ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Chitin-induced dimerization activates a plant immune receptor (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-02
    Description: Pattern recognition receptors confer plant resistance to pathogen infection by recognizing the conserved pathogen-associated molecular patterns. The cell surface receptor chitin elicitor receptor kinase 1 of Arabidopsis (AtCERK1) directly binds chitin through its lysine motif (LysM)-containing ectodomain (AtCERK1-ECD) to activate immune responses. The crystal structure that we solved of an AtCERK1-ECD complexed with a chitin pentamer reveals that their interaction is primarily mediated by a LysM and three chitin residues. By acting as a bivalent ligand, a chitin octamer induces AtCERK1-ECD dimerization that is inhibited by shorter chitin oligomers. A mutation attenuating chitin-induced AtCERK1-ECD dimerization or formation of nonproductive AtCERK1 dimer by overexpression of AtCERK1-ECD compromises AtCERK1-mediated signaling in plant cells. Together, our data support the notion that chitin-induced AtCERK1 dimerization is critical for its activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Tingting -- Liu, Zixu -- Song, Chuanjun -- Hu, Yunfei -- Han, Zhifu -- She, Ji -- Fan, Fangfang -- Wang, Jiawei -- Jin, Changwen -- Chang, Junbiao -- Zhou, Jian-Min -- Chai, Jijie -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1160-4. doi: 10.1126/science.1218867.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22654057" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/chemistry/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/immunology/*metabolism ; Arabidopsis Proteins/*chemistry/genetics/*metabolism ; Binding Sites ; Chitin/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Phosphorylation ; Plants, Genetically Modified ; Protein Multimerization ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/*chemistry/genetics/*metabolism ; Receptors, Pattern Recognition/*chemistry/genetics/*metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Structural insight into brassinosteroid perception by BRI1 (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-06-15
    Description: Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019668/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019668/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉She, Ji -- Han, Zhifu -- Kim, Tae-Wuk -- Wang, Jinjing -- Cheng, Wei -- Chang, Junbiao -- Shi, Shuai -- Wang, Jiawei -- Yang, Maojun -- Wang, Zhi-Yong -- Chai, Jijie -- R01 GM066258/GM/NIGMS NIH HHS/ -- R01GM066258/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Jun 12;474(7352):472-6. doi: 10.1038/nature10178.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21666666" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*chemistry/*metabolism ; Arabidopsis Proteins/*chemistry/*metabolism ; Binding Sites ; Brassinosteroids ; Cholestanols/chemistry/*metabolism ; Crystallography, X-Ray ; Enzyme Activation ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Protein Binding ; Protein Folding ; Protein Kinases/*chemistry/*metabolism ; Protein Structure, Tertiary ; Steroids, Heterocyclic/chemistry/*metabolism ; Structure-Activity Relationship ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Electron tunneling in proteins: coupling through a beta strand (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: Electron coupling through a beta strand has been investigated by measurement of the intramolecular electron-transfer (ET) rates in ruthenium-modified derivatives of the beta barrel blue copper protein Pseudomonas aeruginosa azurin. Surface histidines, introduced on the methionine-121 beta strand by mutagenesis, were modified with a Ru(2,2'-bipyridine)2(imidazole)2+ complex. The Cu+ to Ru3+ rate constants yielded a distance-decay constant of 1.1 per angstrom, a value close to the distance-decay constant of 1.0 per angstrom predicted for electron tunneling through an idealized beta strand. Activationless ET rate constants in combination with a tunneling-pathway analysis of the structures of azurin and cytochrome c confirm that there is a generally efficient network for coupling the internal (native) redox center to the surface of both proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langen, R -- Chang, I J -- Germanas, J P -- Richards, J H -- Winkler, J R -- Gray, H B -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1733-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beckman Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792598" target="_blank"〉PubMed〈/a〉
    Keywords: Azurin/*chemistry/metabolism ; Binding Sites ; Cytochrome c Group/*chemistry/metabolism ; *Electron Transport ; Models, Chemical ; Oxidation-Reduction ; *Protein Structure, Secondary ; Pseudomonas aeruginosa ; Ruthenium/metabolism ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Direct roles of SPEECHLESS in the specification of stomatal self-renewing cells (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-09-06
    Description: Lineage-specific stem cells are critical for the production and maintenance of specific cell types and tissues in multicellular organisms. In Arabidopsis, the initiation and proliferation of stomatal lineage cells is controlled by the basic helix-loop-helix transcription factor SPEECHLESS (SPCH). SPCH-driven asymmetric and self-renewing divisions allow flexibility in stomatal production and overall organ growth. How SPCH directs stomatal lineage cell behaviors, however, is unclear. Here, we improved the chromatin immunoprecipitation (ChIP) assay and profiled the genome-wide targets of Arabidopsis SPCH in vivo. We found that SPCH controls key regulators of cell fate and asymmetric cell divisions and modulates responsiveness to peptide and phytohormone-mediated intercellular communication. Our results delineate the molecular pathways that regulate an essential adult stem cell lineage in plants.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390554/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390554/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lau, On Sun -- Davies, Kelli A -- Chang, Jessica -- Adrian, Jessika -- Rowe, Matthew H -- Ballenger, Catherine E -- Bergmann, Dominique C -- 1R01GM086632/GM/NIGMS NIH HHS/ -- 5T32GM007276/GM/NIGMS NIH HHS/ -- R01 GM086632/GM/NIGMS NIH HHS/ -- T32 GM007276/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2014 Sep 26;345(6204):1605-9. doi: 10.1126/science.1256888. Epub 2014 Sep 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Stanford University, Stanford, CA 94305, USA. ; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA. ; Department of Biology, Stanford University, Stanford, CA 94305, USA. Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA. Carnegie Institution for Science, Stanford, CA 94305, USA. dbergmann@stanford.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25190717" target="_blank"〉PubMed〈/a〉
    Keywords: Adult Stem Cells/*cytology ; Arabidopsis/*cytology/genetics/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Basic Helix-Loop-Helix Transcription Factors/genetics/*metabolism ; Binding Sites ; Cell Communication/drug effects/genetics ; Cell Differentiation/drug effects/*genetics ; Cell Division/drug effects/genetics ; Cell Lineage/drug effects/genetics ; Chromatin Immunoprecipitation ; *Gene Expression Regulation, Plant ; Genome, Plant/genetics ; Plant Growth Regulators/pharmacology/physiology ; Plant Stomata/*cytology/genetics/metabolism ; Transcriptome
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Antibodies to purified insulin receptor have insulin-like activity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-16
    Description: Antibodies to insulin receptors purified from rat liver membranes do not complete with [125I]insulin for binding to the insulin receptor but do precipitate solubilized receptors labeled with [125I]insulin. These antibodies have the insulin-like activities of enhancing glucose oxidation and inhibiting epinephrine-induced lipolysis in rat adipocytes. Thus, antibody binds to the receptor at a different site from that to which insulin binds, yet the interaction can initiate an effective biological response. These results indicate that the previously studied insulin-binding sites are the physiological macromolecular receptors for insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, S -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1283-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663609" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthosis Nigricans/physiopathology ; Adipose Tissue/metabolism ; Animals ; *Antibodies ; Antigen-Antibody Reactions ; Binding Sites ; Binding, Competitive ; Biological Transport ; Epinephrine/pharmacology ; Glucose/metabolism ; Insulin/metabolism ; Lipid Mobilization ; Liver/immunology ; Rats ; Receptor, Insulin/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...