Reactions of isonitriles with [Fe₃(CO)₁₂] and [Ru₃(CO)₁₂] monitored by electrospray mass spectrometry: structural characterisation of [Fe₃(CO)₁₀(CNPh)₂] and [Ru₄(CO)₁₁(μ₃-η²-CNPh)₂(CNPh)]

The reactions of [Fe₃(CO)₁₂] or [Ru₃(CO) ₁₂] with RNC (R=Ph, C₆H₄OMe-p or CH₂SO₂C₆H₄Me-p) have been investigated using electrospray mass spectrometry. Species arising from substitution of up to six ligands were detected for [Fe₃(CO)₁₂], but the higher-substituted compounds were too unstable to be isolated. The crystal structure of [Fe₃(CO)₁₀(CNPh)₂] was determined at 150 and 298 K to show that both isonitrile ligands were trans to each other on the same Fe atom. For [Ru₃(CO)₁₂] substitution of up to three COs was found, together with the formation of higher-nuclearity clusters. [Ru₄(CO)₁₁(CNPh)₃] was structurally characterised and has a spiked-triangular Ru₄ core with two of the CNPh ligands coordinated in an unusual μ₃-η² mode. The substitution reactions of [M₃(CO)₁₂] by RNC have been investigated by electrospray mass spectrometry showing up to six COs can be replaced. [Fe₃(CO)₁₀(CNPh)₂] has both PhNC axially on the same Fe atom, and [Ru₄(CO)₁₁(μ₃-η²-CNPh)₂(CNPh)] has a spiked-triangular cluster core with two PhNC ligands in an unusual coordination mode

Platinum(II), palladium(II), nickel(II), and gold(I) complexes of the “electrospray-friendly” thiolate ligands 4-SC₅H₄N- and 4-SC₆H₄OMe-

The series of platinum(II), palladium(II), and nickel(II) complexes [ML₂(dppe)] [M = Ni, Pd, Pt; L = 4-SC₅H₄N or 4-SC₆H₄OMe; dppe = Ph₂PCH₂CH₂PPh₂] containing pyridine-4-thiolate or 4-methoxybenzenethiolate ligands, together with the corresponding gold(I) complexes [AuL(PPh3)], were prepared and their electrospray ionization mass spectrometric behavior compared with that of the thiophenolate complexes [M(SPh)₂(dppe)] (M = Ni, Pd, Pt) and [Au(SPh)(PPh₃)]. While the pyridine-4-thiolate complexes yielded protonated ions of the type [M + H]+ and [M + 2H]²+ ions in the Ni, Pd, and Pt complexes, an [M + H]+ ion was only observed for the platinum derivative of 4-methoxybenzenethiolate. Other ions, which dominated the spectra of the thiophenolate complexes, were formed by thiolate loss and aggregate formation. The X-ray crystal structure of [Pt(SC₆H₄OMe-4)₂(dppe)] is also reported

Immobilization of [Pt 2(μ-S) 2(PPh 3)4] on polymeric supports by sulfide alkylation and phosphine exchange reactions

10.1080/10426507.2012.761990Phosphorus, Sulfur and Silicon and the Related Elements188111508-1525PSSL

AIMp1 Potentiates TH1 Polarization and Is Critical for Effective Antitumor and Antiviral Immunity

Dendritic cells (DCs) must integrate a broad array of environmental cues to exact control over downstream immune responses including TH polarization. The multienzyme aminoacyl-tRNA synthetase complex component AIMp1/p43 responds to cellular stress and exerts pro-inflammatory functions; however, a role for DC-expressed AIMp1 in TH polarization has not previously been shown. Here, we demonstrate that the absence of AIMp1 in bone marrow-derived DC (BMDC) significantly impairs cytokine and costimulatory molecule expression, p38 MAPK signaling, and TH1 polarization of cocultured T-cells while significantly dysregulating immune-related gene expression. These deficits resulted in significantly compromised BMDC vaccine-mediated protection against melanoma. AIMp1 within the host was also critical for innate and adaptive antiviral immunity against influenza virus infection in vivo. Cancer patients with AIMp1 expression levels in the highest tertiles exhibited a 70% survival advantage at 15-year postdiagnosis as determined by bioinformatics analysis of nearly 9,000 primary human tumor samples in The Cancer Genome Atlas database. These data establish the importance of AIMp1 for the effective governance of antitumor and antiviral immune responses

AIMp1 Potentiates TH1 Polarization and Is Critical for Effective Antitumor and Antiviral Immunity

Dendritic cells (DCs) must integrate a broad array of environmental cues to exact control over downstream immune responses including TH polarization. The multienzyme aminoacyl-tRNA synthetase complex component AIMp1/p43 responds to cellular stress and exerts pro-inflammatory functions; however, a role for DC-expressed AIMp1 in TH polarization has not previously been shown. Here, we demonstrate that the absence of AIMp1 in bone marrow-derived DC (BMDC) significantly impairs cytokine and costimulatory molecule expression, p38 MAPK signaling, and TH1 polarization of cocultured T-cells while significantly dysregulating immune-related gene expression. These deficits resulted in significantly compromised BMDC vaccine-mediated protection against melanoma. AIMp1 within the host was also critical for innate and adaptive antiviral immunity against influenza virus infection in vivo. Cancer patients with AIMp1 expression levels in the highest tertiles exhibited a 70% survival advantage at 15-year postdiagnosis as determined by bioinformatics analysis of nearly 9,000 primary human tumor samples in The Cancer Genome Atlas database. These data establish the importance of AIMp1 for the effective governance of antitumor and antiviral immune responses