online: A molecular and structural mechanism for G protein-mediated microtubule destabilization.

Davé, Rahul H / Saengsawang, Witchuda / Lopus, Manu / Davé, Sonya / Wilson, Leslie / Rasenick, Mark M

The Journal of biological chemistry

2010 Volume 286, Issue 6, Page(s) 4319–4328

Abstract: The heterotrimeric, G protein-coupled receptor-associated G protein, Gα(s), binds tubulin with nanomolar affinity and disrupts microtubules in cells and in vitro. Here we determine that the activated form of Gα(s) binds tubulin with a K(D) of 100 nm, ... ...

Abstract	The heterotrimeric, G protein-coupled receptor-associated G protein, Gα(s), binds tubulin with nanomolar affinity and disrupts microtubules in cells and in vitro. Here we determine that the activated form of Gα(s) binds tubulin with a K(D) of 100 nm, stimulates tubulin GTPase, and promotes microtubule dynamic instability. Moreover, the data reveal that the α3-β5 region of Gα(s) is a functionally important motif in the Gα(s)-mediated microtubule destabilization. Indeed, peptides corresponding to that region of Gα(s) mimic Gα(s) protein in activating tubulin GTPase and increase microtubule dynamic instability. We have identified specific mutations in peptides or proteins that interfere with this process. The data allow for a model of the Gα(s)/tubulin interface in which Gα(s) binds to the microtubule plus-end and activates the intrinsic tubulin GTPase. This model illuminates both the role of tubulin as an "effector" (e.g. adenylyl cyclase) for Gα(s) and the role of Gα(s) as a GTPase activator for tubulin. Given the ability of Gα(s) to translocate intracellularly in response to agonist activation, Gα(s) may play a role in hormone- or neurotransmitter-induced regulation of cellular morphology.
MeSH term(s)	Amino Acid Motifs ; Animals ; Cattle ; Enzyme Activation/physiology ; GTP-Binding Protein alpha Subunits, Gs/genetics ; GTP-Binding Protein alpha Subunits, Gs/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Models, Biological ; Mutation ; Protein Binding ; Protein Structure, Tertiary ; Sheep
Chemical Substances	GTP-Binding Protein alpha Subunits, Gs (EC 3.6.5.1)
Language	English
Publishing date	2010-11-26
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.M110.196436
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Article: Cytosolic G{alpha}s acts as an intracellular messenger to increase microtubule dynamics and promote neurite outgrowth.

Yu, Jiang-Zhou / Dave, Rahul H / Allen, John A / Sarma, Tulika / Rasenick, Mark M

The Journal of biological chemistry

2009 Volume 284, Issue 16, Page(s) 10462–10472

Abstract: It is now evident that Galpha(s) traffics into cytosol following G protein-coupled receptor activation, and alpha subunits of some heterotrimeric G-proteins, including Galpha(s) bind to tubulin in vitro. Nevertheless, many features of G-protein- ... ...

Abstract	It is now evident that Galpha(s) traffics into cytosol following G protein-coupled receptor activation, and alpha subunits of some heterotrimeric G-proteins, including Galpha(s) bind to tubulin in vitro. Nevertheless, many features of G-protein-microtubule interaction and possible intracellular effects of G protein alpha subunits remain unclear. In this study, several biochemical approaches demonstrated that activated Galpha(s) directly bound to tubulin and cellular microtubules, and fluorescence microscopy showed that cholera toxin-activated Galpha(s) colocalized with microtubules. The activated, GTP-bound, Galpha(s) mimicked tubulin in serving as a GTPase activator for beta-tubulin. As a result, activated Galpha(s) made microtubules more dynamic, both in vitro and in cells, decreasing the pool of insoluble microtubules without changing total cellular tubulin content. The amount of acetylated tubulin (an indicator of microtubule stability) was reduced in the presence of Galpha(s) activated by mutation. Previous studies showed that cholera toxin and cAMP analogs may stimulate neurite outgrowth in PC12 cells. However, in this study, overexpression of a constitutively activated Galpha(s) or activation of Galpha(s) with cholera toxin in protein kinase A-deficient PC12 cells promoted neurite outgrowth in a cAMP-independent manner. Thus, it is suggested that activated Galpha(s) acts as an intracellular messenger to regulate directly microtubule dynamics and promote neurite outgrowth. These data serve to link G-protein signaling with modulation of the cytoskeleton and cell morphology.
MeSH term(s)	Animals ; Cholera Toxin/metabolism ; Cyclic AMP/analogs & derivatives ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytosol/metabolism ; GTP-Binding Protein alpha Subunits/genetics ; GTP-Binding Protein alpha Subunits/metabolism ; Guanosine Triphosphate/metabolism ; Microtubules/metabolism ; Neurites/metabolism ; Neurites/ultrastructure ; PC12 Cells ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Rats ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Second Messenger Systems/physiology ; Tubulin/metabolism
Chemical Substances	GTP-Binding Protein alpha Subunits ; Protein Isoforms ; Recombinant Fusion Proteins ; Tubulin ; Guanosine Triphosphate (86-01-1) ; Cholera Toxin (9012-63-9) ; Cyclic AMP (E0399OZS9N) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2009-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M809166200
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Article ; Online: Heterotrimeric G-proteins interact directly with cytoskeletal components to modify microtubule-dependent cellular processes.

Dave, Rahul H / Saengsawang, Witchuda / Yu, Jiang-Zhou / Donati, Robert / Rasenick, Mark M

Neuro-Signals

2009 Volume 17, Issue 1, Page(s) 100–108

Abstract: A large percentage of current drugs target G-protein-coupled receptors, which couple to well-known signaling pathways involving cAMP or calcium. G-proteins themselves may subserve a second messenger function. Here, we review the role of tubulin and ... ...

Abstract	A large percentage of current drugs target G-protein-coupled receptors, which couple to well-known signaling pathways involving cAMP or calcium. G-proteins themselves may subserve a second messenger function. Here, we review the role of tubulin and microtubules in directly mediating effects of heterotrimeric G-proteins on neuronal outgrowth, shape and differentiation. G-protein-tubulin interactions appear to be regulated by neurotransmitter activity, and, in turn, regulate the location of Galpha in membrane microdomains (such as lipid rafts) or the cytosol. Tubulin binds with nanomolar affinity to Gsalpha, Gialpha1 and Gqalpha (but not other Galpha subunits) as well as Gbeta(1)gamma(2) subunits. Galpha subunits destabilize microtubules by stimulating tubulin's GTPase, while Gbetagamma subunits promote microtubule stability. The same region on Gsalpha that binds adenylyl cyclase and Gbetagamma also interacts with tubulin, suggesting that cytoskeletal proteins are novel Galpha effectors. Additionally, intracellular Gialpha-GDP, in concert with other GTPase proteins and Gbetagamma, regulates the position of the mitotic spindle in mitosis. Thus, G-protein activation modulates cell growth and differentiation by directly altering microtubule stability. Further studies are needed to fully establish a structural mechanism of this interaction and its role in synaptic plasticity.
MeSH term(s)	Adenylyl Cyclases/metabolism ; Animals ; Cell Membrane/metabolism ; Cytosol/metabolism ; GTP Phosphohydrolases/metabolism ; Heterotrimeric GTP-Binding Proteins/chemistry ; Heterotrimeric GTP-Binding Proteins/metabolism ; Humans ; Microtubules/metabolism ; Models, Molecular ; Neurogenesis ; Neurons/physiology ; Neurons/ultrastructure ; Neurotransmitter Agents/metabolism ; Protein Stability ; Protein Structure, Quaternary ; Spindle Apparatus/physiology ; Tubulin/metabolism
Chemical Substances	Neurotransmitter Agents ; Tubulin ; GTP Phosphohydrolases (EC 3.6.1.-) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1) ; Adenylyl Cyclases (EC 4.6.1.1)
Language	English
Publishing date	2009-02-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2074039-6
ISSN	1424-8638 ; 1424-862X
ISSN (online)	1424-8638
ISSN	1424-862X
DOI	10.1159/000186693
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