Spectroscopic properties and electronic structures of 17-electron half-sandwich ruthenium acetylide complexes, [Ru(CCAr)(L2)Cp′]+ (Ar=phenyl, p-tolyl, 1-naphthyl, 9-anthryl; L2=(PPh3)2, Cp′=Cp; L2=dppe; Cp′=Cp∗)

A series of half-sandwich bis(phosphine) ruthenium acetylide complexes [Ru(C CAr)(L-2)Cp'] (Ar = phenyl, p-tolyl, 1-naphthyl, 9-anthryl; L2 = (PPh3)(2), Cp' = Cp; L-2 = dppe; Cp' = Cp*) have been examined using electrochemical and spectroelectrochemical methods. One-electron oxidation of these complexes gave the corresponding radical cations [Ru(C CAr)(L2)Cp'](+). Those cations based on Ru(dppe)Cp*, or which feature a para-tolyl acetylide substituent, are more chemically robust than examples featuring the Ru(PPh3)(2)Cp moiety, permitting good quality UV-Vis-NIR and IR spectroscopic data to be obtained using spectroelectrochemical methods. On the basis of TD DFT calculations, the low energy (NIR) absorption bands in the experimental electronic spectra for most of these radical cations are assigned to transitions between the beta-HOSO and beta-LUSO, both of which have appreciable metal d and ethynyl pi character. However, the large contribution from the anthryl moiety to the frontier orbitals of [Ru(C CC14H9)(L2)CP'](+) suggests compounds containing this moiety should be described as metal-stabilised anthryl radical cations.

Na 1 Nachlass Max Horkheimer, 2 - Korrespondenzen u.a. an Raymond Aron (p. I 1, 206-333)

16 Briefe zwischen Ruth Nanda Anshen und Max Horkheimer, 1938-1941; 5 Briefe zwischen Peter Appel und Max Horkheimer, 1937; 1 Drucksache der Arbeitsgemeinschaft Sozialistischer Ärzte in Hessen, Juli 1949; 1 Brief der Arbeitsgemeinschaft für Soziale Betriebsgestaltung in Heidelberg an Max Horkheimer, 18.10.1949; 2 Briefe zwischen Lois Archer und Max Horkheimer, 24.07.1947, 04.08.1947; 2 Briefe zwischen Camille Arnaud und Max Horkheimer, 03.03.1946, 22.03.1946; 39 Briefe zwischen Raymond Aron und Max Horkheimer, 1935-1938; 2 Briefe zwischen Ruth Arrau und Max Horkheimer, 28.06.1949, 10.10.1949; 3 Briefe zwischen S. Aufhauser und Max Horkheimer, 1939-1941, 16.04.1941; 8 Briefe zwischen der Zeitschrift 'Aufbau' und Max Horkheimer, 1944-1944; 3 Briefe zwischen der Automobile Club of New York und Max Horkheimer, 1937, 10.08.1937;

Na 1 Nachlass Max Horkheimer, 60 - Korrespondenzen u.a. mit der American Friends Service Committee (p. II 1, 226-453)

1 Brief von Max Horkheimer an die Commerzbank Stuttgart, 1947; 2 Briefe von Max Horkheimer an die United States Lines, 1946-1947; 4 Brief und Beilage von Max Horkheimer an das American Consulate General Stuttgart, 1940-1941, 1946; 1 Brief von Max Horkheimer an das Hebrew Sheltering and Immigrant Aid, 1946; 1 Brief von Max Horkheimer an Lilly Straus, 1945; 2 Briefe von Max Horkheimer an Herbert S. Eskin, 1945; 3 Briefe von Max Horkheimer an State of New York, 1939-1941; 5 Briefe von Max Horkheimer an das American Friends Service Committee, 1940-1941; 2 Briefe von Max Horkheimer an Elisabeth Kunz, 1941;

Na 1 Nachlass Max Horkheimer, 500 - Korrespondenzen mit Theodor W. Adorno (p. VI 1, 1 - 121)

Briefwechsel zwischen Max Horkheimer und Theodor W. Adorno und Gretel Adorno, 1927 - 1938; 1 Brief (Kopie) von Henri Bergson an Theodor W. Adorno, 1935;

Na 1 Nachlass Max Horkheimer, 501 - Korrespondenzen von Theodor W. Adorno (p. VI 1, 122 - 268)

Briefwechsel zwischen Max Horkheimer und Theodor W. Adorno und Gretel Adorno, 1927 - 1938; 1 Brief vom United States of America General Consulat in London an Theodor W. Adorno, 1937; 1 Brief von Theodor W. Adorno an Frau Sing, 1937; 1 Brief von Theodor W. Adorno an ... Kluthe, 1937; 1 Brief von Theodor W. Adorno an ... Wolfenstein, 1937; 2 Briefe von Theodor W. Adorno und Max Horkheimer an Ernst Krenek, 1937; 1 Brief von Ernst Krenek an Max Horkheimer, 1937; 1 Brief von Paul Oppenheim an Max Horkheimer, 1937; 2 Briefe von Oscar und Maria Wiesengrund an Max Horkheimer, 1937; 1 Brief von Theodor W. Adorno an Siegfried Kracauer, 1937;

Na 1 Nachlass Max Horkheimer, 502 - Korrespondenzen mit Theodor W. Adorno (p. VI 1, 269 - 366; VI 1 A, 1 - 55)

Briefwechsel zwischen Max Horkheimer und Theodor W. Adorno, 1927 - 1938; 1 Brief von Theodor W. Adorno an Hans F. Redlich, 1938; 1 Brief von Max Horkheimer an United States of America General Consul in Stuttgart, 1938; 1 Brief von Rudolph Kolisch an Theodor W. Adorno, 1938; 1 Brief von Paul F. Lazarsfeld an Theodor W. Adorno, 1938; 2 Briefe von Theodor W. Adorno an Paul F. Lazarsfeld, 1938; 1 Brief von Hanna Maaß an Gretel Adorno, 1937; Briefwechsel und Beilagen zwischen Max Horkheimer, Theodor W. Adorno und Gretel Adorno, 1939 - 1940; 1 Brief (Entwurf) von Theodor W. Adorno an Robert M. Hutchins, 1940; 4 Briefe von Friedrich Pollock an Theodor W. Adorno, 1940; 2 Briefe von Margot von Mendelssohn an Theodor W. Adorno, 1940; 2 Briefe von Theodor W. Adorno an Margot von Mendelssohn, 1940; 1 Brief von Franz L. Neumann an Theodor W. Adorno, 1940; 1 Brief (Entwurf von T.W. Adorno) von Max Horkheimer an Mrs. Charles E. Mitchell, 1940; 1 Brief und Beilage von Gretel Adorno an Frederick Wild, 1939; 1 Brief von French und Co. Eifert an Gretel Adorno, 1939; 2 Briefe von Theodor W. Adorno an Herbert W. Schneider, 1939; 1 Brief von Theodor W. Adorno an Jean Wahl, 1939; 1 Brief von Max Horkheimer an Roger M. Howson von der Columbia University Library in New York, 1939;

Na 1 Nachlass Max Horkheimer, 604 - Vorlesung Wintersemester 1925/26: "Geschichte der deutschen idealistischen Philosophie von Kant bis Hegel" (p. VIII 1, 1)

Vorlesungsskript, mit einer später verfaßten Einleitung, Typoskript mit eigenhändigen Korrekturen, 178 Blatt;

Na 1 Nachlass Max Horkheimer, 605 - Weitere Unterlagen betreffs der Vorlesung "Geschichte der deutschen idealistischen Philosophie von Kant bis Hegel" (p. VIII 1, 2-6)

Teilstücke aus Vorlesung, Typoskript, 58 Blatt; Teilstücke aus Vorlesung, Typoskript, 94 Blatt; Teilstücke aus Vorlesung, Typoskript, 16 Blatt; Eigenhändige Notizen zur Vorlesung, 10 Blatt; Kollegheft zur Vorlesung Max Horkheimers, Autor unbekannt, 15 Blatt;

Ms. lat. oct. 148 - In Thomae de Aquino Summam theologiae, P. II., 1.

Vorbesitzer: Johannes Bartholomaei;

Ms. lat. oct. 155 - In Thomae de Aquino Summam theologiae, P. II. 1

Vorbesitzer: Bernhard Diell;

A substance P (neurokinin-1) receptor mutant carboxyl-terminally truncated to resemble a naturally occurring receptor isoform displays enhanced responsiveness and resistance to desensitization

Two isoforms of the substance P (SP) receptor, differing in the length of the cytoplasmic carboxyl-terminus by ≈8 kDa, have been detected previously in rat salivary glands and other tissues. The binding and functional properties of these two isoforms have been investigated using full-length (407 amino acids) and carboxyl-terminally truncated (324 amino acids) rat SP receptors transfected stably into Chinese hamster ovary cells. Both the full-length and the truncated receptor bound radiolabeled SP with a similar Kd (≈0.1 nM). The average number of high affinity SP binding sites per cell was 1.0 × 105 and 0.3 × 105 for the full-length and the truncated SP receptor, respectively. In both cell lines, SP induced a rapid but transient increase in cytosolic calcium concentration ([Ca2+]i), which consisted of the release of Ca2+ from intracellular stores and the influx of extracellular Ca2+. Both components are dependent on phospholipase C activation. Although the full-length and the truncated receptor utilize the same calcium pathways, they differ in their EC50 values (0.28 nM for the full-length; 0.07 nM for the truncated). These differences in responsiveness may be related to the observed differences in receptor desensitization. The truncated receptor, in contrast to the full-length receptor, does not undergo rapid and long-lasting desensitization. Cells possessing the short isoform of the SP receptor would thus be expected to exhibit a prolonged responsiveness.

Interleukin 12 and B7-1 costimulatory molecule expressed by an adenovirus vector act synergistically to facilitate tumor regression

Stimulation of antitumor immune mechanisms is the primary goal of cancer immunotherapy, and accumulating evidence suggests that effective alteration of the host–tumor relationship involves immunomodulating cytokines and also the presence of costimulatory molecules. To examine the antitumor effect of direct in vivo gene transfer of murine interleukin 12 (IL-12) and B7-1 into tumors, we developed an adenovirus (Ad) vector, AdIL12–B7-1, that encodes the two IL-12 subunits in early region 1 (E1) and the B7-1 gene in E3 under control of the murine cytomegalovirus promoter. This vector expressed high levels of IL-12 and B7-1 in infected murine and human cell lines and in primary murine tumor cells. In mice bearing tumors derived from a transgenic mouse mammary adenocarcinoma, a single intratumoral injection with a low dose (2.5 × 107 pfu/mouse) of AdIL12–B7-1 mediated complete regression in 70% of treated animals. By contrast, administration of a similar dose of recombinant virus encoding IL-12 or B7-1 alone resulted in only a delay in tumor growth. Interestingly, coinjection of two different viruses expressing either IL-12 or B7-1 induced complete tumor regression in only 30% of animals treated at this dose. Significantly, cured animals remained tumor free after rechallenge with fresh tumor cells, suggesting that protective immunity had been induced by treatment with AdIL12–B7-1. These results support the use of Ad vectors as a highly efficient delivery system for synergistically acting molecules and show that the combination of IL-12 and B7-1 within a single Ad vector might be a promising approach for in vivo cancer therapy.

HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling

Mutant presenilins have been found to cause Alzheimer disease. Here, we describe the identification and characterization of HOP-1, a Caenorhabditis elegans presenilin that displays much more lower sequence identity with human presenilins than does the other C. elegans presenilin, SEL-12. Despite considerable divergence, HOP-1 appears to be a bona fide presenilin, because HOP-1 can rescue the egg-laying defect caused by mutations in sel-12 when hop-1 is expressed under the control of sel-12 regulatory sequences. HOP-1 also has the essential topological characteristics of the other presenilins. Reducing hop-1 activity in a sel-12 mutant background causes synthetic lethality and terminal phenotypes associated with reducing the function of the C. elegans lin-12 and glp-1 genes. These observations suggest that hop-1 is functionally redundant with sel-12 and underscore the intimate connection between presenilin activity and LIN-12/Notch activity inferred from genetic studies in C. elegans and mammals.

Reverse genetic analysis of Caenorhabditis elegans presenilins reveals redundant but unequal roles for sel-12 and hop-1 in Notch-pathway signaling

Mutations in the human presenilin genes PS1 and PS2 cause early-onset Alzheimer’s disease. Studies in Caenorhabditis elegans and in mice indicate that one function of presenilin genes is to facilitate Notch-pathway signaling. Notably, mutations in the C. elegans presenilin gene sel-12 reduce signaling through an activated version of the Notch receptor LIN-12. To investigate the function of a second C. elegans presenilin gene hop-1 and to examine possible genetic interactions between hop-1 and sel-12, we used a reverse genetic strategy to isolate deletion alleles of both loci. Animals bearing both hop-1 and sel-12 deletions displayed new phenotypes not observed in animals bearing either single deletion. These new phenotypes—germ-line proliferation defects, maternal-effect embryonic lethality, and somatic gonad defects—resemble those resulting from a reduction in signaling through the C. elegans Notch receptors GLP-1 and LIN-12. Thus SEL-12 and HOP-1 appear to function redundantly in promoting Notch-pathway signaling. Phenotypic analyses of hop-1 and sel-12 single and double mutant animals suggest that sel-12 provides more presenilin function than does hop-1.

The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond.

Substance P (SP) is a neuropeptide that mediates multiple physiological responses including transmission of painful stimuli and inflammation via an interaction with a receptor of known primary sequence. To identify the regions of the SP receptor, also termed the NK-1 receptor, involved in peptide recognition, we are using analogues of SP containing the photoreactive amino acid p-benzoyl-L-phenylalanine (Bpa). In the present study, we used radioiodinated Bpa8-SP to covalently label with high efficiency the rat SP receptor expressed in a transfected mammalian cell line. To identify the amino acid residue that serves as the site of covalent attachment, a membrane preparation of labeled receptor was subjected to partial enzymatic cleavage by trypsin. A major digestion product of 22 kDa was identified. Upon reduction with 2-mercaptoethanol the mass of this product decreased to 14 kDa. The 22-kDa tryptic fragment was purified in excellent yield by preparative SDS/PAGE under nonreducing conditions. Subcleavage with Staphylococcus aureus V8 protease and endoproteinase ArgC yielded fragments of 8.2 and 9.0 kDa, respectively. Upon reductive cleavage, the V8 protease fragment decreased to 3.0 kDa while the endoproteinase ArgC fragment decreased to 3.2 kDa. Taking into consideration enzyme specificity, molecular size, determination of the presence or absence of N-glycosylation sites, and recognition by antibodies to specific sequences of the SP receptor, the V8 protease fragment is Thr-173 to Glu-183, while the endoproteinase ArgC fragment is Val-178 to Arg-190. These two fragments share the common sequence Val-Val-Cys-Met-Ile-Glu (residues 178-183). The site of covalent attachment of radioiodinated Bpa8-SP is thus restricted to a residue within this overlap sequence. The data presented here also establish that the cysteine residue in this sequence Cys-180, which is positioned in the middle of the second extracellular loop, participates in a disulfide bond that links the first and second extracellular loops of the receptor.