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Article ; Online: Crystal structure of dopamine D1 receptor in complex with G protein and a non-catechol agonist

Bingfa Sun / Dan Feng / Matthew Ling-Hon Chu / Inbar Fish / Silvia Lovera / Zara A. Sands / Sebastian Kelm / Anne Valade / Martyn Wood / Tom Ceska / Tong Sun Kobilka / Florence Lebon / Brian K. Kobilka

Nature Communications, Vol 12, Iss 1, Pp 1-

2021 Volume 9

Abstract: Recently, a class of non-catechol Dopamine D1 receptor (D1R) selective agonists with novel scaffold and improved pharmacological properties were reported. Here, authors report the crystal structure of D1R in complex with stimulatory G protein (Gs) and a ... ...

Abstract	Recently, a class of non-catechol Dopamine D1 receptor (D1R) selective agonists with novel scaffold and improved pharmacological properties were reported. Here, authors report the crystal structure of D1R in complex with stimulatory G protein (Gs) and a non-catechol agonist Compound 1 which explains the selectivity of this scaffold for D1R over other aminergic receptors and the mechanism of activating D1R.
Keywords	Science ; Q
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Crystal structure of dopamine D1 receptor in complex with G protein and a non-catechol agonist.

Sun, Bingfa / Feng, Dan / Chu, Matthew Ling-Hon / Fish, Inbar / Lovera, Silvia / Sands, Zara A / Kelm, Sebastian / Valade, Anne / Wood, Martyn / Ceska, Tom / Kobilka, Tong Sun / Lebon, Florence / Kobilka, Brian K

Nature communications

2021 Volume 12, Issue 1, Page(s) 3305

Abstract: Dopamine D1 receptor (D1R) is an important drug target implicated in many psychiatric and neurological disorders. Selective agonism of D1R are sought to be the therapeutic strategy for these disorders. Most selective D1R agonists share a dopamine-like ... ...

Abstract	Dopamine D1 receptor (D1R) is an important drug target implicated in many psychiatric and neurological disorders. Selective agonism of D1R are sought to be the therapeutic strategy for these disorders. Most selective D1R agonists share a dopamine-like catechol moiety in their molecular structure, and their therapeutic potential is therefore limited by poor pharmacological properties in vivo. Recently, a class of non-catechol D1R selective agonists with a distinct scaffold and pharmacological properties were reported. Here, we report the crystal structure of D1R in complex with stimulatory G protein (Gs) and a non-catechol agonist Compound 1 at 3.8 Å resolution. The structure reveals the ligand bound to D1R in an extended conformation, spanning from the orthosteric site to extracellular loop 2 (ECL2). Structural analysis reveals that the unique features of D1R ligand binding pocket explains the remarkable selectivity of this scaffold for D1R over other aminergic receptors, and sheds light on the mechanism for D1R activation by the non-catechol agonist.
MeSH term(s)	Binding Sites ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gs/chemistry ; Humans ; In Vitro Techniques ; Ligands ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Protein Engineering ; Protein Structure, Quaternary ; Receptors, Dopamine D1/agonists ; Receptors, Dopamine D1/chemistry ; Recombinant Proteins/chemistry
Chemical Substances	DRD1 protein, human ; Ligands ; Receptors, Dopamine D1 ; Recombinant Proteins ; GTP-Binding Protein alpha Subunits, Gs (EC 3.6.5.1)
Language	English
Publishing date	2021-06-03
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23519-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: One size does not fit all: navigating the multi-dimensional space to optimize T-cell engaging protein therapeutics.

Chen, Wei / Yang, Fan / Wang, Carole / Narula, Jatin / Pascua, Edward / Ni, Irene / Ding, Sheng / Deng, Xiaodi / Chu, Matthew Ling-Hon / Pham, Amber / Jiang, Xiaoyue / Lindquist, Kevin C / Doonan, Patrick J / Van Blarcom, Tom / Yeung, Yik Andy / Chaparro-Riggers, Javier

mAbs

2021 Volume 13, Issue 1, Page(s) 1871171

Abstract: T-cell engaging biologics is a class of novel and promising immune-oncology compounds that leverage the immune system to eradicate cancer. Here, we compared and contrasted a bispecific diabody-Fc format, which displays a relatively short antigen-binding ... ...

Abstract	T-cell engaging biologics is a class of novel and promising immune-oncology compounds that leverage the immune system to eradicate cancer. Here, we compared and contrasted a bispecific diabody-Fc format, which displays a relatively short antigen-binding arm distance, with our bispecific IgG platform. By generating diverse panels of antigen-expressing cells where B cell maturation antigen is either tethered to the cell membrane or located to the juxtamembrane region and masked by elongated structural spacer units, we presented a systematic approach to investigate the role of antigen epitope location and molecular formats in immunological synapse formation and cytotoxicity. We demonstrated that diabody-Fc is more potent for antigen epitopes located in the membrane distal region, while bispecific IgG is more efficient for membrane-proximal epitopes. Additionally, we explored other parameters, including receptor density, antigen-binding affinity, and kinetics. Our results show that molecular format and antigen epitope location, which jointly determine the intermembrane distance between target cells and T cells, allow decoupling of cytotoxicity and cytokine release, while antigen-binding affinities appear to be positively correlated with both readouts. Our work offers new insight that could potentially lead to a wider therapeutic window for T-cell engaging biologics in general.
MeSH term(s)	Animals ; Antibodies, Bispecific/genetics ; Antibodies, Bispecific/immunology ; Antibodies, Bispecific/metabolism ; Antibodies, Bispecific/pharmacology ; Antibody-Dependent Cell Cytotoxicity ; Antigen-Antibody Reactions ; B-Cell Maturation Antigen/immunology ; B-Cell Maturation Antigen/metabolism ; Binding Sites, Antibody ; Biological Products/immunology ; Biological Products/metabolism ; Biological Products/pharmacology ; CD3 Complex/immunology ; CD3 Complex/metabolism ; Cell Line, Tumor ; Cytokines/metabolism ; Epitope Mapping ; Epitopes ; Humans ; Immunoglobulin G/genetics ; Immunoglobulin G/immunology ; Immunoglobulin G/metabolism ; Immunoglobulin G/pharmacology ; Immunological Synapses/drug effects ; Immunological Synapses/immunology ; Immunological Synapses/metabolism ; Kinetics ; Protein Engineering ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism ; T-Lymphocytes/drug effects ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; fms-Like Tyrosine Kinase 3/immunology ; fms-Like Tyrosine Kinase 3/metabolism
Chemical Substances	Antibodies, Bispecific ; B-Cell Maturation Antigen ; Biological Products ; CD3 Complex ; Cytokines ; Epitopes ; Immunoglobulin G ; Receptors, Antigen, T-Cell ; FLT3 protein, human (EC 2.7.10.1) ; fms-Like Tyrosine Kinase 3 (EC 2.7.10.1)
Language	English
Publishing date	2021-02-08
Publishing country	United States
Document type	Comparative Study ; Journal Article
ZDB-ID	2537838-7
ISSN	1942-0870 ; 1942-0870
ISSN (online)	1942-0870
ISSN	1942-0870
DOI	10.1080/19420862.2020.1871171
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Article ; Online: Crystal structure of the adenosine A

Sun, Bingfa / Bachhawat, Priti / Chu, Matthew Ling-Hon / Wood, Martyn / Ceska, Tom / Sands, Zara A / Mercier, Joel / Lebon, Florence / Kobilka, Tong Sun / Kobilka, Brian K

Proceedings of the National Academy of Sciences of the United States of America

2017 Volume 114, Issue 8, Page(s) 2066–2071

Abstract: The adenosine ... ...

Abstract	The adenosine A
Language	English
Publishing date	2017-02-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1621423114
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Article ; Online: Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6.

Stamos, Jennifer L / Chu, Matthew Ling-Hon / Enos, Michael D / Shah, Niket / Weis, William I

eLife

2014 Volume 3, Page(s) e01998

Abstract: Glycogen synthase kinase-3 (GSK-3) is a key regulator of many cellular signaling pathways. Unlike most kinases, GSK-3 is controlled by inhibition rather than by specific activation. In the insulin and several other signaling pathways, phosphorylation of ... ...

Abstract	Glycogen synthase kinase-3 (GSK-3) is a key regulator of many cellular signaling pathways. Unlike most kinases, GSK-3 is controlled by inhibition rather than by specific activation. In the insulin and several other signaling pathways, phosphorylation of a serine present in a conserved sequence near the amino terminus of GSK-3 generates an auto-inhibitory peptide. In contrast, Wnt/β-catenin signal transduction requires phosphorylation of Ser/Pro rich sequences present in the Wnt co-receptors LRP5/6, and these motifs inhibit GSK-3 activity. We present crystal structures of GSK-3 bound to its phosphorylated N-terminus and to two of the phosphorylated LRP6 motifs. A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition. The structures rationalize target sequence preferences and suggest avenues for the design of inhibitors selective for a subset of pathways regulated by GSK-3. DOI: http://dx.doi.org/10.7554/eLife.01998.001.
MeSH term(s)	Amino Acid Sequence ; Animals ; Catalysis ; Crystallography, X-Ray ; Glycogen Synthase Kinase 3/antagonists & inhibitors ; Glycogen Synthase Kinase 3/chemistry ; Glycogen Synthase Kinase 3/metabolism ; Humans ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Sequence Homology, Amino Acid ; Substrate Specificity
Chemical Substances	Glycogen Synthase Kinase 3 (EC 2.7.11.26)
Language	English
Publishing date	2014-03-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.01998
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Article ; Online: Ligand-Blocking and Membrane-Proximal Domain Targeting Anti-OX40 Antibodies Mediate Potent T Cell-Stimulatory and Anti-Tumor Activity

Pamela Zhang / Guang Huan Tu / Jie Wei / Pamela Santiago / Lance R. Larrabee / Sindy Liao-Chan / Tina Mistry / Matthew Ling-Hon Chu / Tao Sai / Kevin Lindquist / Hua Long / Javier Chaparro-Riggers / Shahram Salek-Ardakani / Yik Andy Yeung

Cell Reports, Vol 27, Iss 11, Pp 3117-3123.e

2019 Volume 5

Abstract: Summary: Agonistic antibodies targeting the tumor necrosis factor (TNF) superfamily of co-stimulatory receptors (TNFRSF) are progressing through various stages of clinical development for cancer treatment, but the desired and defining features of these ... ...

Abstract	Summary: Agonistic antibodies targeting the tumor necrosis factor (TNF) superfamily of co-stimulatory receptors (TNFRSF) are progressing through various stages of clinical development for cancer treatment, but the desired and defining features of these agents for optimal biological activity remain controversial. One idea, based on recent studies with CD40, is that non-ligand-blocking antibodies targeting membrane-distal cysteine-rich domain 1 (CRD1) have superior agonistic activities compared with ligand-blocking antibodies targeting more membrane-proximal CRDs. Here, we determined the binding and functional characteristics of a panel of antibodies targeting CRDs 1–4 of OX40 (also known as TNFRSF4 or CD134). In striking contrast to CD40, we found that ligand-blocking CRD2-binding and membrane-proximal CRD4-binding anti-OX40 antibodies have the strongest agonistic and anti-tumor activities. These findings have important translational implications and further highlight that the relationship between epitope specificity and agonistic activity will be an important issue to resolve on a case-by-case basis when optimizing antibodies targeting different co-stimulatory tumor necrosis factor receptors (TNFRs). : Epitope specificity is an important consideration when designing anti-TNFR agonistic antibodies for cancer treatment. Zhang et al. identify a new panel of antibodies targeting CRDs 1–4 of OX40 and show that ligand-blocking CRD2-binding and membrane-proximal CRD4-binding anti-OX40 antibodies have the strongest agonistic and anti-tumor activities. Keywords: OX40, agonist, monoclonal antibody, epitope, TNFR, OX86, ligand-blocking, membrane-proximal
Keywords	Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2019-06-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Ligand-Blocking and Membrane-Proximal Domain Targeting Anti-OX40 Antibodies Mediate Potent T Cell-Stimulatory and Anti-Tumor Activity.

Zhang, Pamela / Tu, Guang Huan / Wei, Jie / Santiago, Pamela / Larrabee, Lance R / Liao-Chan, Sindy / Mistry, Tina / Chu, Matthew Ling-Hon / Sai, Tao / Lindquist, Kevin / Long, Hua / Chaparro-Riggers, Javier / Salek-Ardakani, Shahram / Yeung, Yik Andy

Cell reports

2019 Volume 27, Issue 11, Page(s) 3117–3123.e5

Abstract: Agonistic antibodies targeting the tumor necrosis factor (TNF) superfamily of co-stimulatory receptors (TNFRSF) are progressing through various stages of clinical development for cancer treatment, but the desired and defining features of these agents for ...

Abstract	Agonistic antibodies targeting the tumor necrosis factor (TNF) superfamily of co-stimulatory receptors (TNFRSF) are progressing through various stages of clinical development for cancer treatment, but the desired and defining features of these agents for optimal biological activity remain controversial. One idea, based on recent studies with CD40, is that non-ligand-blocking antibodies targeting membrane-distal cysteine-rich domain 1 (CRD1) have superior agonistic activities compared with ligand-blocking antibodies targeting more membrane-proximal CRDs. Here, we determined the binding and functional characteristics of a panel of antibodies targeting CRDs 1-4 of OX40 (also known as TNFRSF4 or CD134). In striking contrast to CD40, we found that ligand-blocking CRD2-binding and membrane-proximal CRD4-binding anti-OX40 antibodies have the strongest agonistic and anti-tumor activities. These findings have important translational implications and further highlight that the relationship between epitope specificity and agonistic activity will be an important issue to resolve on a case-by-case basis when optimizing antibodies targeting different co-stimulatory tumor necrosis factor receptors (TNFRs).
MeSH term(s)	Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; Epitopes/chemistry ; Epitopes/immunology ; Humans ; Immunotherapy/methods ; Jurkat Cells ; Lymphocyte Activation ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Neoplasms, Experimental/therapy ; OX40 Ligand/chemistry ; OX40 Ligand/immunology ; Rats ; Rats, Inbred Lew ; Receptors, OX40/chemistry ; Receptors, OX40/immunology
Chemical Substances	Antibodies, Monoclonal ; Epitopes ; OX40 Ligand ; Receptors, OX40
Language	English
Publishing date	2019-06-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2019.05.027
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6

Jennifer L Stamos / Matthew Ling-Hon Chu / Michael D Enos / Niket Shah / William I Weis

eLife, Vol

2014 Volume 3

Abstract	Glycogen synthase kinase-3 (GSK-3) is a key regulator of many cellular signaling pathways. Unlike most kinases, GSK-3 is controlled by inhibition rather than by specific activation. In the insulin and several other signaling pathways, phosphorylation of a serine present in a conserved sequence near the amino terminus of GSK-3 generates an auto-inhibitory peptide. In contrast, Wnt/β-catenin signal transduction requires phosphorylation of Ser/Pro rich sequences present in the Wnt co-receptors LRP5/6, and these motifs inhibit GSK-3 activity. We present crystal structures of GSK-3 bound to its phosphorylated N-terminus and to two of the phosphorylated LRP6 motifs. A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition. The structures rationalize target sequence preferences and suggest avenues for the design of inhibitors selective for a subset of pathways regulated by GSK-3.
Keywords	GSK-3 ; Wnt signaling ; protein kinase ; LRP6 ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2014-03-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: structural Studies of Wnts and identification of an LRP6 binding site.

Chu, Matthew Ling-Hon / Ahn, Victoria E / Choi, Hee-Jung / Daniels, Danette L / Nusse, Roel / Weis, William I

Structure (London, England : 1993)

2013 Volume 21, Issue 7, Page(s) 1235–1242

Abstract: Wnts are secreted growth factors that have critical roles in cell fate determination and stem cell renewal. The Wnt/β-catenin pathway is initiated by binding of a Wnt protein to a Frizzled (Fzd) receptor and a coreceptor, LDL receptor-related protein 5 ... ...

Abstract	Wnts are secreted growth factors that have critical roles in cell fate determination and stem cell renewal. The Wnt/β-catenin pathway is initiated by binding of a Wnt protein to a Frizzled (Fzd) receptor and a coreceptor, LDL receptor-related protein 5 or 6 (LRP5/6). We report the 2.1 Å resolution crystal structure of a Drosophila WntD fragment encompassing the N-terminal domain and the linker that connects it to the C-terminal domain. Differences in the structures of WntD and Xenopus Wnt8, including the positions of a receptor-binding β hairpin and a large solvent-filled cavity in the helical core, indicate conformational plasticity in the N-terminal domain that may be important for Wnt-Frizzled specificity. Structure-based mutational analysis of mouse Wnt3a shows that the linker between the N- and C-terminal domains is required for LRP6 binding. These findings provide important insights into Wnt function and evolution.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; Drosophila Proteins/chemistry ; HEK293 Cells ; Humans ; Hydrogen Bonding ; Intracellular Signaling Peptides and Proteins/chemistry ; Low Density Lipoprotein Receptor-Related Protein-6/chemistry ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; Transcriptional Activation ; Wnt Signaling Pathway ; Wnt3A Protein/chemistry ; Wnt3A Protein/genetics ; Wnt3A Protein/metabolism
Chemical Substances	Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; LRP6 protein, human ; Low Density Lipoprotein Receptor-Related Protein-6 ; Wnt3A Protein ; Wnt3a protein, mouse ; WntD protein, Drosophila
Language	English
Publishing date	2013-06-20
Publishing country	United States
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.
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2013.05.006
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 4141: Show issues

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Article: Structural Basis of Wnt Signaling Inhibition by Dickkopf Binding to LRP5/6

Ahn, Victoria E / Chu, Matthew Ling-Hon / Choi, Hee-Jung / Tran, Denise / Abo, Arie / Weis, William I

Developmental cell. 2011 Nov. 15, v. 21, no. 5

2011

Abstract: LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling. The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats. The first two repeats, LRP6( ... ...

Abstract	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling. The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats. The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts. We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts. Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane. Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
Keywords	X-radiation ; antibodies ; crystal structure ; growth factors ; low density lipoprotein
Language	English
Dates of publication	2011-1115
Size	p. 862-873.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2011.09.003
Database	NAL-Catalogue (AGRICOLA)

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