Starting New Accreditation Council for Graduate Medical Education (ACGME) Residency Programs in a Teaching Hospital

Starting a new ACGME approved residency program can positively impact patient care, medical education, hospital operations, and the community as whole. This requires a significant amount of commitment, time, and preparation. The initial application and accreditation process should start early and requires a thorough understanding on the ACGME requirements. Building a new residency program involves collaboration among various stakeholders, starting with the teaching hospital, ACGME, and the Center of Medicare and Medicaid services (CMS). It is prudent to also consider the operational and logistical issues such as budget, faculty and administrative staff hire, faculty time for administrative duties, and educational space for faculty and residents. It is vital to recognize how the institution’s strengths and weaknesses match up to these requirements. A robust educational and clinical curriculum in line with ACGME’s core competencies and useful educational collaboration among various programs is critical for effective program. Recruiting and developing the appropriate faculty members is another important aspect for a successful program. The final challenge is recruiting residents that will fit well into the new residency program. Lastly, we discuss the challenges and tips to mitigate the risks of disappointment in the process of starting and creating a flagship residency program

Gaze following in multiagent contexts: Evidence for a quorum-like principle

Research shows that humans spontaneously follow another individual’s gaze. However, little remains known on how they respond when multiple gaze cues diverge across members of a social group. To address this question, we presented participants with displays depicting three (Experiment 1) or five (Experiment 2) agents showing diverging social cues. In a three-person group, one individual looking at the target (33% of the group) was sufficient to elicit gaze-facilitated target responses. With a five-person group, however, three individuals looking at the target (60% of the group) were necessary to produce the same effect. Gaze following in small groups therefore appears to be based on a quorum-like principle, whereby the critical level of social information needed for gaze following is determined by a proportion of consistent social cues scaled as a function of group size. As group size grows, greater agreement is needed to evoke joint attention

Molecular Mechanisms Underlying Skeletal Muscle Weakness in Human Cancer: Reduced Myosin-Actin Cross-Bridge Formation and Kinetics

PHYSICAL FUNCTION DETERIORATES substantially following a diagnosis of cancer (3, 48), and patients view this decline as one of the most distressing side effects of the disease, more so than classic side effects such as pain, nausea, and vomiting (13, 60). Functional disability can be the impetus for dose reduction or cessation of anticancer treatments and predicts chemotherapy toxicity and survival (12, 30, 33, 39). Our current understanding of the factors contributing to reduced functional capacity in patients with cancer is, however, severely limited. Physiological changes that occur within the skeletal muscle of patients with cancer can contribute to functional deterioration and physical disability. The most common adaptations believed to promote functional impairment are muscle atrophy, reduced cardiorespiratory fitness, and skeletal muscle weakness (20, 32, 54). The vast majority of studies of muscle biology in cancer have focused on signal transduction mechanisms underlying skeletal muscle atrophy (20). Understanding quantitative alterations in skeletal muscle and their mechanisms is important because they have relevance for physical function (38) and clinical outcome (18), but functional deficits persist after controlling for muscle atrophy (34, 54), and there is compelling evidence to suggest that cancer has a unique effect on the intrinsic functionality of muscle (22). In other words, a substantial proportion of the decline in physical capacity is likely explained by reductions in function per unit tissue size. Skeletal muscle contractile dysfunction has received minimal attention as a precipitant of functional changes in patients with cancer (54, 61), with the majority of studies being focused on cardiorespiratory fitness (32). However, reduced skeletal muscle contractile function is a strong predictor of decreased physical functioning in common daily activities (49) in many studies rivaling or exceeding the contribution attributed to diminished aerobic capacity (8, 51). Additionally, at a more fundamental level, the properties of the contractile elements (i.e., myofilament proteins) determine the functional character of skeletal muscle and, correspondingly, whole-body performance (24, 28, 29). As the end effectors of muscle contraction, myofilament mechanical properties necessarily set limits for muscle functionality (10). To date, no studies have evaluated the effects of cancer on myofilament protein content, structure, or functionality in humans. The goal of this study was to examine the effect of cancer on skeletal muscle contractile function at the molecular, cellular, whole-muscle, and whole-body levels. To accomplish this objective, we evaluated whole-body and whole-muscle performance using standard functional assessments and cellular/molecular structure and function on intact and chemically skinned fibers from the vastus lateralis muscle in patients with cancer and controls. Because cancer-related functional deficits are suggested to be more common in patients experiencing weight loss and during treatment (i.e., chemo/radiotherapy), we included both cachectic and noncachectic patients and patients undergoing cancer treatment. In this context, our cohort does not permit us to address the unique effect of cancer per se, but instead encompasses the effects of the disease, its treatment, and disease- and treatment-related sequelae such as weight loss. However, when discussing our findings, we refer to the effects of cancer for simplicity

New sandwich and half-sandwich titanium hydrazido compounds

[EN] New mono- and bis-cyclopentadienyl terminal titanium hydrazido(2-) compounds were prepared by tert-butyl imide/N,N'-disubstituted hydrazine exchange reactions. Reaction of Cp*Ti(N(t)Bu)Cl(PY) (1) with Ph(2)NNH(2) gave the terminal hydrazide Cp*Ti(NNPh(2))Cl(py) (4), whereas the corresponding reaction of CpTi(N(t)Bu)Cl(py) gave the dimer Cp(2)Ti(2)(mu-eta(1):eta(1)-NNPh(2))-(mu-eta(2):eta(1)-NNPh(2))Cl(2). Reaction of 1 with Me(2)NNH(2) (1 equiv) also gave a dimer, Cp*(2)Ti(2)(mu-eta(1):eta(1)-NNMe(2)) (mu-eta(2):eta(1)-NNMe(2))Cl(2), (8), while the reaction with 2 equiv of Me(2)NNH(2) gave Cp*Ti(eta(2)-NHNMe(2))(2)Cl (7) containing two eta(2)-bound hydrazide(1-) ligands. Formation of 7 and 8 proceeds via a common intermediate, Cp*Ti(NH(t)Bu)(eta(2)-NHNMe(2))Cl, observed by NMR spectroscopy. Reaction of 4 with LiNHNPh(2) gave the mixed hydrazide(2-)/hydrazide(1-) derivative Cp*Ti(NNPh(2))-(NHNPh(2))(py) (10). The corresponding reaction of 1 formed Cp*Ti(N(t)Bu)(NHNPh(2))(py), which rearranged to Cp*Ti-(NH(t)Bu)(NNPh(2))(py). The titanocene derivative Cp(2)Ti(NNPh(2))(py) (14) was prepared by reaction of Cp(2)Ti(N(t)Bu)(py) (13) with Ph(2)NNH(2), whereas the corresponding reaction with Me(2)NNH(2) gave mixtures including CpTi(NH(t)Bu)(mu-eta(1):eta(1)-NNMe(2)) (mu-eta(2):eta(1)-NNMe(2))TiCp(eta(1)-Cp). The electronic structure of 14 was investigated by DFT and compared to that of the imido complex 13. Whereas the HOMO of the formally 20 valence electron compound 13 is a ligand-centered orbital based both on the Cp rings and on the imido N, in 14 this is the HOMO-1 and one of the Ti=-N(alpha)pi-bonding MOs is the HOMO, destabilized by an N(alpha)-N(beta) antibonding interaction.We thank the EPSRC, British Council, MESR, and the Spanish Ministerio de Educacion y Ciencia for support. We thank Andrew Cowley for help with some of the X-ray structures.Selby, JD.; Feliz Rodriguez, M.; Schwarz, AD.; Clot, E.; Mountford, P. (2011). New sandwich and half-sandwich titanium hydrazido compounds. Organometallics. 30:2295-2307. doi:10.1021/om200068kS229523073