(%)/total no.(%), if otherwise stated. Percentages are based on patients with complete information in the respective categories. * Two patients missed the detailed information in maternal outcomes. Neonatal outcomes were unknown in four cases. ** One patient missed the detailed information in maternal outcomes. Neonatal outcomes were unknown in two cases.  A scientometric analysis of Indian research output in medicine during 1999–2008 OBJECTIVE: This study analyzes the research activities of India in medicine during 1999–2008, based on the total publication output, its growth rate, quality of papers published and rank of India in the global context. Patterns of international collaborative research output and the major partner countries of India are also discussed. This study also evaluates the research performance of different types of Indian medical colleges, hospitals, research institutes, universities and research foundations and the characteristics of published literature in Indian and foreign journals. It also analyzes the medical research output by disease and organs. MATERIALS AND METHODS: The publication data on medicine has been retrieved by using SCOPUS database. RESULTS: India holds 12th rank among the productive countries in medicine research consisting of 65,745 papers with a global publication share of 1.59% and registering a growth rate of 76.68% for the papers published during 1999–2003 to 2004–2008. CONCLUSION: High quality research in India is grossly inadequate and requires strategic planning, investment and resource support. There is also a need to improve the existing medical education system, which should foster research culture.  Membrane Fusion and Cell Entry of XMRV Are pH-Independent and Modulated by the Envelope Glycoprotein's Cytoplasmic Tail Xenotropic murine leukemia virus-related virus (XMRV) is a gammaretrovirus that was originally identified from human prostate cancer patients and subsequently linked to chronic fatigue syndrome. Recent studies showed that XMRV is a recombinant mouse retrovirus; hence, its association with human diseases has become questionable. Here, we demonstrated that XMRV envelope (Env)-mediated pseudoviral infection is not blocked by lysosomotropic agents and cellular protease inhibitors, suggesting that XMRV entry is not pH-dependent. The full length XMRV Env was unable to induce syncytia formation and cell-cell fusion, even in cells overexpressing the viral receptor, XPR1. However, truncation of the C-terminal 21 or 33 amino acid residues in the cytoplasmic tail (CT) of XMRV Env induced substantial membrane fusion, not only in the permissive 293 cells but also in the nonpermissive CHO cells that lack a functional XPR1 receptor. The increased fusion activities of these truncations correlated with their enhanced SU shedding into culture media, suggesting conformational changes in the ectodomain of XMRV Env. Noticeably, further truncation of the CT of XMRV Env proximal to the membrane-spanning domain severely impaired the Env fusogenicity, as well as dramatically decreased the Env incorporations into MoMLV oncoretroviral and HIV-1 lentiviral vectors resulting in greatly reduced viral transductions. Collectively, our studies reveal that XMRV entry does not require a low pH or low pH-dependent host proteases, and that the cytoplasmic tail of XMRV Env critically modulates membrane fusion and cell entry. Our data also imply that additional cellular factors besides XPR1 are likely to be involved in XMRV entry. Enveloped viruses must fuse with host cell membranes in order to gain entry and initiate infection. For retroviruses, this process is mediated by the envelope glycoprotein (Env) acquired from the viral producer cells. The Env is initially synthesized as a precursor in the endoplasmic reticulum (ER) and subsequently cleaved by cellular proteases in the trans-Golgi complex into the surface (SU) and transmembrane (TM) subunits [1] . The SU subunit contains a receptor binding domain (RBD) that is responsible for interactions with specific cellular receptors or coreceptors, and the TM subunit possesses a fusion peptide, two heptad repeats (HRs), a membranespanning domain (MSD), and a cytoplasmic tail (CT), all of which have been shown to control or regulate membrane fusion [2] . Upon proper triggering, the TM subunit undergoes a large scale conformational rearrangement, leading to the formation of a stable helix bundle (6-HB) that drives fusion between the viral and cellular membranes [3] .